NCBI Conserved Domain Search

Conserved domains on [gi|578809569|ref|XP_006714455|]

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3-oxoacyl-[acyl-carrier-protein] reductase isoform X4 [Homo sapiens]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

NADB_Rossmann super family

cl21454

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...

3-188

3.95e-63

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.

The actual alignment was detected with superfamily member cd05333:

Pssm-ID: 473865 [Multi-domain] Cd Length: 240 Bit Score: 195.46 E-value: 3.95e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVeeiKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:cd05333   81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINIS----------SVVGLIGNPGQANYA 150

                        170       180
                 ....*....|....*....|....*....
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05333  151 ASKAGVIGFTKSLAKELASRGITVNAVAP 179

Name

Accession

Description

Interval

E-value

BKR_SDR_c

cd05333

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...

3-188

3.95e-63

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187594 [Multi-domain] Cd Length: 240 Bit Score: 195.46 E-value: 3.95e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVeeiKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:cd05333   81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINIS----------SVVGLIGNPGQANYA 150

                        170       180
                 ....*....|....*....|....*....
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05333  151 ASKAGVIGFTKSLAKELASRGITVNAVAP 179

FabG

COG1028

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...

1-191

3.36e-62

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis

Pssm-ID: 440651 [Multi-domain] Cd Length: 249 Bit Score: 193.46 E-value: 3.36e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:COG1028    5 KGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELraaGGRALAVAADVTDEAAVEALVAAAVAAFGRL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:COG1028   85 DILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNIS----------SIAGLRGSPGQAA 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 578809569 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:COG1028  155 YAASKAAVVGLTRSLALELAPRGIRVNAVAPGPI 188

fabG

PRK05653

3-oxoacyl-ACP reductase FabG;

1-188

1.58e-61

3-oxoacyl-ACP reductase FabG;

Pssm-ID: 235546 [Multi-domain] Cd Length: 246 Bit Score: 191.53 E-value: 1.58e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK05653   4 QGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELraaGGEARVLVFDVSDEAAVRALIEAAVEAFGAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK05653  84 DILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNIS----------SVSGVTGNPGQTN 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809569 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK05653 154 YSAAKAGVIGFTKALALELASRGITVNAVAP 184

adh_short

pfam00106

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.

3-188

7.86e-56

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.

Pssm-ID: 395056 [Multi-domain] Cd Length: 195 Bit Score: 175.49 E-value: 7.86e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569    3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAkelGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNIS----------SVAGLVPYPGGSAYS 150

                         170       180
                  ....*....|....*....|....*....
gi 578809569  160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:pfam00106 151 ASKAAVIGFTRSLALELAPHGIRVNAVAP 179

PKS_KR

smart00822

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...

9-111

1.03e-10

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.

Pssm-ID: 214833 [Multi-domain] Cd Length: 180 Bit Score: 57.88 E-value: 1.03e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569     9 GGSRGIGRAVAQLMARKGYR-LAVIARNLEGAKAAA------GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:smart00822   7 GGLGGLGRALARWLAERGARrLVLLSRSGPDAPGAAallaelEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLTGVI 86

                           90       100       110
                   ....*....|....*....|....*....|
gi 578809569    82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGS 111
Cdd:smart00822  87 HAAGVLDDGVLASLTPERFAAVLAPKAAGA 116

sepiapter_red

TIGR01500

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...

4-188

1.69e-08

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.

Pssm-ID: 273660 [Multi-domain] Cd Length: 256 Bit Score: 52.99 E-value: 1.69e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569    4 VCAVFGGSRGIGRAVAQLMAR----KGYRLAVIARNLEGAKAAAGDLGGDHLA-----FSCDVAKEHDVQNTFEELEKhL 74
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKclksPGSVLVLSARNDEALRQLKAEIGAERSGlrvvrVSLDLGAEAGLEQLLKALRE-L 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   75 GRVNFLVNAAGINRDGLLVRT-KTEDMVSQL-------HTNLLGSMLTCKAAMRTMIQQQGG--SIVNVGhrremllhkr 144
Cdd:TIGR01500  81 PRPKGLQRLLLINNAGTLGDVsKGFVDLSDStqvqnywALNLTSMLCLTSSVLKAFKDSPGLnrTVVNIS---------- 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578809569  145 SIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:TIGR01500 151 SLCAIQPFKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAP 194

Name

Accession

Description

Interval

E-value

BKR_SDR_c

cd05333

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...

3-188

3.95e-63

Pssm-ID: 187594 [Multi-domain] Cd Length: 240 Bit Score: 195.46 E-value: 3.95e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVeeiKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:cd05333   81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINIS----------SVVGLIGNPGQANYA 150

                        170       180
                 ....*....|....*....|....*....
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05333  151 ASKAGVIGFTKSLAKELASRGITVNAVAP 179

SDR_c

cd05233

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...

5-191

9.69e-63

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 212491 [Multi-domain] Cd Length: 234 Bit Score: 194.42 E-value: 9.69e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   5 CAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG--DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAieALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:cd05233   81 NAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNIS----------SVAGLRPLPGQAAYAASK 150

                        170       180
                 ....*....|....*....|....*....
gi 578809569 163 GGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:cd05233  151 AALEGLTRSLALELAPYGIRVNAVAPGLV 179

FabG

COG1028

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...

1-191

3.36e-62

Pssm-ID: 440651 [Multi-domain] Cd Length: 249 Bit Score: 193.46 E-value: 3.36e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:COG1028    5 KGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELraaGGRALAVAADVTDEAAVEALVAAAVAAFGRL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:COG1028   85 DILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNIS----------SIAGLRGSPGQAA 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 578809569 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:COG1028  155 YAASKAAVVGLTRSLALELAPRGIRVNAVAPGPI 188

fabG

PRK05653

3-oxoacyl-ACP reductase FabG;

1-188

1.58e-61

3-oxoacyl-ACP reductase FabG;

Pssm-ID: 235546 [Multi-domain] Cd Length: 246 Bit Score: 191.53 E-value: 1.58e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK05653   4 QGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELraaGGEARVLVFDVSDEAAVRALIEAAVEAFGAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK05653  84 DILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNIS----------SVSGVTGNPGQTN 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809569 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK05653 154 YSAAKAGVIGFTKALALELASRGITVNAVAP 184

fabG

PRK05557

3-ketoacyl-(acyl-carrier-protein) reductase; Validated

1-188

2.17e-56

3-ketoacyl-(acyl-carrier-protein) reductase; Validated

Pssm-ID: 235500 [Multi-domain] Cd Length: 248 Bit Score: 178.46 E-value: 2.17e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK05557   4 EGKVALVTGASRGIGRAIAERLAAQGANVVInYASSEAGAEALVaeiGALGGKALAVQGDVSDAESVERAVDEAKAEFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:PRK05557  84 VDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINIS----------SVVGLMGNPGQA 153

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK05557 154 NYAASKAGVIGFTKSLARELASRGITVNAVAP 185

YdfG

COG4221

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...

2-188

6.85e-56

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation

Pssm-ID: 443365 [Multi-domain] Cd Length: 240 Bit Score: 176.91 E-value: 6.85e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:COG4221    5 GKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDVLV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSAS 161
Cdd:COG4221   85 NNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNIS----------SIAGLRPYPGGAVYAAT 154

                        170       180
                 ....*....|....*....|....*..
gi 578809569 162 KGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:COG4221  155 KAAVRGLSESLRAELRPTGIRVTVIEP 181

adh_short

pfam00106

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.

3-188

7.86e-56

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.

Pssm-ID: 395056 [Multi-domain] Cd Length: 195 Bit Score: 175.49 E-value: 7.86e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569    3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAkelGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNIS----------SVAGLVPYPGGSAYS 150

                         170       180
                  ....*....|....*....|....*....
gi 578809569  160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:pfam00106 151 ASKAAVIGFTRSLALELAPHGIRVNAVAP 179

YqjQ

COG0300

Short-chain dehydrogenase [General function prediction only];

1-188

3.59e-54

Short-chain dehydrogenase [General function prediction only];

Pssm-ID: 440069 [Multi-domain] Cd Length: 252 Bit Score: 173.13 E-value: 3.59e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:COG0300    4 TGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELraaGARVEVVALDVTDPDAVAALAEAVLARFGPI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:COG0300   84 DVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVS----------SVAGLRGLPGMAA 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809569 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:COG0300  154 YAASKAALEGFSESLRAELAPTGVRVTAVCP 184

fabG

PRK12825

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

1-188

3.43e-49

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

Pssm-ID: 237218 [Multi-domain] Cd Length: 249 Bit Score: 160.42 E-value: 3.43e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIAR-NLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK12825   5 MGRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEaveALGRRAQAVQADVTDKAALEAAVAAAVERFGR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:PRK12825  85 IDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNIS----------SVAGLPGWPGRS 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12825 155 NYAAAKAGLVGLTKALARELAEYGITVNMVAP 186

fabG

PRK05565

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

1-188

3.98e-48

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

Pssm-ID: 235506 [Multi-domain] Cd Length: 247 Bit Score: 157.31 E-value: 3.98e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVI-ARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK05565   4 MGKVAIVTGASGGIGRAIAELLAKEGAKVVIAyDINEEAAQELLeeiKEEGGDAIAVKADVSSEEDVENLVEQIVEKFGK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:PRK05565  84 IDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNIS----------SIWGLIGASCEV 153

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK05565 154 LYSASKGAVNAFTKALAKELAPSGIRVNAVAP 185

PRK12826

SDR family oxidoreductase;

1-188

7.69e-44

SDR family oxidoreductase;

Pssm-ID: 183775 [Multi-domain] Cd Length: 251 Bit Score: 146.60 E-value: 7.69e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK12826   5 EGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVeaaGGKARARQVDVRDRAALKAAVAAGVEDFGRL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGL-KGNSGQS 156
Cdd:PRK12826  85 DILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTS----------SVAGPrVGYPGLA 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12826 155 HYAASKAGLVGFTRALALELAARNITVNSVHP 186

adh_short_C2

pfam13561

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...

12-188

8.63e-44

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.

Pssm-ID: 433310 [Multi-domain] Cd Length: 236 Bit Score: 146.04 E-value: 8.63e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   12 RGIGRAVAQLMARKGYRLAVIARNLEGAKAA---AGDLGGDhlAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGI-- 86
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVeelAEELGAA--VLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFap 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLV 166
Cdd:pfam13561  84 KLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLS----------SIGAERVVPNYNAYGAAKAALE 151

                         170       180
                  ....*....|....*....|..
gi 578809569  167 GFSRALAKEVARKKIRVNVVAP 188
Cdd:pfam13561 152 ALTRYLAVELGPRGIRVNAISP 173

fabG

PRK08217

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

2-191

7.34e-43

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

Pssm-ID: 181297 [Multi-domain] Cd Length: 253 Bit Score: 144.33 E-value: 7.34e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK08217   5 DKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNqekLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQLN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRDGLLVRTKTEDMVSQ---------LHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVghrremllhkrSIVG 148
Cdd:PRK08217  85 GLINNAGILRDGLLVKAKDGKVTSKmsleqfqsvIDVNLTGVFLCGREAAAKMIESgSKGVIINI-----------SSIA 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 578809569 149 LKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK08217 154 RAGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVI 196

PRK06484

short chain dehydrogenase; Validated

3-188

5.28e-40

short chain dehydrogenase; Validated

Pssm-ID: 168574 [Multi-domain] Cd Length: 520 Bit Score: 142.68 E-value: 5.28e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK06484   6 RVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDVLVN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAGINRDGL--LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK06484  86 NAGVTDPTMtaTLDTTLEEFARLQAINLTGAYLVAREALRLMIEQgHGAAIVNVA----------SGAGLVALPKRTAYS 155

                        170       180
                 ....*....|....*....|....*....
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06484 156 ASKAAVISLTRSLACEWAAKGIRVNAVLP 184

PRK12824

3-oxoacyl-ACP reductase;

1-192

3.38e-39

3-oxoacyl-ACP reductase;

Pssm-ID: 183773 [Multi-domain] Cd Length: 245 Bit Score: 134.51 E-value: 3.38e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRlaVIARNLEGAKAAA---GDLGGDHL---AFSCDVAKEHDVQNTFEELEKHL 74
Cdd:PRK12824   1 MKKIALVTGAKRGIGSAIARELLNDGYR--VIATYFSGNDCAKdwfEEYGFTEDqvrLKELDVTDTEECAEALAEIEEEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  75 GRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSG 154
Cdd:PRK12824  79 GPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINIS----------SVNGLKGQFG 148

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 578809569 155 QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTIL 192
Cdd:PRK12824 149 QTNYSAAKAGMIGFTKALASEGARYGITVNCIAPGYIA 186

PRK06841

short chain dehydrogenase; Provisional

2-192

2.25e-38

short chain dehydrogenase; Provisional

Pssm-ID: 180723 [Multi-domain] Cd Length: 255 Bit Score: 132.86 E-value: 2.25e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK06841  15 GKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRIDILV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNvghrremLLHKRSIVGLKGNSGqsvYSAS 161
Cdd:PRK06841  95 NSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVN-------LASQAGVVALERHVA---YCAS 164

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809569 162 KGGLVGFSRALAKEVARKKIRVNVVAPVTIL 192
Cdd:PRK06841 165 KAGVVGMTKVLALEWGPYGITVNAISPTVVL 195

PRK06138

SDR family oxidoreductase;

2-191

1.48e-37

SDR family oxidoreductase;

Pssm-ID: 235712 [Multi-domain] Cd Length: 252 Bit Score: 130.66 E-value: 1.48e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL--GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK06138   5 GRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIaaGGRAFARQGDVGSAEAVEALVDFVAARWGRLDV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllHKRSIVGLKGNSGqsvYS 159
Cdd:PRK06138  85 LVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTA-------SQLALAGGRGRAA---YV 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK06138 155 ASKGAIASLTRAMALDHATDGIRVNAVAPGTI 186

FabG-like

PRK07231

SDR family oxidoreductase;

2-191

3.50e-37

SDR family oxidoreductase;

Pssm-ID: 235975 [Multi-domain] Cd Length: 251 Bit Score: 129.56 E-value: 3.50e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG--GDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07231   5 GKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILagGRAIAVAADVSDEADVEAAVAAALERFGSVDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGIN-RDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:PRK07231  85 LVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVA----------STAGLRPRPGLGWY 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 159 SASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK07231 155 NASKGAVITLTKALAAELGPDKIRVNAVAPVVV 187

Ga5DH-like_SDR_c

cd05347

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...

3-188

1.67e-36

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187605 [Multi-domain] Cd Length: 248 Bit Score: 127.47 E-value: 1.67e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05347    6 KVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIekeGVEATAFTCDVSDEEAIKAAVEAIEEDFGKIDI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:cd05347   86 LVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINIC----------SLLSELGGPPVPAYA 155

                        170       180
                 ....*....|....*....|....*....
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05347  156 ASKGGVAGLTKALATEWARHGIQVNAIAP 184

PRK12429

3-hydroxybutyrate dehydrogenase; Provisional

2-188

2.04e-35

3-hydroxybutyrate dehydrogenase; Provisional

Pssm-ID: 237100 [Multi-domain] Cd Length: 258 Bit Score: 125.00 E-value: 2.04e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK12429   4 GKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALqkaGGKAIGVAMDVTDEEAINAGIDYAVETFGGVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:PRK12429  84 ILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMA----------SVHGLVGSAGKAAY 153

                        170       180       190
                 ....*....|....*....|....*....|
gi 578809569 159 SASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12429 154 VSAKHGLIGLTKVVALEGATHGVTVNAICP 183

KDSR-like_SDR_c

cd08939

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...

2-191

2.21e-35

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187643 [Multi-domain] Cd Length: 239 Bit Score: 124.29 E-value: 2.21e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLA-------FSCDVAKEHDVQNTFEELEKHL 74
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEANAsgqkvsyISADLSDYEEVEQAFAQAVEKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  75 GRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSG 154
Cdd:cd08939   81 GPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVS----------SQAALVGIYG 150

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 578809569 155 QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:cd08939  151 YSAYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDT 187

PRK06484

short chain dehydrogenase; Validated

3-192

1.51e-34

short chain dehydrogenase; Validated

Pssm-ID: 168574 [Multi-domain] Cd Length: 520 Bit Score: 127.66 E-value: 1.51e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK06484 270 RVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRLDVLVN 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAGINRDGL-LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSAS 161
Cdd:PRK06484 350 NAGIAEVFKpSLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNLG----------SIASLLALPPRNAYCAS 417

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809569 162 KGGLVGFSRALAKEVARKKIRVNVVAPVTIL 192
Cdd:PRK06484 418 KAAVTMLSRSLACEWAPAGIRVNTVAPGYIE 448

fabG

PRK07666

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

3-191

1.59e-34

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

Pssm-ID: 236074 [Multi-domain] Cd Length: 239 Bit Score: 122.10 E-value: 1.59e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG--GDHLAF-SCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07666   8 KNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEayGVKVVIaTADVSDYEEVTAAIEQLKNELGSIDI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK07666  88 LINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINIS----------STAGQKGAAVTSAYS 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK07666 158 ASKFGVLGLTESLMQEVRKHNIRVTALTPSTV 189

17beta-HSD-like_SDR_c

cd05374

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...

3-188

7.43e-34

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187632 [Multi-domain] Cd Length: 248 Bit Score: 120.80 E-value: 7.43e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:cd05374   81 NAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVS----------SVAGLVPTPFLGPYCASK 150

                        170       180
                 ....*....|....*....|....*.
gi 578809569 163 GGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05374  151 AALEALSESLRLELAPFGIKVTIIEP 176

PRK12939

short chain dehydrogenase; Provisional

3-188

1.45e-33

short chain dehydrogenase; Provisional

Pssm-ID: 183833 [Multi-domain] Cd Length: 250 Bit Score: 120.08 E-value: 1.45e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK12939   8 KRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALeaaGGRAHAIAADLADPASVQRFFDAAAAALGGLDG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK12939  88 LVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLA----------SDTALWGAPKLGAYV 157

                        170       180
                 ....*....|....*....|....*....
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12939 158 ASKGAVIGMTRSLARELGGRGITVNAIAP 186

PRK06171

sorbitol-6-phosphate 2-dehydrogenase; Provisional

2-188

3.56e-33

sorbitol-6-phosphate 2-dehydrogenase; Provisional

Pssm-ID: 180439 [Multi-domain] Cd Length: 266 Bit Score: 119.35 E-value: 3.56e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNlegakaaAGDLGGDHLAF-SCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK06171   9 GKIIIVTGGSSGIGLAIVKELLANGANVVNADIH-------GGDGQHENYQFvPTDVSSAEEVNHTVAEIIEKFGRIDGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGINRDGLLVRTKTEDMVSQLHT---------NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKG 151
Cdd:PRK06171  82 VNNAGINIPRLLVDEKDPAGKYELNEaafdkmfniNQKGVFLMSQAVARQMVKQHDGVIVNMS----------SEAGLEG 151

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 578809569 152 NSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06171 152 SEGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAP 188

THN_reductase-like_SDR_c

cd05362

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...

3-188

4.62e-33

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187620 [Multi-domain] Cd Length: 243 Bit Score: 118.53 E-value: 4.62e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:cd05362    4 KVALVTGASRGIGRAIAKRLARDGASVVVnYASSKAAAEEVVAeieAAGGKAIAVQADVSDPSQVARLFDAAEKAFGGVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:cd05362   84 ILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINIS----------SSLTAAYTPNYGAY 151

                        170       180       190
                 ....*....|....*....|....*....|
gi 578809569 159 SASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05362  152 AGSKAAVEAFTRVLAKELGGRGITVNAVAP 181

PRK07326

SDR family oxidoreductase;

1-188

7.45e-33

SDR family oxidoreductase;

Pssm-ID: 235990 [Multi-domain] Cd Length: 237 Bit Score: 117.80 E-value: 7.45e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG--GDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07326   5 KGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNnkGNVLGLAADVRDEADVQRAVDAIVAAFGGLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:PRK07326  85 VLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPAL-KRGGGYIINIS----------SLAGTNFFAGGAAY 153

                        170       180       190
                 ....*....|....*....|....*....|
gi 578809569 159 SASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07326 154 NASKFGLVGFSEAAMLDLRQYGIKVSTIMP 183

PRK08213

gluconate 5-dehydrogenase; Provisional

3-188

9.61e-33

gluconate 5-dehydrogenase; Provisional

Pssm-ID: 181295 [Multi-domain] Cd Length: 259 Bit Score: 118.13 E-value: 9.61e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIAR---NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK08213  13 KTALVTGGSRGLGLQIAEALGEAGARVVLSARkaeELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFGHVDI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDgllvrTKTEDMVSQ-----LHTNLLGS-MLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNS 153
Cdd:PRK08213  93 LVNNAGATWG-----APAEDHPVEawdkvMNLNVRGLfLLSQAVAKRSMIPRGYGRIINVA----------SVAGLGGNP 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 578809569 154 GQSV----YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08213 158 PEVMdtiaYNTSKGAVINFTRALAAEWGPHGIRVNAIAP 196

MDH-like_SDR_c

cd05352

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...

2-188

1.36e-32

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).

Pssm-ID: 187610 [Multi-domain] Cd Length: 252 Bit Score: 117.43 E-value: 1.36e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH----LAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd05352    8 GKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYgvktKAYKCDVSSQESVEKTFKQIQKDFGKI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINRD-GLLVRTKtEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGN--SG 154
Cdd:cd05352   88 DILIANAGITVHkPALDYTY-EQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITA----------SMSGTIVNrpQP 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 578809569 155 QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05352  157 QAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISP 190

PRK06172

SDR family oxidoreductase;

2-191

1.70e-32

SDR family oxidoreductase;

Pssm-ID: 180440 [Multi-domain] Cd Length: 253 Bit Score: 117.54 E-value: 1.70e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNL---EGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK06172   7 GKVALVTGGAAGIGRATALAFAREGAKVVVADRDAaggEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAYGRLD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRDGLLVRTKTEDMVSQL-HTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK06172  87 YAFNNAGIEIEQGRLAEGSEAEFDAImGVNVKGVWLCMKYQIPLMLAQGGGAIVNTA----------SVAGLGAAPKMSI 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 578809569 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK06172 157 YAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVI 190

BKR_2_SDR_c

cd05349

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...

3-188

1.83e-32

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187607 [Multi-domain] Cd Length: 246 Bit Score: 117.17 E-value: 1.83e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVnYYRSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGINR--DGLLVRTKT----EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:cd05349   81 NNALIDFpfDPDQRKTFDtidwEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIG----------TNLFQNPVVPY 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05349  151 HDYTTAKAALLGFTRNMAKELGPYGITVNMVSG 183

GlcDH_SDR_c

cd05358

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...

3-191

4.17e-32

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187616 [Multi-domain] Cd Length: 253 Bit Score: 116.33 E-value: 4.17e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAViarNLEGAKAAAGDL-------GGDHLAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:cd05358    4 KVALVTGASSGIGKAIAIRLATAGANVVV---NYRSKEDAAEEVveeikavGGKAIAVQADVSKEEDVVALFQSAIKEFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQG-GSIVNVGHRREMLLHkrsivglkgnSG 154
Cdd:cd05358   81 TLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKIkGKIINMSSVHEKIPW----------PG 150

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 578809569 155 QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:cd05358  151 HVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAI 187

PRK12936

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed

7-188

4.94e-32

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed

Pssm-ID: 171820 [Multi-domain] Cd Length: 245 Bit Score: 116.17 E-value: 4.94e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGI 86
Cdd:PRK12936  11 VTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEADLEGVDILVNNAGI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkRSIVGLKGNSGQSVYSASKGGLV 166
Cdd:PRK12936  91 TKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINI----------TSVVGVTGNPGQANYCASKAGMI 160

                        170       180
                 ....*....|....*....|..
gi 578809569 167 GFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12936 161 GFSKSLAQEIATRNVTVNCVAP 182

PRK07063

SDR family oxidoreductase;

3-192

6.50e-32

SDR family oxidoreductase;

Pssm-ID: 235924 [Multi-domain] Cd Length: 260 Bit Score: 115.92 E-value: 6.50e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK07063   8 KVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIardvaGARVLAVPADVTDAASVAAAVAAAEEAFGPL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGIN--RDGLlvRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHrremlLHKRSIVglkgnSGQ 155
Cdd:PRK07063  88 DVLVNNAGINvfADPL--AMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIAS-----THAFKII-----PGC 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTIL 192
Cdd:PRK07063 156 FPYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIE 192

BKR_like_SDR_like

cd05344

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...

2-188

8.62e-32

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187602 [Multi-domain] Cd Length: 253 Bit Score: 115.45 E-value: 8.62e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELragGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:cd05344   81 ILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNIS----------SLTVKEPEPNLVLS 150

                        170       180       190
                 ....*....|....*....|....*....|
gi 578809569 159 SASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05344  151 NVARAGLIGLVKTLSRELAPDGVTVNSVLP 180

ADH_SDR_c_like

cd05323

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...

3-188

5.79e-31

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187584 [Multi-domain] Cd Length: 244 Bit Score: 113.16 E-value: 5.79e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLE-GAKAAAGDLGGDHLA--FSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENpGAAAELQAINPKVKAtfVQCDVTSWEQLAAAFKKAIEKFGRVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGIN--RDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ---GGSIVNVGhrremllhkrSIVGLKGNSG 154
Cdd:cd05323   81 LINNAGILdeKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKggkGGVIVNIG----------SVAGLYPAPQ 150

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 578809569 155 QSVYSASKGGLVGFSRALAKEVARKK-IRVNVVAP 188
Cdd:cd05323  151 FPVYSASKHGVVGFTRSLADLLEYKTgVRVNAICP 185

3beta-17beta-HSD_like_SDR_c

cd05341

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...

2-188

7.26e-31

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187600 [Multi-domain] Cd Length: 247 Bit Score: 112.86 E-value: 7.26e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:cd05341    5 GKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFGRLDVLV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSAS 161
Cdd:cd05341   85 NNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMS----------SIEGLVGDPALAAYNAS 154

                        170       180
                 ....*....|....*....|....*....
gi 578809569 162 KGGLVGFSRALAKEVARKK--IRVNVVAP 188
Cdd:cd05341  155 KGAVRGLTKSAALECATQGygIRVNSVHP 183

PRK12935

acetoacetyl-CoA reductase; Provisional

3-188

1.19e-30

acetoacetyl-CoA reductase; Provisional

Pssm-ID: 183832 [Multi-domain] Cd Length: 247 Bit Score: 112.41 E-value: 1.19e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAViarNLEGAKAAA-------GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:PRK12935   7 KVAIVTGGAKGIGKAITVALAQEGAKVVI---NYNSSKEAAenlvnelGKEGHDVYAVQADVSKVEDANRLVEEAVNHFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:PRK12935  84 KVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISIS----------SIIGQAGGFGQ 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12935 154 TNYSAAKAGMLGFTKSLALELAKTNVTVNAICP 186

17beta-HSDXI-like_SDR_c

cd05339

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...

4-191

1.30e-30

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187598 [Multi-domain] Cd Length: 243 Bit Score: 112.34 E-value: 1.30e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   4 VCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:cd05339    1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETAnnvRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:cd05339   81 INNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIA----------SVAGLISPAGLADYCA 150

                        170       180       190
                 ....*....|....*....|....*....|....
gi 578809569 161 SKGGLVGFSRALAKEVAR---KKIRVNVVAPVTI 191
Cdd:cd05339  151 SKAAAVGFHESLRLELKAygkPGIKTTLVCPYFI 184

SDR_c4

cd08929

classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...

3-191

1.75e-30

classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187634 [Multi-domain] Cd Length: 226 Bit Score: 111.45 E-value: 1.75e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:cd08929   81 NAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVG----------SLAGKNAFKGGAAYNASK 150

                        170       180
                 ....*....|....*....|....*....
gi 578809569 163 GGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:cd08929  151 FGLLGLSEAAMLDLREANIRVVNVMPGSV 179

hydroxyacyl-CoA-like_DH_SDR_c-like

cd05353

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...

2-188

3.67e-30

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187611 [Multi-domain] Cd Length: 250 Bit Score: 111.26 E-value: 3.67e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAV----IARNLEGAKAAAGDL--------GGDHLAFSCDVAkehDVQNTFEE 69
Cdd:cd05353    5 GRVVLVTGAGGGLGRAYALAFAERGAKVVVndlgGDRKGSGKSSSAADKvvdeikaaGGKAVANYDSVE---DGEKIVKT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  70 LEKHLGRVNFLVNAAGINRDGLLVRTKTE--DMVSQLHtnLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIV 147
Cdd:cd05353   82 AIDAFGRVDILVNNAGILRDRSFAKMSEEdwDLVMRVH--LKGSFKVTRAAWPYMRKQKFGRIINTS----------SAA 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 578809569 148 GLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05353  150 GLYGNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAP 190

PRK12828

short chain dehydrogenase; Provisional

3-191

8.31e-30

short chain dehydrogenase; Provisional

Pssm-ID: 237220 [Multi-domain] Cd Length: 239 Bit Score: 109.89 E-value: 8.31e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFS-CDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK12828   8 KVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGgIDLVDPQAARRAVDEVNRQFGRLDALV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSAS 161
Cdd:PRK12828  88 NIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIG----------AGAALKAGPGMGAYAAA 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 578809569 162 KGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK12828 158 KAGVARLTEALAAELLDRGITVNAVLPSII 187

PRK12829

short chain dehydrogenase; Provisional

1-191

1.53e-29

short chain dehydrogenase; Provisional

Pssm-ID: 183778 [Multi-domain] Cd Length: 264 Bit Score: 110.15 E-value: 1.53e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGG-DHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK12829  10 DGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPGaKVTATVADVADPAQVERVFDTAVERFGGLDV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGI-NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK12829  90 LVNNAGIaGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGhGGVIIALS----------SVAGRLGYPGRTP 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 578809569 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK12829 160 YAASKWAVVGLVKSLAIELGPLGIRVNAILPGIV 193

SDR_c3

cd05360

classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...

4-187

1.85e-29

classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a canonical active site triad (and also active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187618 [Multi-domain] Cd Length: 233 Bit Score: 109.01 E-value: 1.85e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   4 VCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:cd05360    2 VVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVrelGGEAIAVVADVADAAQVERAADTAVERFGRIDTW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:cd05360   82 VNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVG----------SLLGYRSAPLQAAYSA 151

                        170       180
                 ....*....|....*....|....*..
gi 578809569 161 SKGGLVGFSRALAKEVARKKIRVNVVA 187
Cdd:cd05360  152 SKHAVRGFTESLRAELAHDGAPISVTL 178

TER_DECR_SDR_a

cd05369

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...

2-188

1.99e-29

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187627 [Multi-domain] Cd Length: 249 Bit Score: 109.21 E-value: 1.99e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd05369    3 GKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEIssatGGRAHPIQCDVRDPEAVEAAVDETLKEFGKI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINrdgllVRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGhrremllhkrSIVGLKG 151
Cdd:cd05369   83 DILINNAAGN-----FLAPAESLSPNgfktvIDIDLNGTFNTTKAVGKRLIEAKhGGSILNIS----------ATYAYTG 147

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 578809569 152 NSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05369  148 SPFQVHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAP 184

SDR_c12

cd08944

classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...

3-188

2.67e-29

classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site tetrad and glycine-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187648 [Multi-domain] Cd Length: 246 Bit Score: 109.12 E-value: 2.67e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd08944    4 KVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFGGLDLLVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAGI-NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSAS 161
Cdd:cd08944   84 NAGAmHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLS----------SIAGQSGDPGYGAYGAS 153

                        170       180
                 ....*....|....*....|....*..
gi 578809569 162 KGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08944  154 KAAIRNLTRTLAAELRHAGIRCNALAP 180

HSD10-like_SDR_c

cd05371

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...

1-188

2.75e-29

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187629 [Multi-domain] Cd Length: 252 Bit Score: 108.92 E-value: 2.75e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGdlGGDHLAFS-CDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05371    1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAK--LGDNCRFVpVDVTSEKDVKAALALAKAKFGRLDI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGI-------NRDGLLVRtKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQG------GSIVNVGhrremllhkrSI 146
Cdd:cd05371   79 VVNCAGIavaaktyNKKGQQPH-SLELFQRVINVNLIGTFNVIRLAAGAMGKNEPdqggerGVIINTA----------SV 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 578809569 147 VGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05371  148 AAFEGQIGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAP 189

PRK06123

SDR family oxidoreductase;

1-191

3.02e-29

SDR family oxidoreductase;

Pssm-ID: 180411 [Multi-domain] Cd Length: 248 Bit Score: 108.71 E-value: 3.02e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKA---AAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK06123   1 MRKVMIITGASRGIGAATALLAAERGYAVCLnYLRNRDAAEAvvqAIRRQGGEALAVAADVADEADVLRLFEAVDRELGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGInrdgLLVRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQ---QGGSIVNVGhrremllhkrSIVG 148
Cdd:PRK06123  81 LDALVNNAGI----LEAQMRLEQMDAArltriFATNVVGSFLCAREAVKRMSTRhggRGGAIVNVS----------SMAA 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 578809569 149 LKGNSGQSV-YSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK06123 147 RLGSPGEYIdYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVI 190

PRK07109

short chain dehydrogenase; Provisional

2-188

3.07e-29

short chain dehydrogenase; Provisional

Pssm-ID: 235935 [Multi-domain] Cd Length: 334 Bit Score: 110.78 E-value: 3.07e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07109   8 RQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIraaGGEALAVVADVADAEAVQAAADRAEEELGPID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHrremLLHKRSIVgLkgnsgQSVY 158
Cdd:PRK07109  88 TWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGS----ALAYRSIP-L-----QSAY 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 159 SASKGGLVGFSRALAKEV--ARKKIRVNVVAP 188
Cdd:PRK07109 158 CAAKHAIRGFTDSLRCELlhDGSPVSVTMVQP 189

PRK12827

short chain dehydrogenase; Provisional

1-191

3.08e-29

short chain dehydrogenase; Provisional

Pssm-ID: 237219 [Multi-domain] Cd Length: 249 Bit Score: 108.65 E-value: 3.08e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIA----RNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKH 73
Cdd:PRK12827   5 DSRRVLITGGSGGLGRAIAVRLAADGADVIVLDihpmRGRAEADAVAAGIeaaGGKALGLAFDVRDFAATRAALDAGVEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  74 LGRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQ-QQGGSIVNVGhrremllhkrSIVGLKGN 152
Cdd:PRK12827  85 FGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRaRRGGRIVNIA----------SVAGVRGN 154

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 578809569 153 SGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK12827 155 RGQVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAI 193

HetN_like_SDR_c

cd08932

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...

3-188

6.31e-29

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 212493 [Multi-domain] Cd Length: 223 Bit Score: 107.45 E-value: 6.31e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDlGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS-GGDVEAVPYDARDPEDARALVDALRDRFGRIDVLVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:cd08932   80 NAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLN----------SLSGKRVLAGNAGYSASK 149

                        170       180
                 ....*....|....*....|....*.
gi 578809569 163 GGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08932  150 FALRALAHALRQEGWDHGVRVSAVCP 175

PRK06057

short chain dehydrogenase; Provisional

2-188

6.88e-29

short chain dehydrogenase; Provisional

Pssm-ID: 180371 [Multi-domain] Cd Length: 255 Bit Score: 107.89 E-value: 6.88e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGdhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK06057   7 GRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGG--LFVPTDVTDEDAVNALFDTAAETYGSVDIAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGIN--RDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGN-SGQSVY 158
Cdd:PRK06057  85 NNAGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTA----------SFVAVMGSaTSQISY 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 578809569 159 SASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06057 155 TASKGGVLAMSRELGVQFARQGIRVNALCP 184

PRK07035

SDR family oxidoreductase;

3-188

7.13e-29

SDR family oxidoreductase;

Pssm-ID: 180802 [Multi-domain] Cd Length: 252 Bit Score: 107.79 E-value: 7.13e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07035   9 KIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIvaaGGKAEALACHIGEMEQIDALFAHIRERHGRLDI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGIN-------RDGLLVRTKTEDMvsqlhtNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGN 152
Cdd:PRK07035  89 LVNNAAANpyfghilDTDLGAFQKTVDV------NIRGYFFMSVEAGKLMKEQGGGSIVNVA----------SVNGVSPG 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 578809569 153 SGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07035 153 DFQGIYSITKAAVISMTKAFAKECAPFGIRVNALLP 188

PRK09072

SDR family oxidoreductase;

9-188

9.00e-29

SDR family oxidoreductase;

Pssm-ID: 236372 [Multi-domain] Cd Length: 263 Bit Score: 108.11 E-value: 9.00e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEG--AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHlGRVNFLVNAAGI 86
Cdd:PRK09072  12 GASGGIGQALAEALAAAGARLLLVGRNAEKleALAARLPYPGRHRWVVADLTSEAGREAVLARAREM-GGINVLINNAGV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLV 166
Cdd:PRK09072  91 NHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVG----------STFGSIGYPGYASYCASKFALR 160

                        170       180
                 ....*....|....*....|..
gi 578809569 167 GFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK09072 161 GFSEALRRELADTGVRVLYLAP 182

DHRS1_HSDL2-like_SDR_c

cd05338

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...

3-191

9.01e-29

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187597 [Multi-domain] Cd Length: 246 Bit Score: 107.48 E-value: 9.01e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN-----------LEG----AKAAAGDLGGDHLAFSCDVAKEHDVQNTF 67
Cdd:cd05338    4 KVAFVTGASRGIGRAIALRLAKAGATVVVAAKTasegdngsaksLPGtieeTAEEIEAAGGQALPIVVDVRDEDQVRALV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  68 EELEKHLGRVNFLVNAAGInrdglLVRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllh 142
Cdd:cd05338   84 EATVDQFGRLDILVNNAGA-----IWLSLVEDTPAKrfdlmQRVNLRGTYLLSQAALPHMVKAGQGHILNIS-------- 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 578809569 143 krSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:cd05338  151 --PPLSLRPARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTA 197

meso-BDH-like_SDR_c

cd05366

meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...

1-191

9.87e-29

meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187624 [Multi-domain] Cd Length: 257 Bit Score: 107.85 E-value: 9.87e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLE-GAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd05366    1 MSKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEeAAKSTIQEIseaGYNAVAVGADVTDKDDVEALIDQAVEKFGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:cd05366   81 FDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINAS----------SIAGVQGFPNL 150

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:cd05366  151 GAYSASKFAVRGLTQTAAQELAPKGITVNAYAPGIV 186

CAD_SDR_c

cd08934

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...

3-191

1.18e-28

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187639 [Multi-domain] Cd Length: 243 Bit Score: 107.24 E-value: 1.18e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd08934    4 KVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELeaeGGKALVLELDVTDEQQVDAAVERTVEALGRLDI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:cd08934   84 LVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNIS----------SVAGRVAVRNSAVYN 153

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:cd08934  154 ATKFGVNAFSEGLRQEVTERGVRVVVIEPGTV 185

PRK09730

SDR family oxidoreductase;

3-188

1.78e-28

SDR family oxidoreductase;

Pssm-ID: 182051 [Multi-domain] Cd Length: 247 Bit Score: 106.86 E-value: 1.78e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVAVnYQQNLHAAQEVVNLItqaGGKAFVLQADISDENQVVAMFTAIDQHDEPLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGInrdgLLVRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQ---QGGSIVNVGhrremllhkrSIVGLK 150
Cdd:PRK09730  82 ALVNNAGI----LFTQCTVENLTAErinrvLSTNVTGYFLCCREAVKRMALKhggSGGAIVNVS----------SAASRL 147

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 578809569 151 GNSGQSV-YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK09730 148 GAPGEYVdYAASKGAIDTLTTGLSLEVAAQGIRVNCVRP 186

secoisolariciresinol-DH_like_SDR_c

cd05326

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...

2-191

3.54e-28

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187587 [Multi-domain] Cd Length: 249 Bit Score: 106.00 E-value: 3.54e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAF-SCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:cd05326    4 GKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFvHCDVTVEADVRAAVDTAVARFGRLDIM 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGI--NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:cd05326   84 FNNAGVlgAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVA----------SVAGVVGGLGPHAY 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 159 SASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:cd05326  154 TASKHAVLGLTRSAATELGEHGIRVNCVSPYGV 186

PRK12384

sorbitol-6-phosphate dehydrogenase; Provisional

1-192

3.92e-28

sorbitol-6-phosphate dehydrogenase; Provisional

Pssm-ID: 183489 [Multi-domain] Cd Length: 259 Bit Score: 106.27 E-value: 3.92e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH-----LAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYgegmaYGFGADATSEQSVLALSRGVDEIFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGhrremllHKRSIVGLKGNSG 154
Cdd:PRK12384  81 RVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIQIN-------SKSGKVGSKHNSG 153

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 578809569 155 qsvYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTIL 192
Cdd:PRK12384 154 ---YSAAKFGGVGLTQSLALDLAEYGITVHSLMLGNLL 188

PRK12937

short chain dehydrogenase; Provisional

3-188

5.78e-28

short chain dehydrogenase; Provisional

Pssm-ID: 171821 [Multi-domain] Cd Length: 245 Bit Score: 105.59 E-value: 5.78e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAViarNLEGAKAAAGDL-------GGDHLAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:PRK12937   6 KVAIVTGASRGIGAAIARRLAADGFAVAV---NYAGSAAAADELvaeieaaGGRAIAVQADVADAAAVTRLFDAAETAFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVghrremllhKRSIVGLKGNSGq 155
Cdd:PRK12937  83 RIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINL---------STSVIALPLPGY- 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12937 151 GPYAASKAAVEGLVHVLANELRGRGITVNAVAP 183

PRK06180

short chain dehydrogenase; Provisional

9-188

6.54e-28

short chain dehydrogenase; Provisional

Pssm-ID: 180446 [Multi-domain] Cd Length: 277 Bit Score: 106.15 E-value: 6.54e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGINR 88
Cdd:PRK06180  11 GVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFGPIDVLVNNAGYGH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  89 DGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkRSIVGLKGNSGQSVYSASKGGLVGF 168
Cdd:PRK06180  91 EGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNI----------TSMGGLITMPGIGYYCGSKFALEGI 160

                        170       180
                 ....*....|....*....|
gi 578809569 169 SRALAKEVARKKIRVNVVAP 188
Cdd:PRK06180 161 SESLAKEVAPFGIHVTAVEP 180

PRK07825

short chain dehydrogenase; Provisional

2-188

9.24e-28

short chain dehydrogenase; Provisional

Pssm-ID: 181136 [Multi-domain] Cd Length: 273 Bit Score: 105.41 E-value: 9.24e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHlAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK07825   5 GKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELGLVV-GGPLDVTDPASFAAFLDAVEADLGPIDVLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSAS 161
Cdd:PRK07825  84 NNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVA----------SLAGKIPVPGMATYCAS 153

                        170       180
                 ....*....|....*....|....*..
gi 578809569 162 KGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07825 154 KHAVVGFTDAARLELRGTGVHVSVVLP 180

PRK06198

short chain dehydrogenase; Provisional

2-188

1.03e-27

short chain dehydrogenase; Provisional

Pssm-ID: 180462 [Multi-domain] Cd Length: 260 Bit Score: 105.09 E-value: 1.03e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYR-LAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK06198   6 GKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELealGAKAVFVQADLSDVEDCRRVVAAADEAFGRL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQG-GSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:PRK06198  86 DALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVNIG----------SMSAHGGQPFLA 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06198 156 AYCASKGALATLTRNAAYALLRNRIRVNGLNI 187

PRK08324

bifunctional aldolase/short-chain dehydrogenase;

3-192

1.17e-27

bifunctional aldolase/short-chain dehydrogenase;

Pssm-ID: 236241 [Multi-domain] Cd Length: 681 Bit Score: 109.16 E-value: 1.17e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGG--DHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK08324 423 KVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGpdRALGVACDVTDEAAVQAAFEEAALAFGGVDIV 502

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGhrremllHKRSIVGLKGNSGqsvYS 159
Cdd:PRK08324 503 VSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGlGGSIVFIA-------SKNAVNPGPNFGA---YG 572

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPVTIL 192
Cdd:PRK08324 573 AAKAAELHLVRQLALELGPDGIRVNGVNPDAVV 605

PRK06701

short chain dehydrogenase; Provisional

2-188

1.23e-27

short chain dehydrogenase; Provisional

Pssm-ID: 235853 [Multi-domain] Cd Length: 290 Bit Score: 105.50 E-value: 1.23e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEG----AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK06701  46 GKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEdaneTKQRVEKEGVKCLLIPGDVSDEAFCKDAVEETVRELGRL 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAG--INRDGLlvrtktEDMVSQ-----LHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLK 150
Cdd:PRK06701 126 DILVNNAAfqYPQQSL------EDITAEqldktFKTNIYSYFHMTKAALPHL--KQGSAIINTG----------SITGYE 187

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 578809569 151 GNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06701 188 GNETLIDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAP 225

PRK08643

(S)-acetoin forming diacetyl reductase;

1-188

7.11e-27

(S)-acetoin forming diacetyl reductase;

Pssm-ID: 181518 [Multi-domain] Cd Length: 256 Bit Score: 102.88 E-value: 7.11e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLskdGGKAIAVKADVSDRDQVFAAVRQVVDTFGDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINrDGLLVRTKTEDMVSQLH-TNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:PRK08643  81 NVVVNNAGVA-PTTPIETITEEQFDKVYnINVGGVIWGIQAAQEAFKKLgHGGKIINAT----------SQAGVVGNPEL 149

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08643 150 AVYSSTKFAVRGLTQTAARDLASEGITVNAYAP 182

SDR_c6

cd05350

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...

6-188

7.81e-27

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187608 [Multi-domain] Cd Length: 239 Bit Score: 102.41 E-value: 7.81e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   6 AVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH---LAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05350    2 LITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNpsvEVEILDVTDEERNQLVIAELEAELGGLDLVII 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:cd05350   82 NAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLIS----------SVAALRGLPGAAAYSASK 151

                        170       180
                 ....*....|....*....|....*.
gi 578809569 163 GGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05350  152 AALSSLAESLRYDVKKRGIRVTVINP 177

SDH_SDR_c_like

cd05322

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...

1-197

8.06e-27

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187583 [Multi-domain] Cd Length: 257 Bit Score: 102.54 E-value: 8.06e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA----GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd05322    1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVAdeinAEYGEKAYGFGADATNEQSVIALSKGVDEIFKR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllHKRSIVGLKGNSGq 155
Cdd:cd05322   81 VDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDgIQGRIIQIN-------SKSGKVGSKHNSG- 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 578809569 156 svYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTILVWSLF 197
Cdd:cd05322  153 --YSAAKFGGVGLTQSLALDLAEHGITVNSLMLGNLLKSPMF 192

BKR_3_SDR_c

cd05345

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...

1-189

8.70e-27

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187603 [Multi-domain] Cd Length: 248 Bit Score: 102.47 E-value: 8.70e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:cd05345    4 EGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFGRLDIL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGI---NRDGLLVRTKTEDMVSQLhtNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:cd05345   84 VNNAGIthrNKPMLEVDEEEFDRVFAV--NVKSIYLSAQALVPHMEEQGGGVIINIA----------STAGLRPRPGLTW 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAPV 189
Cdd:cd05345  152 YNASKGWVVTATKAMAVELAPRNIRVNCLCPV 183

PRK07454

SDR family oxidoreductase;

9-188

9.88e-27

SDR family oxidoreductase;

Pssm-ID: 180984 [Multi-domain] Cd Length: 241 Bit Score: 101.96 E-value: 9.88e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   9 GGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:PRK07454  13 GASSGIGKATALAFAKAGWDLALVARSqdaLEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDVLINNAG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  86 INRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGL 165
Cdd:PRK07454  93 MAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVS----------SIAARNAFPQWGAYCVSKAAL 162

                        170       180
                 ....*....|....*....|...
gi 578809569 166 VGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07454 163 AAFTKCLAEEERSHGIRVCTITL 185

PRK06124

SDR family oxidoreductase;

3-188

1.42e-26

SDR family oxidoreductase;

Pssm-ID: 235702 [Multi-domain] Cd Length: 256 Bit Score: 102.10 E-value: 1.42e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK06124  12 QVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALraaGGAAEALAFDIADEEAVAAAFARIDAEHGRLDI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGI-NRDGLLvRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkRSIVGLKGNSGQSVY 158
Cdd:PRK06124  92 LVNNVGArDRRPLA-ELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAI----------TSIAGQVARAGDAVY 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 578809569 159 SASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06124 161 PAAKQGLTGLMRALAAEFGPHGITSNAIAP 190

PRK08263

short chain dehydrogenase; Provisional

1-188

1.43e-26

short chain dehydrogenase; Provisional

Pssm-ID: 181334 [Multi-domain] Cd Length: 275 Bit Score: 102.42 E-value: 1.43e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK08263   2 MEKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGRLDIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:PRK08263  82 VNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQIS----------SIGGISAFPMSGIYHA 151

                        170       180
                 ....*....|....*....|....*...
gi 578809569 161 SKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08263 152 SKWALEGMSEALAQEVAEFGIKVTLVEP 179

PRK07060

short chain dehydrogenase; Provisional

3-192

2.48e-26

short chain dehydrogenase; Provisional

Pssm-ID: 180817 [Multi-domain] Cd Length: 245 Bit Score: 100.94 E-value: 2.48e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFscDVAKEHDVQNTFEELekhlGRVNFLVN 82
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCEPLRL--DVGDDAAIRAALAAA----GAFDGLVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMI-QQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSAS 161
Cdd:PRK07060  84 CAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIaAGRGGSIVNVS----------SQAALVGLPDHLAYCAS 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809569 162 KGGLVGFSRALAKEVARKKIRVNVVAPVTIL 192
Cdd:PRK07060 154 KAALDAITRVLCVELGPHGIRVNSVNPTVTL 184

PRK12938

3-ketoacyl-ACP reductase;

3-188

3.92e-26

3-ketoacyl-ACP reductase;

Pssm-ID: 171822 [Multi-domain] Cd Length: 246 Bit Score: 100.86 E-value: 3.92e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV--------IARNLEGAKAaagdLGGDHLAFSCDVAKEHDVQNTFEELEKHL 74
Cdd:PRK12938   4 RIAYVTGGMGGIGTSICQRLHKDGFKVVAgcgpnsprRVKWLEDQKA----LGFDFIASEGNVGDWDSTKAAFDKVKAEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  75 GRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSG 154
Cdd:PRK12938  80 GEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINIS----------SVNGQKGQFG 149

                        170       180       190
                 ....*....|....*....|....*....|....
gi 578809569 155 QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12938 150 QTNYSTAKAGIHGFTMSLAQEVATKGVTVNTVSP 183

PRK07074

SDR family oxidoreductase;

1-191

4.65e-26

SDR family oxidoreductase;

Pssm-ID: 180823 [Multi-domain] Cd Length: 257 Bit Score: 100.61 E-value: 4.65e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH-LAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07074   1 TKRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDARfVPVACDLTDAASLAAALANAAAERGPVDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGnSGQSVYS 159
Cdd:PRK07074  81 LVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIG----------SVNGMAA-LGHPAYS 149

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK07074 150 AAKAGLIHYTKLLAVEYGRFGIRANAVAPGTV 181

SDR_c11

cd05364

classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...

2-192

7.78e-26

classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187622 [Multi-domain] Cd Length: 253 Bit Score: 100.18 E-value: 7.78e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKA------AAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:cd05364    3 GKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEEtrqsclQAGVSEKKILLVVADLTEEEGQDRIISTTLAKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQgGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:cd05364   83 RLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVS----------SVAGGRSFPGV 151

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTIL 192
Cdd:cd05364  152 LYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIV 188

PRK08277

D-mannonate oxidoreductase; Provisional

2-188

8.14e-26

D-mannonate oxidoreductase; Provisional

Pssm-ID: 236216 [Multi-domain] Cd Length: 278 Bit Score: 100.36 E-value: 8.14e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK08277  10 GKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIkaaGGEALAVKADVLDKESLEQARQQILEDFGPCD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINR---------DGLLVRTKT------EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhk 143
Cdd:PRK08277  90 ILINGAGGNHpkattdnefHELIEPTKTffdldeEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINIS--------- 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 578809569 144 rSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08277 161 -SMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAP 204

PRK06947

SDR family oxidoreductase;

1-191

1.27e-25

SDR family oxidoreductase;

Pssm-ID: 180771 [Multi-domain] Cd Length: 248 Bit Score: 99.49 E-value: 1.27e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK06947   1 MRKVVLITGASRGIGRATAVLAAARGWSVGInYARDAAAAEETADavrAAGGRACVVAGDVANEADVIAMFDAVQSAFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGINRDGL-LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ---GGSIVNVGhrremllhkrSIVGLKGN 152
Cdd:PRK06947  81 LDALVNNAGIVAPSMpLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRggrGGAIVNVS----------SIASRLGS 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 578809569 153 SGQSV-YSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK06947 151 PNEYVdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLI 190

fabG

PRK08642

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

1-187

2.40e-25

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

Pssm-ID: 181517 [Multi-domain] Cd Length: 253 Bit Score: 98.62 E-value: 2.40e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR-VN 78
Cdd:PRK08642   4 SEQTVLVTGGSRGLGAAIARAFAREGARVVVnYHQSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEHFGKpIT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAA-------GINRDGLLVRTkTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRremlLHKRSIVGLKG 151
Cdd:PRK08642  84 TVVNNAladfsfdGDARKKADDIT-WEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGTN----LFQNPVVPYHD 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 578809569 152 nsgqsvYSASKGGLVGFSRALAKEVARKKIRVNVVA 187
Cdd:PRK08642 159 ------YTTAKAALLGLTRNLAAELGPYGITVNMVS 188

PRK06398

aldose dehydrogenase; Validated

2-192

4.15e-25

aldose dehydrogenase; Validated

Pssm-ID: 235794 [Multi-domain] Cd Length: 258 Bit Score: 98.37 E-value: 4.15e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGakaaagDLGGDHlaFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK06398   6 DKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPS------YNDVDY--FKVDVSNKEQVIKGIDYVISKYGRIDILV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREMLLHKRSivglkgnsgqSVYSAS 161
Cdd:PRK06398  78 NNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNA----------AAYVTS 147

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809569 162 KGGLVGFSRALAKEVArKKIRVNVVAPVTIL 192
Cdd:PRK06398 148 KHAVLGLTRSIAVDYA-PTIRCVAVCPGSIR 177

fabG

PRK08261

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

3-188

5.10e-25

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

Pssm-ID: 236207 [Multi-domain] Cd Length: 450 Bit Score: 100.68 E-value: 5.10e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRlaVIARNLEGAKAA----AGDLGGDHLAfsCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK08261 211 KVALVTGAARGIGAAIAEVLARDGAH--VVCLDVPAAGEAlaavANRVGGTALA--LDITAPDAPARIAEHLAERHGGLD 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRDGLLVRTKTE--DMVsqLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:PRK08261 287 IVVHNAGITRDKTLANMDEArwDSV--LAVNLLAPLRITEALLAAGALGDGGRIVGVS----------SISGIAGNRGQT 354

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08261 355 NYAASKAGVIGLVQALAPLLAERGITINAVAP 386

PRK08589

SDR family oxidoreductase;

2-191

8.80e-25

SDR family oxidoreductase;

Pssm-ID: 181491 [Multi-domain] Cd Length: 272 Bit Score: 97.54 E-value: 8.80e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKG-YRLAV-IARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK08589   6 NKVAVITGASTGIGQASAIALAQEGaYVLAVdIAEAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRVDV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMIQQqGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:PRK08589  86 LFNNAGVDNAAGRIHEYPVDVFDKiMAVDMRGTFLMTKMLLPLMMEQ-GGSIINTS----------SFSGQAADLYRSGY 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 159 SASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK08589 155 NAAKGAVINFTKSIAIEYGRDGIRANAIAPGTI 187

PRK07067

L-iditol 2-dehydrogenase;

2-188

1.05e-24

L-iditol 2-dehydrogenase;

Pssm-ID: 235925 [Multi-domain] Cd Length: 257 Bit Score: 97.02 E-value: 1.05e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK07067   6 GKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFGGIDILF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:PRK07067  86 NNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQgRGGKIINMA----------SQAGRRGEALVSHYCA 155

                        170       180
                 ....*....|....*....|....*...
gi 578809569 161 SKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07067 156 TKAAVISYTQSAALALIRHGINVNAIAP 183

PRK08628

SDR family oxidoreductase;

2-188

1.19e-24

SDR family oxidoreductase;

Pssm-ID: 181508 [Multi-domain] Cd Length: 258 Bit Score: 96.95 E-value: 1.19e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG--DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK08628   7 DKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDEFAEElrALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRIDG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINrDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMrTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK08628  87 LVNNAGVN-DGVGLEAGREAFVASLERNLIHYYVMAHYCL-PHLKASRGAIVNIS----------SKTALTGQGGTSGYA 154

                        170       180
                 ....*....|....*....|....*....
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08628 155 AAKGAQLALTREWAVALAKDGVRVNAVIP 183

SDR_c8

cd08930

classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...

1-188

1.23e-24

classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187635 [Multi-domain] Cd Length: 250 Bit Score: 96.63 E-value: 1.23e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELtnlyKNRVIALELDITSKESIKELIESYLEKFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGINRDGLLVR---TKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGL---- 149
Cdd:cd08930   81 IDILINNAYPSPKVWGSRfeeFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIA----------SIYGViapd 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 578809569 150 ----KGNSGQS--VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08930  151 friyENTQMYSpvEYSVIKAGIIHLTKYLAKYYADTGIRVNAISP 195

PRK06181

SDR family oxidoreductase;

2-188

1.48e-24

SDR family oxidoreductase;

Pssm-ID: 235726 [Multi-domain] Cd Length: 263 Bit Score: 96.97 E-value: 1.48e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNetrLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRDGLLVRTKTEDMVSQL-HTNLLGSMLTCKAAMRTMIQQQgGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK06181  81 ILVNNAGITMWSRFDELTDLSVFERVmRVNYLGAVYCTHAALPHLKASR-GQIVVVS----------SLAGLTGVPTRSG 149

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809569 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06181 150 YAASKHALHGFFDSLRIELADDGVAVTVVCP 180

PRK13394

3-hydroxybutyrate dehydrogenase; Provisional

3-188

2.32e-24

3-hydroxybutyrate dehydrogenase; Provisional

Pssm-ID: 184025 [Multi-domain] Cd Length: 262 Bit Score: 96.50 E-value: 2.32e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK13394   8 KTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVAdeiNKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGSVDI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQ-QQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:PRK13394  88 LVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKdDRGGVVIYMG----------SVHSHEASPLKSAY 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 578809569 159 SASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK13394 158 VTAKHGLLGLARVLAKEGAKHNVRSHVVCP 187

R1PA_ADH_SDR_c

cd08943

rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...

3-192

3.15e-24

rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has bifunctional proteins with an N-terminal aldolase and a C-terminal classical SDR domain. One member is identified as a rhamnulose-1-phosphate aldolase/alcohol dehydrogenase. The SDR domain has a canonical SDR glycine-rich NAD(P) binding motif and a match to the characteristic active site triad. However, it lacks an upstream active site Asn typical of SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187647 [Multi-domain] Cd Length: 250 Bit Score: 95.54 E-value: 3.15e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGD--LGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:cd08943    2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAaqGGPRALGVQCDVTSEAQVQSAFEQAVLEFGGLDIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGhrremllHKRSIVGLKGNSGqsvYS 159
Cdd:cd08943   82 VSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGiGGNIVFNA-------SKNAVAPGPNAAA---YS 151

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPVTIL 192
Cdd:cd08943  152 AAKAAEAHLARCLALEGGEDGIRVNTVNPDAVF 184

PRK05867

SDR family oxidoreductase;

7-188

3.78e-24

SDR family oxidoreductase;

Pssm-ID: 135631 [Multi-domain] Cd Length: 253 Bit Score: 95.49 E-value: 3.78e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA 83
Cdd:PRK05867  14 ITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIgtsGGKVVPVCCDVSQHQQVTSMLDQVTAELGGIDIAVCN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  84 AGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSV--YSA 160
Cdd:PRK05867  94 AGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQgQGGVIINTA----------SMSGHIINVPQQVshYCA 163

                        170       180
                 ....*....|....*....|....*...
gi 578809569 161 SKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK05867 164 SKAAVIHLTKAMAVELAPHKIRVNSVSP 191

fabG

PRK06463

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

2-188

8.77e-24

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

Pssm-ID: 180576 [Multi-domain] Cd Length: 255 Bit Score: 94.85 E-value: 8.77e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGdhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK06463   7 GKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKELREKGV--FTIKCDVGNRDQVKKSKEVVEKEFGRVDVLV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGI-------NRDgllvRTKTEDMVSqlhTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGL-KGNS 153
Cdd:PRK06463  85 NNAGImylmpfeEFD----EEKYNKMIK---INLNGAIYTTYEFLPLLKLSKNGAIVNIA----------SNAGIgTAAE 147

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 578809569 154 GQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06463 148 GTTFYAITKAGIIILTRRLAFELGKYGIRVNAVAP 182

RDH_SDR_c

cd08933

retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...

2-191

9.13e-24

retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the short-chain dehydrogenases/reductase family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187638 [Multi-domain] Cd Length: 261 Bit Score: 94.91 E-value: 9.13e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG----GDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd08933    9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNragpGSCKFVPCDVTKEEDIKTLISVTVERFGRI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINRDGLLV-RTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGgSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:cd08933   89 DCLVNNAGWHPPHQTTdETSAQEFRDLLNLNLISYFLASKYALPHLRKSQG-NIINLS----------SLVGSIGQKQAA 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 578809569 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:cd08933  158 PYVATKGAITAMTKALAVDESRYGVRVNCISPGNI 192

PRK05650

SDR family oxidoreductase;

9-188

1.54e-23

SDR family oxidoreductase;

Pssm-ID: 235545 [Multi-domain] Cd Length: 270 Bit Score: 94.34 E-value: 1.54e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:PRK05650   7 GAASGLGRAIALRWAREGWRLALADVNEEGGEETLkllREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVIVNNAG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  86 INRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGL 165
Cdd:PRK05650  87 VASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIA----------SMAGLMQGPAMSSYNVAKAGV 156

                        170       180
                 ....*....|....*....|...
gi 578809569 166 VGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK05650 157 VALSETLLVELADDEIGVHVVCP 179

SDR_c1

cd05355

classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...

2-188

1.67e-23

classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187613 [Multi-domain] Cd Length: 270 Bit Score: 94.28 E-value: 1.67e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKA-----AAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd05355   26 GKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEDDAeetkkLIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEFGK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGINRDGLLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:cd05355  106 LDILVNNAAYQHPQESIEDITTEQLEKtFRTNIFSMFYLTKAALPHL--KKGSSIINTT----------SVTAYKGSPHL 173

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05355  174 LDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAP 206

SDR_c10

cd05373

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...

4-183

2.12e-23

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187631 [Multi-domain] Cd Length: 238 Bit Score: 93.22 E-value: 2.12e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   4 VCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKA----AAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05373    1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEAllvdIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:cd05373   81 LVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTG----------ATASLRGRAGFAAFA 150

                        170       180
                 ....*....|....*....|....
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRV 183
Cdd:cd05373  151 GAKFALRALAQSMARELGPKGIHV 174

PRK08936

glucose-1-dehydrogenase; Provisional

2-191

2.17e-23

glucose-1-dehydrogenase; Provisional

Pssm-ID: 181585 [Multi-domain] Cd Length: 261 Bit Score: 93.64 E-value: 2.17e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIAR-NLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK08936   7 GKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANDVAEEIkkaGGEAIAVKGDVTVESDVVNLIQTAVKEFGTL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGHRREML-----LHkrsivglkg 151
Cdd:PRK08936  87 DVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHdIKGNIINMSSVHEQIpwplfVH--------- 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 578809569 152 nsgqsvYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK08936 158 ------YAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAI 191

DHRS6_like_SDR_c

cd05368

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...

3-191

2.42e-23

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).

Pssm-ID: 187626 [Multi-domain] Cd Length: 241 Bit Score: 93.30 E-value: 2.42e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRlaVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELekhlGRVNFLVN 82
Cdd:cd05368    3 KVALITAAAQGIGRAIALAFAREGAN--VIATDINEEKLKELERGPGITTRVLDVTDKEQVAALAKEE----GRIDVLFN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVG-LKGNSGQSVYSAS 161
Cdd:cd05368   77 CAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMS----------SVASsIKGVPNRFVYSTT 146

                        170       180       190
                 ....*....|....*....|....*....|
gi 578809569 162 KGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:cd05368  147 KAAVIGLTKSVAADFAQQGIRCNAICPGTV 176

11beta-HSD1_like_SDR_c

cd05332

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...

1-188

2.47e-23

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187593 [Multi-domain] Cd Length: 257 Bit Score: 93.42 E-value: 2.47e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL--GGDHLAFSC--DVAKEHDVQNTFEELEKHLGR 76
Cdd:cd05332    2 QGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECleLGAPSPHVVplDMSDLEDAEQVVEEALKLFGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:cd05332   82 LDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVS----------SIAGKIGVPFRT 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05332  152 AYAASKHALQGFFDSLRAELSEPNISVTVVCP 183

PRK08226

SDR family oxidoreductase UcpA;

3-188

3.84e-23

SDR family oxidoreductase UcpA;

Pssm-ID: 181305 [Multi-domain] Cd Length: 263 Bit Score: 93.33 E-value: 3.84e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA--GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK08226   7 KTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADelCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGRIDIL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVG-LKGNSGQSVYS 159
Cdd:PRK08226  87 VNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMS----------SVTGdMVADPGETAYA 156

                        170       180
                 ....*....|....*....|....*....
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08226 157 LTKAAIVGLTKSLAVEYAQSGIRVNAICP 185

PRK06179

short chain dehydrogenase; Provisional

3-188

6.44e-23

short chain dehydrogenase; Provisional

Pssm-ID: 235725 [Multi-domain] Cd Length: 270 Bit Score: 92.66 E-value: 6.44e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDhlafsCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK06179   5 KVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIPGVELLE-----LDVTDDASVQAAVDEVIARAGRIDVLVN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:PRK06179  80 NAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINIS----------SVLGFLPAPYMALYAASK 149

                        170       180
                 ....*....|....*....|....*.
gi 578809569 163 GGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06179 150 HAVEGYSESLDHEVRQFGIRVSLVEP 175

PRK06914

SDR family oxidoreductase;

1-188

9.48e-23

SDR family oxidoreductase;

Pssm-ID: 180744 [Multi-domain] Cd Length: 280 Bit Score: 92.39 E-value: 9.48e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAK-----AAAGDLGGDHLAFSCDVAKEHDVQNtFEELEKHLG 75
Cdd:PRK06914   2 NKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQEnllsqATQLNLQQNIKVQQLDVTDQNSIHN-FQLVLKEIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:PRK06914  81 RIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINIS----------SISGRVGFPGL 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06914 151 SPYVSSKYALEGFSESLRLELKPFGIDVALIEP 183

SDR_c5

cd05346

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...

9-188

1.01e-22

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187604 [Multi-domain] Cd Length: 249 Bit Score: 91.57 E-value: 1.01e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH----LAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAA 84
Cdd:cd05346    7 GASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFpvkvLPLQLDVSDRESIEAALENLPEEFRDIDILVNNA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  85 GINRdGL--LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:cd05346   87 GLAL-GLdpAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLG----------SIAGRYPYAGGNVYCATK 155

                        170       180
                 ....*....|....*....|....*.
gi 578809569 163 GGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05346  156 AAVRQFSLNLRKDLIGTGIRVTNIEP 181

DHB_DH-like_SDR_c

cd08937

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...

2-188

1.18e-22

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187642 [Multi-domain] Cd Length: 256 Bit Score: 91.82 E-value: 1.18e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG--DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd08937    4 GKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAEilAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVDV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGinrdGLLVR-----TKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNsg 154
Cdd:cd08937   84 LINNVG----GTIWAkpyehYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVS----------SIATRGIY-- 147

                        170       180       190
                 ....*....|....*....|....*....|....
gi 578809569 155 QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08937  148 RIPYSAAKGGVNALTASLAFEHARDGIRVNAVAP 181

cyclohexanol_reductase_SDR_c

cd05330

cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...

2-192

1.46e-22

cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol reductases,including (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) reductase of Corynebacterium aquaticum, catalyze the reversible oxidoreduction of hydroxycyclohexanone derivatives. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187591 [Multi-domain] Cd Length: 257 Bit Score: 91.43 E-value: 1.46e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd05330    3 DKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALleiapDAEVLLIKADVSDEAQVEAYVDATVEQFGR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGIN-RDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:cd05330   83 IDGFFNNAGIEgKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTA----------SVGGIRGVGNQ 152

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTIL 192
Cdd:cd05330  153 SGYAAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAIL 189

TR_SDR_c

cd05329

tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...

7-192

1.46e-22

tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup includes TR-I and TR-II; these proteins are members of the SDR family. TRs catalyze the NADPH-dependent reductions of the 3-carbonyl group of tropinone, to a beta-hydroxyl group. TR-I and TR-II produce different stereoisomers from tropinone, TR-I produces tropine (3alpha-hydroxytropane), and TR-II, produces pseudotropine (sigma-tropine, 3beta-hydroxytropane). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187590 [Multi-domain] Cd Length: 251 Bit Score: 91.36 E-value: 1.46e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHL-GRVNFLVN 82
Cdd:cd05329   11 VTGGTKGIGYAIVEELAGLGAEVYTCARNqkeLDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFgGKLNILVN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:cd05329   91 NAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFIS----------SVAGVIAVPSGAPYGATK 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 578809569 163 GGLVGFSRALAKEVARKKIRVNVVAPVTIL 192
Cdd:cd05329  161 GALNQLTRSLACEWAKDNIRVNAVAPWVIA 190

PRK06114

SDR family oxidoreductase;

2-188

1.52e-22

SDR family oxidoreductase;

Pssm-ID: 180408 [Multi-domain] Cd Length: 254 Bit Score: 91.38 E-value: 1.52e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGD----LGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK06114   8 GQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETAEhieaAGRRAIQIAADVTSKADLRAAVARTEAELGAL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINRdgllvRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGN 152
Cdd:PRK06114  88 TLAVNAAGIAN-----ANPAEEMEEEqwqtvMDINLTGVFLSCQAEARAMLENGGGSIVNIA----------SMSGIIVN 152

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 578809569 153 SG--QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06114 153 RGllQAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISP 190

17beta-HSD1_like_SDR_c

cd05356

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...

2-188

1.80e-22

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187614 [Multi-domain] Cd Length: 239 Bit Score: 90.74 E-value: 1.80e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH----LAFSCDVAKEHDVqntFEELEKHLGR- 76
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYgvetKTIAADFSAGDDI---YERIEKELEGl 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 -VNFLVNAAGINRD--GLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNS 153
Cdd:cd05356   78 dIGILVNNVGISHSipEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNIS----------SFAGLIPTP 147

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 578809569 154 GQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05356  148 LLATYSASKAFLDFFSRALYEEYKSQGIDVQSLLP 182

PRK07890

short chain dehydrogenase; Provisional

2-188

2.50e-22

short chain dehydrogenase; Provisional

Pssm-ID: 181159 [Multi-domain] Cd Length: 258 Bit Score: 90.79 E-value: 2.50e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIAR---NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07890   5 GKVVVVSGVGPGLGRTLAVRAARAGADVVLAARtaeRLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERFGRVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVN-AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQqGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK07890  85 ALVNnAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAES-GGSIVMIN----------SMVLRHSQPKYGA 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809569 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07890 154 YKMAKGALLAASQSLATELGPQGIRVNSVAP 184

PRK08265

short chain dehydrogenase; Provisional

2-188

2.77e-22

short chain dehydrogenase; Provisional

Pssm-ID: 236209 [Multi-domain] Cd Length: 261 Bit Score: 90.84 E-value: 2.77e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK08265   6 GKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFGRVDILV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 N-AAGINRDGLlvRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:PRK08265  86 NlACTYLDDGL--ASSRADWLAALDVNLVSAAMLAQAAHPHLA-RGGGAIVNFT----------SISAKFAQTGRWLYPA 152

                        170       180
                 ....*....|....*....|....*...
gi 578809569 161 SKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08265 153 SKAAIRQLTRSMAMDLAPDGIRVNSVSP 180

mannonate_red_SDR_c

cd08935

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...

2-188

2.95e-22

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187640 [Multi-domain] Cd Length: 271 Bit Score: 90.98 E-value: 2.95e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:cd08935    5 NKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEItalGGRAIALAADVLDRASLERAREEIVAQFGTVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINR-------DGLLVRTKT-------EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkr 144
Cdd:cd08935   85 ILINGAGGNHpdattdpEHYEPETEQnffdldeEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINIS---------- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 578809569 145 SIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08935  155 SMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAP 198

PRK07856

SDR family oxidoreductase;

2-188

3.77e-22

SDR family oxidoreductase;

Pssm-ID: 236116 [Multi-domain] Cd Length: 252 Bit Score: 90.38 E-value: 3.77e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNlegAKAAAGDLGGDHLAfsCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK07856   6 GRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRR---APETVDGRPAEFHA--ADVRDPDQVAALVDAIVERHGRLDVLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:PRK07856  81 NNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQpGGGSIVNIG----------SVSGRRPSPGTAAYGA 150

                        170       180
                 ....*....|....*....|....*...
gi 578809569 161 SKGGLVGFSRALAKEVArKKIRVNVVAP 188
Cdd:PRK07856 151 AKAGLLNLTRSLAVEWA-PKVRVNAVVV 177

SDH_SDR_c

cd05363

Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...

2-188

5.29e-22

Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter sphaeroides SDH, and other SDHs. SDH preferentially interconverts D-sorbitol (D-glucitol) and D-fructose, but also interconverts L-iditol/L-sorbose and galactitol/D-tagatose. SDH is NAD-dependent and is a dimeric member of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187621 [Multi-domain] Cd Length: 254 Bit Score: 89.98 E-value: 5.29e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:cd05363    3 GKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWGSIDILV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:cd05363   83 NNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMA----------SQAGRRGEALVGVYCA 152

                        170       180
                 ....*....|....*....|....*...
gi 578809569 161 SKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05363  153 TKAAVISLTQSAGLNLIRHGINVNAIAP 180

benD

PRK12823

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional

2-188

6.41e-22

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional

Pssm-ID: 183772 [Multi-domain] Cd Length: 260 Bit Score: 89.62 E-value: 6.41e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN--LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK12823   8 GKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSelVHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRIDV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGinrdGLlVRTK------TEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHrremlLHKRSIvglkgns 153
Cdd:PRK12823  88 LINNVG----GT-IWAKpfeeyeEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSS-----IATRGI------- 150

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 578809569 154 GQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12823 151 NRVPYSAAKGGVNALTASLAFEYAEHGIRVNAVAP 185

carb_red_PTCR-like_SDR_c

cd05324

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...

3-188

6.78e-22

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187585 [Multi-domain] Cd Length: 225 Bit Score: 88.83 E-value: 6.78e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKG-YRLAVIARNLEGAKAAAGDLGGDHL---AFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGpGTVILTARDVERGQAAVEKLRAEGLsvrFHQLDVTDDASIEAAADFVEEKYGGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRDGLLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGlkgnSGQSV 157
Cdd:cd05324   81 ILVNNAGIAFKGFDDSTPTREQAREtMKTNFFGTVDVTQALLPLLKKSPAGRIVNVS----------SGLG----SLTSA 146

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809569 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05324  147 YGVSKAALNALTRILAKELKETGIKVNACCP 177

PRK07774

SDR family oxidoreductase;

2-188

7.48e-22

SDR family oxidoreductase;

Pssm-ID: 236094 [Multi-domain] Cd Length: 250 Bit Score: 89.42 E-value: 7.48e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07774   6 DKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIvadGGTAIAVQVDVSDPDSAKAMADATVSAFGGID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRD---GLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNvghrremllhkRSIVGLKGNSGq 155
Cdd:PRK07774  86 YLVNNAAIYGGmklDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVN-----------QSSTAAWLYSN- 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 156 sVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07774 154 -FYGLAKVGLNGLTQQLARELGGMNIRVNAIAP 185

PRK09242

SDR family oxidoreductase;

2-188

1.72e-21

SDR family oxidoreductase;

Pssm-ID: 181721 [Multi-domain] Cd Length: 257 Bit Score: 88.65 E-value: 1.72e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK09242   9 GQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELaeefpEREVHGLAADVSDDEDRRAILDWVEDHWDG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGINrdgllVRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKG 151
Cdd:PRK09242  89 LHILVNNAGGN-----IRKAAIDYTEDewrgiFETNLFSAFELSRYAHPLLKQHASSAIVNIG----------SVSGLTH 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 578809569 152 NSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK09242 154 VRSGAPYGMTKAALLQMTRNLAVEWAEDGIRVNAVAP 190

ChcA_like_SDR_c

cd05359

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...

7-188

2.21e-21

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187617 [Multi-domain] Cd Length: 242 Bit Score: 88.18 E-value: 2.21e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAGD---LGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05359    3 VTGGSRGIGKAIALRLAERGADVVInYRKSKDAAAEVAAEieeLGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDVLVS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 --AAGINRDglLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:cd05359   83 naAAGAFRP--LSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAIS----------SLGSIRALPNYLAVGT 150

                        170       180
                 ....*....|....*....|....*...
gi 578809569 161 SKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05359  151 AKAALEALVRYLAVELGPRGIRVNAVSP 178

PRK07097

gluconate 5-dehydrogenase; Provisional

3-188

4.54e-21

gluconate 5-dehydrogenase; Provisional

Pssm-ID: 235933 [Multi-domain] Cd Length: 265 Bit Score: 87.81 E-value: 4.54e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV---IARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07097  11 KIALITGASYGIGFAIAKAYAKAGATIVFndiNQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVGVIDI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK07097  91 LVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINIC----------SMMSELGRETVSAYA 160

                        170       180
                 ....*....|....*....|....*....
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07097 161 AAKGGLKMLTKNIASEYGEANIQCNGIGP 189

PRK07478

short chain dehydrogenase; Provisional

2-188

5.26e-21

short chain dehydrogenase; Provisional

Pssm-ID: 180993 [Multi-domain] Cd Length: 254 Bit Score: 87.29 E-value: 5.26e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07478   6 GKVAIITGASSGIGRAAAKLFAREGAKVVVGARRqaeLDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERFGGLD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRDGLLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMIQQQGGSIVN----VGHRremllhkrsiVGLKGNS 153
Cdd:PRK07478  86 IAFNNAGTLGEMGPVAEMSLEGWREtLATNLTSAFLGAKHQIPAMLARGGGSLIFtstfVGHT----------AGFPGMA 155

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 578809569 154 gqsVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07478 156 ---AYAASKAGLIGLTQVLAAEYGAQGIRVNALLP 187

DH-DHB-DH_SDR_c

cd05331

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...

7-188

6.52e-21

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187592 [Multi-domain] Cd Length: 244 Bit Score: 86.75 E-value: 6.52e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRlaVIARNLEGAKAAAGdlgGDHL-AFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:cd05331    3 VTGAAQGIGRAVARHLLQAGAT--VIALDLPFVLLLEY---GDPLrLTPLDVADAAAVREVCSRLLAEHGPIDALVNCAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  86 INRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGL 165
Cdd:cd05331   78 VLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVA----------SNAAHVPRISMAAYGASKAAL 147

                        170       180
                 ....*....|....*....|...
gi 578809569 166 VGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05331  148 ASLSKCLGLELAPYGVRCNVVSP 170

PRK07831

SDR family oxidoreductase;

13-188

6.54e-21

SDR family oxidoreductase;

Pssm-ID: 236110 [Multi-domain] Cd Length: 262 Bit Score: 87.01 E-value: 6.54e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  13 GIGRAVAQLMARKGYRLAVI---ARNL-EGAKAAAGDLGGDHL-AFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGIN 87
Cdd:PRK07831  29 GIGSATARRALEEGARVVISdihERRLgETADELAAELGLGRVeAVVCDVTSEAQVDALIDAAVERLGRLDVLVNNAGLG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  88 RDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMI-QQQGGSIVNvghrremllhKRSIVGLKGNSGQSVYSASKGGLV 166
Cdd:PRK07831 109 GQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRaRGHGGVIVN----------NASVLGWRAQHGQAHYAAAKAGVM 178

                        170       180
                 ....*....|....*....|..
gi 578809569 167 GFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07831 179 ALTRCSALEAAEYGVRINAVAP 200

SDR_c9

cd08931

classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...

6-188

6.72e-21

classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187636 [Multi-domain] Cd Length: 227 Bit Score: 86.35 E-value: 6.72e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   6 AVF--GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHL-AFSCDVAKEHDVQNTFEEL-EKHLGRVNFLV 81
Cdd:cd08931    2 AIFitGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGAENVvAGALDVTDRAAWAAALADFaAATGGRLDALF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSAS 161
Cdd:cd08931   82 NNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTA----------SSSAIYGQPDLAVYSAT 151

                        170       180
                 ....*....|....*....|....*..
gi 578809569 162 KGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08931  152 KFAVRGLTEALDVEWARHGIRVADVWP 178

PRK12743

SDR family oxidoreductase;

1-191

7.13e-21

SDR family oxidoreductase;

Pssm-ID: 237187 [Multi-domain] Cd Length: 256 Bit Score: 87.01 E-value: 7.13e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVI-ARNLEGAKAAAGD---LGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK12743   1 MAQVAIVTASDSGIGKACALLLAQQGFDIGITwHSDEEGAKETAEEvrsHGVRAEIRQLDLSDLPEGAQALDKLIQRLGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGHRREmllHKRSIvglkgnsGQ 155
Cdd:PRK12743  81 IDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQgQGGRIINITSVHE---HTPLP-------GA 150

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK12743 151 SAYTAAKHALGGLTKAMALELVEHGILVNAVAPGAI 186

PRK08220

2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated

3-188

7.62e-21

2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated

Pssm-ID: 236190 [Multi-domain] Cd Length: 252 Bit Score: 86.86 E-value: 7.62e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKaaagdlgGDHLA-FSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK08220   9 KTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQE-------DYPFAtFVLDVSDAAAVAQVCQRLLAETGPLDVLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGH------RREMllhkrsivglkgnsgq 155
Cdd:PRK08220  82 NAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSnaahvpRIGM---------------- 145

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08220 146 AAYGASKAALTSLAKCVGLELAPYGVRCNVVSP 178

HBDH_SDR_c

cd08940

d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...

1-188

8.26e-21

d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187644 [Multi-domain] Cd Length: 258 Bit Score: 86.73 E-value: 8.26e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGyrlAVIARNLEGAKA--------AAGDLGGDHLAFSCDVAKEHDVQNTFEELEK 72
Cdd:cd08940    1 KGKVALVTGSTSGIGLGIARALAAAG---ANIVLNGFGDAAeieavragLAAKHGVKVLYHGADLSKPAAIEDMVAYAQR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  73 HLGRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGN 152
Cdd:cd08940   78 QFGGVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIA----------SVHGLVAS 147

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 578809569 153 SGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08940  148 ANKSAYVAAKHGVVGLTKVVALETAGTGVTCNAICP 183

PRK08267

SDR family oxidoreductase;

6-188

8.41e-21

SDR family oxidoreductase;

Pssm-ID: 236210 [Multi-domain] Cd Length: 260 Bit Score: 86.92 E-value: 8.41e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   6 AVF--GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHL-AFSCDVAKEHDVQNTFEELEKHL-GRVNFLV 81
Cdd:PRK08267   3 SIFitGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAGNAwTGALDVTDRAAWDAALADFAAATgGRLDVLF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSAS 161
Cdd:PRK08267  83 NNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTS----------SASAIYGQPGLAVYSAT 152

                        170       180
                 ....*....|....*....|....*..
gi 578809569 162 KGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08267 153 KFAVRGLTEALDLEWRRHGIRVADVMP 179

PRK08063

enoyl-[acyl-carrier-protein] reductase FabL;

1-187

1.23e-20

enoyl-[acyl-carrier-protein] reductase FabL;

Pssm-ID: 236145 [Multi-domain] Cd Length: 250 Bit Score: 86.31 E-value: 1.23e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVI-ARNLEGAKAAAGD---LGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK08063   3 SGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEieaLGRKALAVKANVGDVEKIKEMFAQIDEEFGR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVN--AAGINRDGLLVRTKTEDMVsqLHTNLLGSMLTCKAAMRTMIQQQGGSIVNV---GHRRemLLHKRSIVGlkg 151
Cdd:PRK08063  83 LDVFVNnaASGVLRPAMELEESHWDWT--MNINAKALLFCAQEAAKLMEKVGGGKIISLsslGSIR--YLENYTTVG--- 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 578809569 152 nsgqsvysASKGGLVGFSRALAKEVARKKIRVNVVA 187
Cdd:PRK08063 156 --------VSKAALEALTRYLAVELAPKGIAVNAVS 183

PRK06935

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;

3-188

1.56e-20

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;

Pssm-ID: 180761 [Multi-domain] Cd Length: 258 Bit Score: 85.94 E-value: 1.56e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIA--RNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK06935  16 KVAIVTGGNTGLGQGYAVALAKAGADIIITThgTNWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKIDIL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:PRK06935  96 VNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIA----------SMLSFQGGKFVPAYTA 165

                        170       180
                 ....*....|....*....|....*...
gi 578809569 161 SKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06935 166 SKHGVAGLTKAFANELAAYNIQVNAIAP 193

PRK07062

SDR family oxidoreductase;

2-184

1.70e-20

SDR family oxidoreductase;

Pssm-ID: 180818 [Multi-domain] Cd Length: 265 Bit Score: 86.25 E-value: 1.70e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH-----LAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK07062   8 GRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFpgarlLAARCDVLDEADVAAFAAAVEARFGG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:PRK07062  88 VDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVN----------SLLALQPEPHMV 157

                        170       180
                 ....*....|....*....|....*...
gi 578809569 157 VYSASKGGLVGFSRALAKEVARKKIRVN 184
Cdd:PRK07062 158 ATSAARAGLLNLVKSLATELAPKGVRVN 185

PRK07201

SDR family oxidoreductase;

3-181

1.78e-20

SDR family oxidoreductase;

Pssm-ID: 235962 [Multi-domain] Cd Length: 657 Bit Score: 88.47 E-value: 1.78e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07201 372 KVVLITGASSGIGRATAIKVAEAGATVFLVARNgeaLDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHGHVDY 451

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGinRDgllVRTKTEDMVSQLH-------TNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkrSIVGLKGN 152
Cdd:PRK07201 452 LVNNAG--RS---IRRSVENSTDRFHdyertmaVNYFGAVRLILGLLPHMRERRFGHVVNV-----------SSIGVQTN 515

                        170       180       190
                 ....*....|....*....|....*....|
gi 578809569 153 SGQ-SVYSASKGGLVGFSRALAKEVARKKI 181
Cdd:PRK07201 516 APRfSAYVASKAALDAFSDVAASETLSDGI 545

Mgc4172-like_SDR_c

cd05343

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...

2-188

2.98e-20

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187601 [Multi-domain] Cd Length: 250 Bit Score: 85.26 E-value: 2.98e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd05343    6 GRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECqsagYPTLFPYQCDLSNEEQILSMFSAIRTQHQGV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ--QGGSIVNV----GHRremllhkrsivgLKG 151
Cdd:cd05343   86 DVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERnvDDGHIINInsmsGHR------------VPP 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 578809569 152 NSGQSVYSASKGGLVGFSRALAKEV--ARKKIRVNVVAP 188
Cdd:cd05343  154 VSVFHFYAATKHAVTALTEGLRQELreAKTHIRATSISP 192

PRK07069

short chain dehydrogenase; Validated

7-191

3.95e-20

short chain dehydrogenase; Validated

Pssm-ID: 180822 [Multi-domain] Cd Length: 251 Bit Score: 84.76 E-value: 3.95e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARN-LEGAKAAAGDLGGDH-----LAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK07069   4 ITGAAGGLGRAIARRMAEQGAKVFLTDINdAAGLDAFAAEINAAHgegvaFAAVQDVTDEAQWQALLAQAADAMGGLSVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:PRK07069  84 VNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNIS----------SVAAFKAEPDYTAYNA 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 161 SKGGLVGFSRALAKEVARKK--IRVNVVAPVTI 191
Cdd:PRK07069 154 SKAAVASLTKSIALDCARRGldVRCNSIHPTFI 186

fabG

PRK06077

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

2-188

6.36e-20

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

Pssm-ID: 235693 [Multi-domain] Cd Length: 252 Bit Score: 84.39 E-value: 6.36e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIAR----NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK06077   6 DKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKkraeEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRYGVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK06077  86 DILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIA----------SVAGIRPAYGLSI 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809569 158 YSASKGGLVGFSRALAKEVArKKIRVNVVAP 188
Cdd:PRK06077 154 YGAMKAAVINLTKYLALELA-PKIRVNAIAP 183

PRK08085

gluconate 5-dehydrogenase; Provisional

9-188

9.13e-20

gluconate 5-dehydrogenase; Provisional

Pssm-ID: 181225 [Multi-domain] Cd Length: 254 Bit Score: 84.04 E-value: 9.13e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:PRK08085  16 GSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLrqeGIKAHAAPFNVTHKQEVEAAIEHIEKDIGPIDVLINNAG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  86 INRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREMLlhkrsivglkGNSGQSVYSASKGGL 165
Cdd:PRK08085  96 IQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSEL----------GRDTITPYAASKGAV 165

                        170       180
                 ....*....|....*....|...
gi 578809569 166 VGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08085 166 KMLTRGMCVELARHNIQVNGIAP 188

DltE

COG3967

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...

9-172

1.30e-19

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];

Pssm-ID: 443167 [Multi-domain] Cd Length: 246 Bit Score: 83.29 E-value: 1.30e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHlAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGINR 88
Cdd:COG3967   12 GGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANPGLH-TIVLDVADPASIAALAEQVTAEFPDLNVLINNAGIMR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  89 DGLLVRTKT--EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLV 166
Cdd:COG3967   91 AEDLLDEAEdlADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVS----------SGLAFVPLAVTPTYSATKAALH 160


                 ....*.
gi 578809569 167 GFSRAL 172
Cdd:COG3967  161 SYTQSL 166

PRK12745

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

1-188

2.18e-19

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

Pssm-ID: 237188 [Multi-domain] Cd Length: 256 Bit Score: 83.09 E-value: 2.18e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIAR----NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK12745   1 MRPVALVTGGRRGIGLGIARALAAAGFDLAINDRpddeELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGI---NRDGLLvRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQG------GSIVNVGhrremllhKRSIV 147
Cdd:PRK12745  81 IDCLVNNAGVgvkVRGDLL-DLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphRSIVFVS--------SVNAI 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 578809569 148 GLKGNSGQsvYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12745 152 MVSPNRGE--YCISKAGLSMAAQLFAARLAEEGIGVYEVRP 190

PKR_SDR_c

cd08945

Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...

3-188

2.25e-19

Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR with a characteristic NAD-binding pattern and active site tetrad. Aromatic polyketides include various aromatic compounds of pharmaceutical interest. Polyketide KR, part of the type II polyketide synthase (PKS) complex, is comprised of stand-alone domains that resemble the domains found in fatty acid synthase and multidomain type I PKS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187649 [Multi-domain] Cd Length: 258 Bit Score: 82.97 E-value: 2.25e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd08945    4 EVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELreaGVEADGRTCDVRSVPEIEALVAAAVARYGPIDV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRT--MIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:cd08945   84 LVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIA----------STGGKQGVVHAAP 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809569 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08945  154 YSASKHGVVGFTKALGLELARTGITVNAVCP 184

PRK07832

SDR family oxidoreductase;

3-188

3.01e-19

SDR family oxidoreductase;

Pssm-ID: 181139 [Multi-domain] Cd Length: 272 Bit Score: 82.78 E-value: 3.01e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGD---LGG---DHLAFscDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADaraLGGtvpEHRAL--DISDYDAVAAFAADIHAAHGS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:PRK07832  79 MDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAgRGGHLVNVS----------SAAGLVALPWH 148

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07832 149 AAYSASKFGLRGLSEVLRFDLARHGIGVSVVVP 181

fabG

PRK06550

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

1-188

5.16e-19

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

Pssm-ID: 180617 [Multi-domain] Cd Length: 235 Bit Score: 81.55 E-value: 5.16e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRlaVIARNLEGAKAAAGDLGgdhlafscdvAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK06550   4 MTKTVLITGAASGIGLAQARAFLAQGAQ--VYGVDKQDKPDLSGNFH----------FLQLDLSDDLEPLFDWVPSVDIL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGInRDGL--LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:PRK06550  72 CNTAGI-LDDYkpLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMC----------SIASFVAGGGGAAY 140

                        170       180       190
                 ....*....|....*....|....*....|
gi 578809569 159 SASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06550 141 TASKHALAGFTKQLALDYAKDGIQVFGIAP 170

PRK07775

SDR family oxidoreductase;

7-196

7.91e-19

SDR family oxidoreductase;

Pssm-ID: 181113 [Multi-domain] Cd Length: 274 Bit Score: 81.72 E-value: 7.91e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA 83
Cdd:PRK07775  15 VAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIradGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEVLVSG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  84 AGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKG 163
Cdd:PRK07775  95 AGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVG----------SDVALRQRPHMGAYGAAKA 164

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 578809569 164 GLVGFSRALAKEVARKKIRVNVVAP---VTILVWSL 196
Cdd:PRK07775 165 GLEAMVTNLQMELEGTGVRASIVHPgptLTGMGWSL 200

PRK07791

short chain dehydrogenase; Provisional

3-189

8.98e-19

short chain dehydrogenase; Provisional

Pssm-ID: 236099 [Multi-domain] Cd Length: 286 Bit Score: 81.64 E-value: 8.98e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV--IARNLEGAKAAAG----------DLGGDHLAFSCDVAKEHDVQNTFEEL 70
Cdd:PRK07791   7 RVVIVTGAGGGIGRAHALAFAAEGARVVVndIGVGLDGSASGGSaaqavvdeivAAGGEAVANGDDIADWDGAANLVDAA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  71 EKHLGRVNFLVNAAGINRDGLLVRTKTE--DMVSQLHtnLLGSMLTCK-AAMRTMIQQQGGSIVNVghrreMLLHKRSIV 147
Cdd:PRK07791  87 VETFGGLDVLVNNAGILRDRMIANMSEEewDAVIAVH--LKGHFATLRhAAAYWRAESKAGRAVDA-----RIINTSSGA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 578809569 148 GLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPV 189
Cdd:PRK07791 160 GLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPA 201

PLN02253

xanthoxin dehydrogenase

3-191

9.95e-19

xanthoxin dehydrogenase

Pssm-ID: 177895 [Multi-domain] Cd Length: 280 Bit Score: 81.79 E-value: 9.95e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLA--FSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PLN02253  19 KVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNVcfFHCDVTVEDDVSRAVDFTVDKFGTLDIM 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGINRDGL--LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:PLN02253  99 VNNAGLTGPPCpdIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLC----------SVASAIGGLGPHAY 168

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 159 SASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PLN02253 169 TGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAV 201

PRK06523

short chain dehydrogenase; Provisional

7-188

1.28e-18

short chain dehydrogenase; Provisional

Pssm-ID: 180604 [Multi-domain] Cd Length: 260 Bit Score: 81.10 E-value: 1.28e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNlegakaAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGI 86
Cdd:PRK06523  14 VTGGTKGIGAATVARLLEAGARVVTTARS------RPDDLPEGVEFVAADLTTAEGCAAVARAVLERLGGVDILVHVLGG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  87 NR---DGLLVRTKtEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGH-RREMLLHKRSIVglkgnsgqsvYSASK 162
Cdd:PRK06523  88 SSapaGGFAALTD-EEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSiQRRLPLPESTTA----------YAAAK 156

                        170       180
                 ....*....|....*....|....*.
gi 578809569 163 GGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06523 157 AALSTYSKSLSKEVAPKGVRVNTVSP 182

PRK05855

SDR family oxidoreductase;

2-188

2.22e-18

SDR family oxidoreductase;

Pssm-ID: 235628 [Multi-domain] Cd Length: 582 Bit Score: 82.34 E-value: 2.22e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAeliRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPD 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK05855 395 IVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERgTGGHIVNVA----------SAAAYAPSRSLPA 464

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809569 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK05855 465 YATSKAAVLMLSECLRAELAAAGIGVTAICP 495

PRK06139

SDR family oxidoreductase;

2-177

3.78e-18

SDR family oxidoreductase;

Pssm-ID: 235713 [Multi-domain] Cd Length: 330 Bit Score: 80.53 E-value: 3.78e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK06139   7 GAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEecrALGAEVLVVPTDVTDADQVKALATQAASFGGRID 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNvghrreMLlhkrSIVGLKGNSGQSVY 158
Cdd:PRK06139  87 VWVNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFIN------MI----SLGGFAAQPYAAAY 156

                        170
                 ....*....|....*....
gi 578809569 159 SASKGGLVGFSRALAKEVA 177
Cdd:PRK06139 157 SASKFGLRGFSEALRGELA 175

PRK06128

SDR family oxidoreductase;

9-188

5.72e-18

SDR family oxidoreductase;

Pssm-ID: 180413 [Multi-domain] Cd Length: 300 Bit Score: 79.90 E-value: 5.72e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA-----GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA 83
Cdd:PRK06128  62 GADSGIGRATAIAFAREGADIALNYLPEEEQDAAEvvqliQAEGRKAVALPGDLKDEAFCRQLVERAVKELGGLDILVNI 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  84 AG---INRDglLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:PRK06128 142 AGkqtAVKD--IADITTEQFDATFKTNVYAMFWLCKAAIPHL--PPGASIINTG----------SIQSYQPSPTLLDYAS 207

                        170       180
                 ....*....|....*....|....*...
gi 578809569 161 SKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06128 208 TKAAIVAFTKALAKQVAEKGIRVNAVAP 235

PRK07577

SDR family oxidoreductase;

2-188

8.67e-18

SDR family oxidoreductase;

Pssm-ID: 181044 [Multi-domain] Cd Length: 234 Bit Score: 78.23 E-value: 8.67e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNlegakaAAGDLGGDHLAfsCDVAKEHDVQNTFEELEKHlGRVNFLV 81
Cdd:PRK07577   3 SRTVLVTGATKGIGLALSLRLANLGHQVIGIARS------AIDDFPGELFA--CDLADIEQTAATLAQINEI-HPVDAIV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhKRSIVGLKgnsGQSVYSAS 161
Cdd:PRK07577  74 NNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNIC--------SRAIFGAL---DRTSYSAA 142

                        170       180
                 ....*....|....*....|....*..
gi 578809569 162 KGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07577 143 KSALVGCTRTWALELAEYGITVNAVAP 169

RhlG_SDR_c

cd08942

RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...

2-188

9.36e-18

RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is an SDR-family beta-ketoacyl reductase involved in Rhamnolipid biosynthesis. RhlG is similar to but distinct from the FabG family of beta-ketoacyl-acyl carrier protein (ACP) of type II fatty acid synthesis. RhlG and related proteins are classical SDRs, with a canonical active site tetrad and glycine-rich NAD(P)-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187646 [Multi-domain] Cd Length: 250 Bit Score: 78.68 E-value: 9.36e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG--GDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd08942    6 GKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSayGECIAIPADLSSEEGIEALVARVAERSDRLDV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLL--VRTKTEDMVSQLHTNllgSMLTCKAAMRTMIQQQG-----GSIVNVGhrremllhkrSIVGLKGN 152
Cdd:cd08942   86 LVNNAGATWGAPLeaFPESGWDKVMDINVK---SVFFLTQALLPLLRAAAtaenpARVINIG----------SIAGIVVS 152

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 578809569 153 SGQSV-YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08942  153 GLENYsYGASKAAVHQLTRKLAKELAGEHITVNAIAP 189

A3DFK9-like_SDR_c

cd09761

Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...

3-188

1.11e-17

Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, classical (c) SDRs; This subgroup includes a putative carbohydrate or polyalcohol metabolizing SDR (A3DFK9) from Clostridium thermocellum. Its members have a TGXXXGXG classical-SDR glycine-rich NAD-binding motif, and some have a canonical SDR active site tetrad (A3DFK9 lacks the upstream Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187662 [Multi-domain] Cd Length: 242 Bit Score: 78.00 E-value: 1.11e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLaVIARNLEGAKAAAGDLGGDHLAF-SCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:cd09761    2 KVAIVTGGGHGIGKQICLDFLEAGDKV-VFADIDEERGADFAEAEGPNLFFvHGDVADETLVKFVVYAMLEKLGRIDVLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIqQQGGSIVNVGHRRemllhkrsivGLKGNSGQSVYSAS 161
Cdd:cd09761   81 NNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELI-KNKGRIINIASTR----------AFQSEPDSEAYAAS 149

                        170       180
                 ....*....|....*....|....*..
gi 578809569 162 KGGLVGFSRALAKEVARkKIRVNVVAP 188
Cdd:cd09761  150 KGGLVALTHALAMSLGP-DIRVNCISP 175

PRK05872

short chain dehydrogenase; Provisional

2-185

1.13e-17

short chain dehydrogenase; Provisional

Pssm-ID: 235633 [Multi-domain] Cd Length: 296 Bit Score: 78.86 E-value: 1.13e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAF--SCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK05872   9 GKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDRVLtvVADVTDLAAMQAAAEEAVERFGGIDV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIqqqggsivnvgHRREMLLHKRSIVGLKGNSGQSVYS 159
Cdd:PRK05872  89 VVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALI-----------ERRGYVLQVSSLAAFAAAPGMAAYC 157

                        170       180
                 ....*....|....*....|....*.
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNV 185
Cdd:PRK05872 158 ASKAGVEAFANALRLEVAHHGVTVGS 183

CR_SDR_c

cd08936

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...

2-191

1.56e-17

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187641 [Multi-domain] Cd Length: 256 Bit Score: 77.97 E-value: 1.56e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFS---CDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:cd08936   10 NKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTgtvCHVGKAEDRERLVATAVNLHGGVD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINR-DGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:cd08936   90 ILVSNAAVNPfFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVS----------SVAAFHPFPGLGP 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 578809569 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:cd08936  160 YNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLI 193

fabG

PRK07792

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

3-188

1.70e-17

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

Pssm-ID: 181120 [Multi-domain] Cd Length: 306 Bit Score: 78.67 E-value: 1.70e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV--IARNLEGAKAAA--GDLGGDHLAFSCDVAkEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07792  13 KVAVVTGAAAGLGRAEALGLARLGATVVVndVASALDASDVLDeiRAAGAKAVAVAGDIS-QRATADELVATAVGLGGLD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAM---RTMIQQQGGSIVNvghrreMLLHKRSIVGLKGNSGQ 155
Cdd:PRK07792  92 IVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAaywRAKAKAAGGPVYG------RIVNTSSEAGLVGPVGQ 165

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07792 166 ANYGAAKAGITALTLSAARALGRYGVRANAICP 198

7_alpha_HSDH_SDR_c

cd05365

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...

4-192

2.23e-17

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187623 [Multi-domain] Cd Length: 242 Bit Score: 77.22 E-value: 2.23e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   4 VCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGD---LGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:cd05365    1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAiqqAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VN-AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:cd05365   81 VNnAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNIS----------SMSSENKNVRIAAYG 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPVTIL 192
Cdd:cd05365  151 SSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVK 183

BphB-like_SDR_c

cd05348

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...

2-188

2.24e-17

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187606 [Multi-domain] Cd Length: 257 Bit Score: 77.39 E-value: 2.24e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:cd05348    4 GEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGKLDCFI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGINRDGLLVRTKTEDMVSQL-----HTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkrSIVGLKGNSGQS 156
Cdd:cd05348   84 GNAGIWDYSTSLVDIPEEKLDEAfdelfHINVKGYILGAKAALPALYATEGSVIFTV-----------SNAGFYPGGGGP 152

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 157 VYSASKGGLVGFSRALAKEVArKKIRVNVVAP 188
Cdd:cd05348  153 LYTASKHAVVGLVKQLAYELA-PHIRVNGVAP 183

retinol-DH_like_SDR_c_like

cd05327

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...

2-188

7.14e-17

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 212492 [Multi-domain] Cd Length: 269 Bit Score: 76.49 E-value: 7.14e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL----GGDHLAFS-CDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIkketGNAKVEVIqLDLSSLASVRQFAEEFLARFPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGInrdGLLVRTKTED-MVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVG---HRR-----EMLLHKRSiv 147
Cdd:cd05327   81 LDILINNAGI---MAPPRRLTKDgFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSsiaHRAgpidfNDLDLENN-- 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 578809569 148 glKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05327  156 --KEYSPYKAYGQSKLANILFTRELARRLEGTGVTVNALHP 194

PR_SDR_c

cd05357

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...

7-192

8.89e-17

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187615 [Multi-domain] Cd Length: 234 Bit Score: 75.39 E-value: 8.89e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGD----LGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05357    5 VTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQRLKDelnaLRNSAVLVQADLSDFAACADLVAAAFRAFGRCDVLVN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:cd05357   85 NASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINII----------DAMTDRPLTGYFAYCMSK 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 578809569 163 GGLVGFSRALAKEVArKKIRVNVVAPVTIL 192
Cdd:cd05357  155 AALEGLTRSAALELA-PNIRVNGIAPGLIL 183

Tthb094_like_SDR_c

cd11730

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...

7-188

9.62e-17

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 212496 [Multi-domain] Cd Length: 206 Bit Score: 74.87 E-value: 9.62e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGdhLAFSCDVAKEHDVQNTFEElekhLGRVNFLVNAAGI 86
Cdd:cd11730    3 ILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGA--LARPADVAAELEVWALAQE----LGPLDLLVYAAGA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIqqQGGSIVNVGHRREMllhkrsiVGLKGNSGqsvYSASKGGLV 166
Cdd:cd11730   77 ILGKPLARTKPAAWRRILDANLTGAALVLKHALALLA--AGARLVFLGAYPEL-------VMLPGLSA---YAAAKAALE 144

                        170       180
                 ....*....|....*....|..
gi 578809569 167 GFSRALAKEVarKKIRVNVVAP 188
Cdd:cd11730  145 AYVEVARKEV--RGLRLTLVRP 164

PRK06113

7-alpha-hydroxysteroid dehydrogenase; Validated

2-192

1.22e-16

7-alpha-hydroxysteroid dehydrogenase; Validated

Pssm-ID: 135765 [Multi-domain] Cd Length: 255 Bit Score: 75.65 E-value: 1.22e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK06113  11 GKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVdeiQQLGGQAFACRCDITSEQELSALADFALSKLGKVD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRDGLLvRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:PRK06113  91 ILVNNAGGGGPKPF-DMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTIT----------SMAAENKNINMTSY 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 578809569 159 SASKGGLVGFSRALAKEVARKKIRVNVVAPVTIL 192
Cdd:PRK06113 160 ASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAIL 193

PRK08264

SDR family oxidoreductase;

2-183

1.09e-15

SDR family oxidoreductase;

Pssm-ID: 181335 [Multi-domain] Cd Length: 238 Bit Score: 72.61 E-value: 1.09e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRA-VAQLMARKGYRLAVIARNLEGAKaaagDLGGDHLAFSCDVAKEHDVQntfeELEKHLGRVNFL 80
Cdd:PRK08264   6 GKVVLVTGANRGIGRAfVEQLLARGAAKVYAAARDPESVT----DLGPRVVPLQLDVTDPASVA----AAAEAASDVTIL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGINRDGLLVRTKTED-MVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkRSIVGLKGNSGQSVYS 159
Cdd:PRK08264  78 VNNAGIFRTGSLLLEGDEDaLRAEMETNYFGPLAMARAFAPVLAANGGGAIVNV----------LSVLSWVNFPNLGTYS 147

                        170       180
                 ....*....|....*....|....
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRV 183
Cdd:PRK08264 148 ASKAAAWSLTQALRAELAPQGTRV 171

PRK09186

flagellin modification protein A; Provisional

2-192

1.88e-15

flagellin modification protein A; Provisional

Pssm-ID: 236399 [Multi-domain] Cd Length: 256 Bit Score: 72.33 E-value: 1.88e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGD-----HLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK09186   4 GKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEfkskkLSLVELDITDQESLEEFLSKSAEKYGK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAginrdglLVRTKT----------EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSI 146
Cdd:PRK09186  84 IDGAVNCA-------YPRNKDygkkffdvslDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNIS----------SI 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809569 147 VGL--------KGNSGQSV--YSASKGGLVGFSRALAKEVARKKIRVNVVAPVTIL 192
Cdd:PRK09186 147 YGVvapkfeiyEGTSMTSPveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGIL 202

PRK06200

2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional

2-188

3.52e-15

2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional

Pssm-ID: 235739 [Multi-domain] Cd Length: 263 Bit Score: 71.52 E-value: 3.52e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK06200   6 GQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAFGKLDCFV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGINRDGL-LVRTKTEDMVSQL----HTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkrSIVGLKGNSGQS 156
Cdd:PRK06200  86 GNAGIWDYNTsLVDIPAETLDTAFdeifNVNVKGYLLGAKAALPALKASGGSMIFTL-----------SNSSFYPGGGGP 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 157 VYSASKGGLVGFSRALAKEVArKKIRVNVVAP 188
Cdd:PRK06200 155 LYTASKHAVVGLVRQLAYELA-PKIRVNGVAP 185

XR_like_SDR_c

cd05351

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...

2-192

3.97e-15

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).

Pssm-ID: 187609 [Multi-domain] Cd Length: 244 Bit Score: 71.35 E-value: 3.97e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEgakaaagDLggDHLAFSC--------DVAkehDVQNTFEELEKH 73
Cdd:cd05351    7 GKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQA-------DL--DSLVRECpgiepvcvDLS---DWDATEEALGSV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  74 lGRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGhrremllhkrSIVGLKGN 152
Cdd:cd05351   75 -GPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVS----------SQASQRAL 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 578809569 153 SGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTIL 192
Cdd:cd05351  144 TNHTVYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVM 183

BKR_1_SDR_c

cd05337

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...

4-192

5.36e-15

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187596 [Multi-domain] Cd Length: 255 Bit Score: 70.95 E-value: 5.36e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   4 VCAVFGGSRGIGRAVAQLMARKGYRLAVIAR----NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05337    3 VAIVTGASRGIGRAIATELAARGFDIAINDLpdddQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGIN---RDGLLvrTKTEDMVSQL-HTNLLGSMLTCKAAMRTMIQQQGgsivnvghrREMLLHkRSIVGLKGNSGQ 155
Cdd:cd05337   83 LVNNAGIAvrpRGDLL--DLTEDSFDRLiAINLRGPFFLTQAVARRMVEQPD---------RFDGPH-RSIIFVTSINAY 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 578809569 156 SV------YSASKGGLVGFSRALAKEVARKKIRVNVVAPVTIL 192
Cdd:cd05337  151 LVspnrgeYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIH 193

PRK06500

SDR family oxidoreductase;

1-188

8.06e-15

SDR family oxidoreductase;

Pssm-ID: 235816 [Multi-domain] Cd Length: 249 Bit Score: 70.37 E-value: 8.06e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK06500   5 QGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAAQKALAQALAEAFGRLDAV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGINRDGLLVRTkTEDMVSQL-HTNLLGSMLTCKAAMRtmIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK06500  85 FINAGVAKFAPLEDW-DEAMFDRSfNTNVKGPYFLIQALLP--LLANPASIVLNG----------SINAHIGMPNSSVYA 151

                        170       180
                 ....*....|....*....|....*....
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06500 152 ASKAALLSLAKTLSGELLPRGIRVNAVSP 180

PRK07814

SDR family oxidoreductase;

2-196

2.24e-14

SDR family oxidoreductase;

Pssm-ID: 181131 [Multi-domain] Cd Length: 263 Bit Score: 69.42 E-value: 2.24e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07814  10 DQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEqirAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRLD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQG-GSIVNVghrremllhkRSIVGLKGNSGQSV 157
Cdd:PRK07814  90 IVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSGgGSVINI----------SSTMGRLAGRGFAA 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 578809569 158 YSASKGGLVGFSRALAKEVArKKIRVNVVAPVTILVWSL 196
Cdd:PRK07814 160 YGTAKAALAHYTRLAALDLC-PRIRVNAIAPGSILTSAL 197

SDR_c2

cd05370

classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...

7-188

3.22e-14

classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187628 [Multi-domain] Cd Length: 228 Bit Score: 68.49 E-value: 3.22e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHlAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGI 86
Cdd:cd05370   10 ITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPNIH-TIVLDVGDAESVEALAEALLSEYPNLDILINNAGI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  87 --NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGG 164
Cdd:cd05370   89 qrPIDLRDPASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVS----------SGLAFVPMAANPVYCATKAA 158

                        170       180
                 ....*....|....*....|....
gi 578809569 165 LVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05370  159 LHSYTLALRHQLKDTGVEVVEIVP 182

PRK05876

short chain dehydrogenase; Provisional

7-191

3.64e-14

short chain dehydrogenase; Provisional

Pssm-ID: 135637 [Multi-domain] Cd Length: 275 Bit Score: 69.21 E-value: 3.64e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA 83
Cdd:PRK05876  11 ITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLraeGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDVVFSN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  84 AGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGsivnvGHrremLLHKRSIVGLKGNSGQSVYSASKG 163
Cdd:PRK05876  91 AGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTG-----GH----VVFTASFAGLVPNAGLGAYGVAKY 161

                        170       180
                 ....*....|....*....|....*...
gi 578809569 164 GLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK05876 162 GVVGLAETLAREVTADGIGVSVLCPMVV 189

PRK06482

SDR family oxidoreductase;

1-188

5.04e-14

SDR family oxidoreductase;

Pssm-ID: 235813 [Multi-domain] Cd Length: 276 Bit Score: 68.60 E-value: 5.04e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLegakAAAGDLG---GDHL-AFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK06482   1 MSKTWFITGASSGFGRGMTERLLARGDRVAATVRRP----DALDDLKaryGDRLwVLQLDVTDSAAVRAVVDRAFAALGR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:PRK06482  77 IDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVS----------SEGGQIAYPGFS 146

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06482 147 LYHATKWGIEGFVEAVAQEVAPFGIEFTIVEP 178

Lin1944_like_SDR_c

cd11731

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...

7-188

5.65e-14

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 212497 [Multi-domain] Cd Length: 198 Bit Score: 67.22 E-value: 5.65e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNlegakaaagdlGGDHLafsCDVAKEHDVQNTFEElekhLGRVNFLVNAAGI 86
Cdd:cd11731    3 VIGATGTIGLAVAQLLSAHGHEVITAGRS-----------SGDYQ---VDITDEASIKALFEK----VGHFDAIVSTAGD 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLV 166
Cdd:cd11731   65 AEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYL--NDGGSITLTS----------GILAQRPIPGGAAAATVNGALE 132

                        170       180
                 ....*....|....*....|..
gi 578809569 167 GFSRALAKEVARkKIRVNVVAP 188
Cdd:cd11731  133 GFVRAAAIELPR-GIRINAVSP 153

PRK06182

short chain dehydrogenase; Validated

3-188

6.93e-14

short chain dehydrogenase; Validated

Pssm-ID: 180448 [Multi-domain] Cd Length: 273 Bit Score: 68.06 E-value: 6.93e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAgDLGGDHLAFscDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLA-SLGVHPLSL--DVTDEASIKAAVDTIIAEEGRIDVLVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:PRK06182  81 NAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINIS----------SMGGKIYTPLGAWYHATK 150

                        170       180
                 ....*....|....*....|....*.
gi 578809569 163 GGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06182 151 FALEGFSDALRLEVAPFGIDVVVIEP 176

PRK05866

SDR family oxidoreductase;

9-186

7.10e-14

SDR family oxidoreductase;

Pssm-ID: 235631 [Multi-domain] Cd Length: 293 Bit Score: 68.61 E-value: 7.10e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:PRK05866  47 GASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRItraGGDAMAVPCDLSDLDAVDALVADVEKRIGGVDILINNAG 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  86 INrdgllVRTKTEDMVSQLH-------TNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREmllhkrsivgLKGNSGQ-SV 157
Cdd:PRK05866 127 RS-----IRRPLAESLDRWHdvertmvLNYYAPLRLIRGLAPGMLERGDGHIINVATWGV----------LSEASPLfSV 191

                        170       180
                 ....*....|....*....|....*....
gi 578809569 158 YSASKGGLVGFSRALAKEVARKKIRVNVV 186
Cdd:PRK05866 192 YNASKAALSAVSRVIETEWGDRGVHSTTL 220

PRK09135

pteridine reductase; Provisional

1-192

1.03e-13

pteridine reductase; Provisional

Pssm-ID: 181668 [Multi-domain] Cd Length: 249 Bit Score: 67.26 E-value: 1.03e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN-LEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:PRK09135   5 SAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRsAAEADALAAELnalrPGSAAALQADLLDPDALPELVAACVAAFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  76 RVNFLVNAAGinrdgLLVRTKTEDMVSQLHTNLLGSMLtcKA------AMRTMIQQQGGSIVNvghrremllhkrsIVGL 149
Cdd:PRK09135  85 RLDALVNNAS-----SFYPTPLGSITEAQWDDLFASNL--KApfflsqAAAPQLRKQRGAIVN-------------ITDI 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 578809569 150 KGN---SGQSVYSASKGGLVGFSRALAKEVArKKIRVNVVAPVTIL 192
Cdd:PRK09135 145 HAErplKGYPVYCAAKAALEMLTRSLALELA-PEVRVNAVAPGAIL 189

SPR-like_SDR_c

cd05367

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...

4-188

1.28e-13

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187625 [Multi-domain] Cd Length: 241 Bit Score: 66.93 E-value: 1.28e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   4 VCAVFGGSRGIGRAVAQLMARKGY--RLAVIARNLEGAKAAAGDL-GGDHLAF-SCDVAKEHDVQNTFEEL-EKHLGRVN 78
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGSpsVVVLLARSEEPLQELKEELrPGLRVTTvKADLSDAAGVEQLLEAIrKLDGERDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQG-GSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:cd05367   81 LINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkKTVVNVS----------SGAAVNPFKGWGL 150

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809569 158 YSASKGGLVGFSRALAKEvaRKKIRVNVVAP 188
Cdd:cd05367  151 YCSSKAARDMFFRVLAAE--EPDVRVLSYAP 179

PRK08251

SDR family oxidoreductase;

9-188

1.78e-13

SDR family oxidoreductase;

Pssm-ID: 181324 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 1.78e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH-----LAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA 83
Cdd:PRK08251   9 GASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARYpgikvAVAALDVNDHDQVFEVFAEFRDELGGLDRVIVN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  84 AGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSG-QSVYSASK 162
Cdd:PRK08251  89 AGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGSGHLVLIS----------SVSAVRGLPGvKAAYAASK 158

                        170       180
                 ....*....|....*....|....*.
gi 578809569 163 GGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08251 159 AGVASLGEGLRAELAKTPIKVSTIEP 184

PRK06949

SDR family oxidoreductase;

3-188

2.34e-13

SDR family oxidoreductase;

Pssm-ID: 180773 [Multi-domain] Cd Length: 258 Bit Score: 66.71 E-value: 2.34e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK06949  10 KVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIeaeGGAAHVVSLDVTDYQSIKAAVAHAETEAGTIDI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGS--------IVNVGhrremllhkrSIVGLKG 151
Cdd:PRK06949  90 LVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKGAgntkpggrIINIA----------SVAGLRV 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 578809569 152 NSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06949 160 LPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICP 196

PRK07523

gluconate 5-dehydrogenase; Provisional

7-188

2.76e-13

gluconate 5-dehydrogenase; Provisional

Pssm-ID: 236040 [Multi-domain] Cd Length: 255 Bit Score: 66.33 E-value: 2.76e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH-----LAFscDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK07523  15 VTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGlsahaLAF--DVTDHDAVRAAIDAFEAEIGPIDILV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAGINRdgllvRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREMLlhkrsivglkGNSGQS 156
Cdd:PRK07523  93 NNAGMQF-----RTPLEDFPADaferlLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSAL----------ARPGIA 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07523 158 PYTATKGAVGNLTKGMATDWAKHGLQCNAIAP 189

PRK05693

SDR family oxidoreductase;

3-191

2.94e-13

SDR family oxidoreductase;

Pssm-ID: 168186 [Multi-domain] Cd Length: 274 Bit Score: 66.35 E-value: 2.94e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLE--GAKAAAGdlggdHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGYEVWATARKAEdvEALAAAG-----FTAVQLDVNDGAALARLAEELEAEHGGLDVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLgSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:PRK05693  77 INNAGYGAMGPLLDGGVEAMRRQFETNVF-AVVGVTRALFPLLRRSRGLVVNIG----------SVSGVLVTPFAGAYCA 145

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809569 161 SKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK05693 146 SKAAVHALSDALRLELAPFGVQVMEVQPGAI 176

SDR_c7

cd05354

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...

2-191

2.97e-13

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187612 [Multi-domain] Cd Length: 235 Bit Score: 65.89 E-value: 2.97e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQ-LMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKehdvQNTFEELEKHLGRVNFL 80
Cdd:cd05354    3 DKTVLVTGANRGIGKAFVEsLLAHGAKKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTD----PESIKAAAAQAKDVDVV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGINR-DGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkRSIVGLKGNSGQSVYS 159
Cdd:cd05354   79 INNAGVLKpATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNL----------NSVASLKNFPAMGTYS 148

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:cd05354  149 ASKSAAYSLTQGLRAELAAQGTLVLSVHPGPI 180

PRK08219

SDR family oxidoreductase;

1-188

5.30e-13

SDR family oxidoreductase;

Pssm-ID: 181298 [Multi-domain] Cd Length: 227 Bit Score: 65.34 E-value: 5.30e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARkGYRLAVIARNLEGAKAAAGDLGGDHlAFSCDVAKEHDVQNTFEelekHLGRVNFL 80
Cdd:PRK08219   2 ERPTALITGASRGIGAAIARELAP-THTLLLGGRPAERLDELAAELPGAT-PFPVDLTDPEAIAAAVE----QLGRLDVL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSM-LTckAAMRTMIQQQGGSIVNVghrremllhkRSIVGLKGNSGQSVYS 159
Cdd:PRK08219  76 VHNAGVADLGPVAESTVDEWRATLEVNVVAPAeLT--RLLLPALRAAHGHVVFI----------NSGAGLRANPGWGSYA 143

                        170       180
                 ....*....|....*....|....*....
gi 578809569 160 ASKGGLVGFSRALAKEvARKKIRVNVVAP 188
Cdd:PRK08219 144 ASKFALRALADALREE-EPGNVRVTSVHP 171

carb_red_sniffer_like_SDR_c

cd05325

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...

7-188

1.60e-12

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187586 [Multi-domain] Cd Length: 233 Bit Score: 63.85 E-value: 1.60e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRA-VAQLMARKGYRLAVIARNLEGAKAAAGdLGGDHLAFSC---DVAKEhdVQNTFEELEKHLG--RVNFL 80
Cdd:cd05325    3 ITGASRGIGLElVRQLLARGNNTVIATCRDPSAATELAA-LGASHSRLHIlelDVTDE--IAESAEAVAERLGdaGLDVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGINRDGLLVRTKT-EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREmllhkrSIvGLKGNSGQSVYS 159
Cdd:cd05325   80 INNAGILHSYGPASEVDsEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVG------SI-GDNTSGGWYSYR 152

                        170       180
                 ....*....|....*....|....*....
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05325  153 ASKAALNMLTKSLAVELKRDGITVVSLHP 181

PRK12481

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;

3-188

3.17e-12

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;

Pssm-ID: 171531 [Multi-domain] Cd Length: 251 Bit Score: 63.39 E-value: 3.17e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGyrLAVIARNLEGA---KAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK12481   9 KVAIITGCNTGLGQGMAIGLAKAG--ADIVGVGVAEApetQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGHIDI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINR--DGLLVRTKTEDMVSQLHTNLLgSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK12481  87 LINNAGIIRrqDLLEFGNKDWDDVININQKTV-FFLSQAVAKQFVKQGNGGKIINIA----------SMLSFQGGIRVPS 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809569 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12481 156 YTASKSAVMGLTRALATELSQYNINVNAIAP 186

retinol-DH_like_SDR_c

cd09807

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...

3-188

3.40e-12

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 212495 [Multi-domain] Cd Length: 274 Bit Score: 63.64 E-value: 3.40e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHL-----AFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd09807    2 KTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLnheviVRHLDLASLKSIRAFAAEFLAEEDRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINRdglLVRTKTED-MVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHrremLLHKRSIVGLKG-NSGQ 155
Cdd:cd09807   82 DVLINNAGVMR---CPYSKTEDgFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSS----LAHKAGKINFDDlNSEK 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 578809569 156 S-----VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd09807  155 SyntgfAYCQSKLANVLFTRELARRLQGTGVTVNALHP 192

PRK07677

short chain dehydrogenase; Provisional

3-188

3.93e-12

short chain dehydrogenase; Provisional

Pssm-ID: 181077 [Multi-domain] Cd Length: 252 Bit Score: 63.16 E-value: 3.93e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07677   2 KVVIITGGSSGMGKAMAKRFAEEGANVVITGRTkekLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINrdgLLVRtkTEDMV-----SQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVghrremllhkrsIVGLKGNS 153
Cdd:PRK07677  82 LINNAAGN---FICP--AEDLSvngwnSVIDIVLNGTFYCSQAVGKYWIEKgIKGNIINM------------VATYAWDA 144

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 578809569 154 GQSV-YSAS-KGGLVGFSRALAKEVARK-KIRVNVVAP 188
Cdd:PRK07677 145 GPGViHSAAaKAGVLAMTRTLAVEWGRKyGIRVNAIAP 182

PRK07024

SDR family oxidoreductase;

7-188

5.69e-12

SDR family oxidoreductase;

Pssm-ID: 235910 [Multi-domain] Cd Length: 257 Bit Score: 62.64 E-value: 5.69e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VF--GGSRGIGRAVAQLMARKGYRLAVIARNLEG--AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK07024   5 VFitGASSGIGQALAREYARQGATLGLVARRTDAlqAFAARLPKAARVSVYAADVRDADALAAAAADFIAAHGLPDVVIA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAGINRdGLLVRTkTED---MVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK07024  85 NAGISV-GTLTEE-REDlavFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIA----------SVAGVRGLPGAGAYS 152

                        170       180
                 ....*....|....*....|....*....
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07024 153 ASKAAAIKYLESLRVELRPAGVRVVTIAP 181

PRK06194

hypothetical protein; Provisional

3-188

6.77e-12

hypothetical protein; Provisional

Pssm-ID: 180458 [Multi-domain] Cd Length: 287 Bit Score: 62.73 E-value: 6.77e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLA---VIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK06194   7 KVAVITGAASGFGLAFARIGAALGMKLVladVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFGAVHL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHrremLLHKRSIVGLKGNSGQSVYS 159
Cdd:PRK06194  87 LFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAEKDPAYEGH----IVNTASMAGLLAPPAMGIYN 162

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809569 160 ASKGGLVGFSRALAK--EVARKKIRVNVVAP 188
Cdd:PRK06194 163 VSKHAVVSLTETLYQdlSLVTDQVGASVLCP 193

PRK05717

SDR family oxidoreductase;

3-188

8.81e-12

SDR family oxidoreductase;

Pssm-ID: 168204 [Multi-domain] Cd Length: 255 Bit Score: 62.21 E-value: 8.81e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFIAMDVADEAQVAAGVAEVLGQFGRLDALVC 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAGIN--RDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMrTMIQQQGGSIVNVGHRREMllhkrsivglKGNSGQSVYSA 160
Cdd:PRK05717  91 NAAIAdpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCA-PYLRAHNGAIVNLASTRAR----------QSEPDTEAYAA 159

                        170       180
                 ....*....|....*....|....*...
gi 578809569 161 SKGGLVGFSRALAKEVArKKIRVNVVAP 188
Cdd:PRK05717 160 SKGGLLALTHALAISLG-PEIRVNAVSP 186

DHRS1-like_SDR_c

cd09763

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...

3-188

2.28e-11

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This subgroup includes human DHRS1 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187664 [Multi-domain] Cd Length: 265 Bit Score: 61.31 E-value: 2.28e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN----LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHL-GRV 77
Cdd:cd09763    4 KIALVTGASRGIGRGIALQLGEAGATVYITGRTilpqLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQqGRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAA-GINRDGLLVRTKT---------EDMVSqlhTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkrSIV 147
Cdd:cd09763   84 DILVNNAyAAVQLILVGVAKPfweepptiwDDINN---VGLRAHYACSVYAAPLMVKAGKGLIVII-----------SST 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 578809569 148 GLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd09763  150 GGLEYLFNVAYGVGKAAIDRMAADMAHELKPHGVAVVSLWP 190

Ycik_SDR_c

cd05340

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...

2-188

2.39e-11

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187599 [Multi-domain] Cd Length: 236 Bit Score: 60.67 E-value: 2.39e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAK------AAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:cd05340    4 DRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRqvadhiNEEGGRQPQWFILDLLTCTSENCQQLAQRIAVNYP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  76 RVN-FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSG 154
Cdd:cd05340   84 RLDgVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTS----------SSVGRQGRAN 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 578809569 155 QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05340  154 WGAYAVSKFATEGL*QVLADEYQQRNLRVNCINP 187

PRK07041

SDR family oxidoreductase;

7-195

2.66e-11

SDR family oxidoreductase;

Pssm-ID: 235914 [Multi-domain] Cd Length: 230 Bit Score: 60.44 E-value: 2.66e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH--LAFSCDVAKEHDVQNTFEElekhLGRVNFLVNAA 84
Cdd:PRK07041   2 VVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGApvRTAALDITDEAAVDAFFAE----AGPFDHVVITA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  85 GINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAmrtmIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGG 164
Cdd:PRK07041  78 ADTPGGPVRALPLAAAQAAMDSKFWGAYRVARAA----RIAPGGSLTFVS----------GFAAVRPSASGVLQGAINAA 143

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 165 LVGFSRALAKEVArkKIRVNVVAP--VTILVWS 195
Cdd:PRK07041 144 LEALARGLALELA--PVRVNTVSPglVDTPLWS 174

DHPR_SDR_c_like

cd05334

dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...

3-191

2.71e-11

dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an NAD-binding protein related to the SDRs. It converts dihydrobiopterin into tetrahydrobiopterin, a cofactor necessary in catecholamines synthesis. Dihydropteridine reductase has the YXXXK of these tyrosine-dependent oxidoreductases, but lacks the typical upstream Asn and Ser catalytic residues. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187595 [Multi-domain] Cd Length: 221 Bit Score: 60.42 E-value: 2.71e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNlEGAKAAAGDLGGDHlafSCDVAKEHDVqntFEELEKHLGRVNFLVN 82
Cdd:cd05334    2 RVVLVYGGRGALGSAVVQAFKSRGWWVASIDLA-ENEEADASIIVLDS---DSFTEQAKQV---VASVARLSGKVDALIC 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAG-----INRDGLLVRTkTEDMVSQlhtNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:cd05334   75 VAGgwaggSAKSKSFVKN-WDLMWKQ---NLWTSFIASHLATKHL--LSGGLLVLTG----------AKAALEPTPGMIG 138

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 578809569 158 YSASKGGLVGFSRALAKE--VARKKIRVNVVAPVTI 191
Cdd:cd05334  139 YGAAKAAVHQLTQSLAAEnsGLPAGSTANAILPVTL 174

PRK06924

(S)-benzoin forming benzil reductase;

7-187

2.72e-11

(S)-benzoin forming benzil reductase;

Pssm-ID: 180753 [Multi-domain] Cd Length: 251 Bit Score: 60.85 E-value: 2.72e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIAR--NLEGAKAAaGDLGGDHLAFSCDVAKEHDVQNTFEE----LEKHLGRVNFL 80
Cdd:PRK06924   6 ITGTSQGLGEAIANQLLEKGTHVISISRteNKELTKLA-EQYNSNLTFHSLDLQDVHELETNFNEilssIQEDNVSSIHL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAG----INRDGllvRTKTEDMVSQLHTNLLGSMLTCKAAM-RTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:PRK06924  85 INNAGmvapIKPIE---KAESEELITNVHLNLLAPMILTSTFMkHTKDWKVDKRVINIS----------SGAAKNPYFGW 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVA 187
Cdd:PRK06924 152 SAYCSSKAGLDMFTQTVATEQEEEEYPVKIVA 183

KR_2_SDR_x

cd08953

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...

7-174

2.77e-11

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187656 [Multi-domain] Cd Length: 436 Bit Score: 61.61 E-value: 2.77e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARK-GYRLAVIAR--------NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd08953  210 VTGGAGGIGRALARALARRyGARLVLLGRsplppeeeWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRERYGAI 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSmltckAAMRTMIQQQggsivnvghRREMLLHKRSIVGLKGNSGQSV 157
Cdd:cd08953  290 DGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGL-----LNLAQALADE---------PLDFFVLFSSVSAFFGGAGQAD 355

                        170
                 ....*....|....*..
gi 578809569 158 YSASKGGLVGFSRALAK 174
Cdd:cd08953  356 YAAANAFLDAFAAYLRQ 372

PRK06125

short chain dehydrogenase; Provisional

9-188

3.27e-11

short chain dehydrogenase; Provisional

Pssm-ID: 235703 [Multi-domain] Cd Length: 259 Bit Score: 60.44 E-value: 3.27e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH----LAFSCDVAKEHDVqntfEELEKHLGRVNFLVNAA 84
Cdd:PRK06125  14 GASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHgvdvAVHALDLSSPEAR----EQLAAEAGDIDILVNNA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  85 GINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkrsiVGLKGNSGQSVY---SAS 161
Cdd:PRK06125  90 GAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNV-------------IGAAGENPDADYicgSAG 156

                        170       180
                 ....*....|....*....|....*..
gi 578809569 162 KGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06125 157 NAALMAFTRALGGKSLDDGVRVVGVNP 183

PRK08993

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;

3-188

4.21e-11

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;

Pssm-ID: 181605 [Multi-domain] Cd Length: 253 Bit Score: 60.27 E-value: 4.21e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVI-----ARNLEGAKAaagdLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK08993  11 KVAVVTGCDTGLGQGMALGLAEAGCDIVGInivepTETIEQVTA----LGRRFLSLTADLRKIDGIPALLERAVAEFGHI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:PRK08993  87 DILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQgNGGKIINIA----------SMLSFQGGIRVP 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809569 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08993 157 SYTASKSGVMGVTRLMANEWAKHNINVNAIAP 188

type1_17beta-HSD-like_SDR_c

cd09806

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...

3-188

4.29e-11

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187666 [Multi-domain] Cd Length: 258 Bit Score: 60.17 E-value: 4.29e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMAR---KGYRLAVIARNL---EGAKAAAGDLGGDHLAF-SCDVAKEHDVQNTFEELEKhlG 75
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLASdpsKRFKVYATMRDLkkkGRLWEAAGALAGGTLETlQLDVCDSKSVAAAVERVTE--R 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:cd09806   79 HVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTS----------SVGGLQGLPFN 148

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd09806  149 DVYCASKFALEGLCESLAVQLLPFNVHLSLIEC 181

PRK07576

short chain dehydrogenase; Provisional

3-188

7.28e-11

short chain dehydrogenase; Provisional

Pssm-ID: 236056 [Multi-domain] Cd Length: 264 Bit Score: 59.58 E-value: 7.28e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV-- 77
Cdd:PRK07576  10 KNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVaqlQQAGPEGLGVSADVRDYAAVEAAFAQIADEFGPIdv 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 -------NFLVNAAGINRDGLlvRTKTEdmvsqlhTNLLGSMLTCKAAMRTMiQQQGGSIVNVGhrremllHKRSIVGLK 150
Cdd:PRK07576  90 lvsgaagNFPAPAAGMSANGF--KTVVD-------IDLLGTFNVLKAAYPLL-RRPGASIIQIS-------APQAFVPMP 152

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 578809569 151 gnsGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07576 153 ---MQAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVP 187

PRK09291

SDR family oxidoreductase;

1-188

9.15e-11

SDR family oxidoreductase;

Pssm-ID: 181762 [Multi-domain] Cd Length: 257 Bit Score: 59.24 E-value: 9.15e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRL---AVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEElekhlgRV 77
Cdd:PRK09291   1 MSKTILITGAGSGFGREVALRLARKGHNViagVQIAPQVTALRAEAARRGLALRVEKLDLTDAIDRAQAAEW------DV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK09291  75 DVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTS----------SMAGLITGPFTGA 144

                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809569 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK09291 145 YCASKHALEAIAEAMHAELKPFGIQVATVNP 175

PKS_KR

smart00822

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...

9-111

1.03e-10

Pssm-ID: 214833 [Multi-domain] Cd Length: 180 Bit Score: 57.88 E-value: 1.03e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569     9 GGSRGIGRAVAQLMARKGYR-LAVIARNLEGAKAAA------GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:smart00822   7 GGLGGLGRALARWLAERGARrLVLLSRSGPDAPGAAallaelEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLTGVI 86

                           90       100       110
                   ....*....|....*....|....*....|
gi 578809569    82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGS 111
Cdd:smart00822  87 HAAGVLDDGVLASLTPERFAAVLAPKAAGA 116

SDR

cd02266

Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...

76-191

1.05e-10

Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187535 [Multi-domain] Cd Length: 186 Bit Score: 58.30 E-value: 1.05e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:cd02266   31 RRDVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILIS----------SVAGLFGAPGL 100

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:cd02266  101 GGYAASKAALDGLAQQWASEGWGNGLPATAVACGTW 136

fabG

PRK05786

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

3-191

1.14e-10

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

Pssm-ID: 235608 [Multi-domain] Cd Length: 238 Bit Score: 59.00 E-value: 1.14e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFScDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK05786   6 KKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNenkLKRMKKTLSKYGNIHYVVG-DVSSTESARNVIEKAAKVLNAIDG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 L-VNAAGINRDGLLVRTKTEDMvsqLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGL-KGNSGQSV 157
Cdd:PRK05786  85 LvVTVGGYVEDTVEEFSGLEEM---LTNHIKIPLYAVNASLRFL--KEGSSIVLVS----------SMSGIyKASPDQLS 149

                        170       180       190
                 ....*....|....*....|....*....|....
gi 578809569 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK05786 150 YAVAKAGLAKAVEILASELLGRGIRVNGIAPTTI 183

pfam08659

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...

9-160

1.40e-10

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.

Pssm-ID: 430138 [Multi-domain] Cd Length: 180 Bit Score: 57.57 E-value: 1.40e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569    9 GGSRGIGRAVAQLMARKGYR-LAVIARNLEGAKAAAG------DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:pfam08659   7 GGLGGLGRELARWLAERGARhLVLLSRSAAPRPDAQAliaeleARGVEVVVVACDVSDPDAVAALLAEIKAEGPPIRGVI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSM----LTCKAAMRTMIqqqggsivnvghrreMLlhkRSIVGLKGNSGQSV 157
Cdd:pfam08659  87 HAAGVLRDALLENMTDEDWRRVLAPKVTGTWnlheATPDEPLDFFV---------------LF---SSIAGLLGSPGQAN 148


                  ...
gi 578809569  158 YSA 160
Cdd:pfam08659 149 YAA 151

PRK07985

SDR family oxidoreductase;

2-195

1.49e-10

SDR family oxidoreductase;

Pssm-ID: 181188 [Multi-domain] Cd Length: 294 Bit Score: 59.24 E-value: 1.49e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVI-----ARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK07985  49 DRKALVTGGDSGIGRAAAIAYAREGADVAISylpveEEDAQDVKKIIEECGRKAVLLPGDLSDEKFARSLVHEAHKALGG 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLH-TNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:PRK07985 129 LDIMALVAGKQVAIPDIADLTSEQFQKTFaINVFALFWLTQEAIPLL--PKGASIITTS----------SIQAYQPSPHL 196

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTIlvWS 195
Cdd:PRK07985 197 LDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPI--WT 234

PRK08278

SDR family oxidoreductase;

9-119

2.67e-10

SDR family oxidoreductase;

Pssm-ID: 181349 [Multi-domain] Cd Length: 273 Bit Score: 57.99 E-value: 2.67e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   9 GGSRGIGRAVAQLMARKGYRLAVIAR------NLEG----AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK08278  13 GASRGIGLAIALRAARDGANIVIAAKtaephpKLPGtihtAAEEIEAAGGQALPLVGDVRDEDQVAAAVAKAVERFGGID 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 578809569  79 FLVNAAG-INRDGLL-VRTKTEDMVSQLhtNLLGSMLTCKAAM 119
Cdd:PRK08278  93 ICVNNASaINLTGTEdTPMKRFDLMQQI--NVRGTFLVSQACL 133

PRK09134

SDR family oxidoreductase;

7-188

5.03e-10

SDR family oxidoreductase;

Pssm-ID: 236389 [Multi-domain] Cd Length: 258 Bit Score: 57.24 E-value: 5.03e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK09134  14 VTGAARRIGRAIALDLAAHGFDVAVhYNRSRDEAEALAaeiRALGRRAVALQADLADEAEVRALVARASAALGPITLLVN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAGI-NRDglLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREmllhkrsivgLKGNSGQSVYSA 160
Cdd:PRK09134  94 NASLfEYD--SAASFTRASWDRhMATNLRAPFVLAQAFARALPADARGLVVNMIDQRV----------WNLNPDFLSYTL 161

                        170       180
                 ....*....|....*....|....*...
gi 578809569 161 SKGGLVGFSRALAKEVArKKIRVNVVAP 188
Cdd:PRK09134 162 SKAALWTATRTLAQALA-PRIRVNAIGP 188

PRK05875

short chain dehydrogenase; Provisional

2-188

3.49e-09

short chain dehydrogenase; Provisional

Pssm-ID: 180300 [Multi-domain] Cd Length: 276 Bit Score: 55.19 E-value: 3.49e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK05875   7 DRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIealkgAGAVRYEPADVTDEDQVARAVDAATAWHGR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGINRD-GLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:PRK05875  87 LHGVVHCAGGSETiGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGIS----------SIAASNTHRWF 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK05875 157 GAYGVTKSAVDHLMKLAADELGPSWVRVNSIRP 189

PRK12859

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

3-188

4.08e-09

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

Pssm-ID: 183797 [Multi-domain] Cd Length: 256 Bit Score: 54.79 E-value: 4.08e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSR--GIGRAVAQLMARKGYRL---------------------AVIARNLE--GAKAAAGDLggdhlafscDV 57
Cdd:PRK12859   7 KVAVVTGVSRldGIGAAICKELAEAGADIfftywtaydkempwgvdqdeqIQLQEELLknGVKVSSMEL---------DL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  58 AKEHDVQNTFEELEKHLGRVNFLVNAAGINRDgLLVRTKTEDMVSQLH-TNLLGSMLTCKAAMRTMIQQQGGSIVNVghr 136
Cdd:PRK12859  78 TQNDAPKELLNKVTEQLGYPHILVNNAAYSTN-NDFSNLTAEELDKHYmVNVRATTLLSSQFARGFDKKSGGRIINM--- 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809569 137 remllhkRSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12859 154 -------TSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINP 198

PRK12744

SDR family oxidoreductase;

2-188

7.59e-09

SDR family oxidoreductase;

Pssm-ID: 183716 [Multi-domain] Cd Length: 257 Bit Score: 53.98 E-value: 7.59e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG-------DLGGDHLAFSCDVAKEHDVQNTFEELEKHL 74
Cdd:PRK12744   8 GKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSAASKADAEetvaavkAAGAKAVAFQADLTTAAAVEKLFDDAKAAF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  75 GRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVghrremllhkrsIVGLKG--N 152
Cdd:PRK12744  88 GRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHL--NDNGKIVTL------------VTSLLGafT 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 578809569 153 SGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12744 154 PFYSAYAGSKAPVEHFTRAASKEFGARGISVTAVGP 189

HSDL2_SDR_c

cd09762

human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...

5-190

8.30e-09

human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human HSDL2 and related protens. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187663 [Multi-domain] Cd Length: 243 Bit Score: 53.60 E-value: 8.30e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   5 CAVF--GGSRGIGRAVAQLMARKGYRLAVIARNLEG----------AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEK 72
Cdd:cd09762    4 KTLFitGASRGIGKAIALKAARDGANVVIAAKTAEPhpklpgtiytAAEEIEAAGGKALPCIVDIRDEDQVRAAVEKAVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  73 HLGRVNFLV-NAAGIN-RDGLLVRTKTEDMVSQLhtNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREMllhkrsivGLK 150
Cdd:cd09762   84 KFGGIDILVnNASAISlTGTLDTPMKRYDLMMGV--NTRGTYLCSKACLPYLKKSKNPHILNLSPPLNL--------NPK 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 578809569 151 GNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPVT 190
Cdd:cd09762  154 WFKNHTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWPRT 193

PRK08945

putative oxoacyl-(acyl carrier protein) reductase; Provisional

2-188

8.96e-09

putative oxoacyl-(acyl carrier protein) reductase; Provisional

Pssm-ID: 236357 [Multi-domain] Cd Length: 247 Bit Score: 53.72 E-value: 8.96e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLA-FSCDV--AKEHDVQNTFEELEKHLG 75
Cdd:PRK08945  12 DRIILVTGAGDGIGREAALTYARHGATVILLGRTeekLEAVYDEIEAAGGPQPAiIPLDLltATPQNYQQLADTIEEQFG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  76 RVNFLVNAAGInrdgLLVRT----KTEDMVSQ-LHTNLLGS-MLTcKAAMRTMIQQQGGSIVnvghrremllHKRSIVGL 149
Cdd:PRK08945  92 RLDGVLHNAGL----LGELGpmeqQDPEVWQDvMQVNVNATfMLT-QALLPLLLKSPAASLV----------FTSSSVGR 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 578809569 150 KGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08945 157 QGRANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINP 195

PRK12746

SDR family oxidoreductase;

3-188

9.11e-09

SDR family oxidoreductase;

Pssm-ID: 183718 [Multi-domain] Cd Length: 254 Bit Score: 53.50 E-value: 9.11e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHL---- 74
Cdd:PRK12746   7 KVALVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETIREIesnGGKAFLIEADLNSIDGVKKLVEQLKNELqirv 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  75 --GRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGHRREMLlhkrsivglkGN 152
Cdd:PRK12746  87 gtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL--RAEGRVINISSAEVRL----------GF 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 578809569 153 SGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12746 155 TGSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMP 190

ENR_SDR

cd05372

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...

3-187

1.10e-08

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187630 [Multi-domain] Cd Length: 250 Bit Score: 53.35 E-value: 1.10e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFG--GSRGIGRAVAQLMARKGYRLAVIARN--LEG-AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd05372    2 KRILITGiaNDRSIAWGIAKALHEAGAELAFTYQPeaLRKrVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKDWGKL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGI-NRDGLLVRTktedmvsqLHTNLLGSMLT-----------CKAAMRTMiqQQGGSIVNVGHrremllhkrs 145
Cdd:cd05372   82 DGLVHSIAFaPKVQLKGPF--------LDTSRKGFLKAldisayslvslAKAALPIM--NPGGSIVTLSY---------- 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 578809569 146 IVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVA 187
Cdd:cd05372  142 LGSERVVPGYNVMGVAKAALESSVRYLAYELGRKGIRVNAIS 183

FabI

COG0623

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...

7-188

1.29e-08

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis

Pssm-ID: 440388 [Multi-domain] Cd Length: 254 Bit Score: 53.10 E-value: 1.29e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFG--GSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:COG0623   10 ITGvaNDRSIAWGIAKALHEEGAELAFTYQGealKKRVEPLAEELGSA-LVLPCDVTDDEQIDALFDEIKEKWGKLDFLV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  82 NAAG-------------INRDGLLvrtKTEDmVS--QLHtnllgSMltCKAAMRTMiqQQGGSIVNV---GHRREMllhk 143
Cdd:COG0623   89 HSIAfapkeelggrfldTSREGFL---LAMD-ISaySLV-----AL--AKAAEPLM--NEGGSIVTLtylGAERVV---- 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 578809569 144 rsivglkgnSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:COG0623  152 ---------PNYNVMGVAKAALEASVRYLAADLGPKGIRVNAISA 187

sepiapter_red

TIGR01500

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...

4-188

1.69e-08

Pssm-ID: 273660 [Multi-domain] Cd Length: 256 Bit Score: 52.99 E-value: 1.69e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569    4 VCAVFGGSRGIGRAVAQLMAR----KGYRLAVIARNLEGAKAAAGDLGGDHLA-----FSCDVAKEHDVQNTFEELEKhL 74
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKclksPGSVLVLSARNDEALRQLKAEIGAERSGlrvvrVSLDLGAEAGLEQLLKALRE-L 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   75 GRVNFLVNAAGINRDGLLVRT-KTEDMVSQL-------HTNLLGSMLTCKAAMRTMIQQQGG--SIVNVGhrremllhkr 144
Cdd:TIGR01500  81 PRPKGLQRLLLINNAGTLGDVsKGFVDLSDStqvqnywALNLTSMLCLTSSVLKAFKDSPGLnrTVVNIS---------- 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578809569  145 SIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:TIGR01500 151 SLCAIQPFKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAP 194

PRK08017

SDR family oxidoreductase;

1-188

2.18e-08

SDR family oxidoreductase;

Pssm-ID: 181198 [Multi-domain] Cd Length: 256 Bit Score: 52.40 E-value: 2.18e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAkAAAGDLGGDHLAFSCDVAKEHDvQNTFEELEKHLGRVNFL 80
Cdd:PRK08017   1 MQKSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDV-ARMNSLGFTGILLDLDDPESVE-RAADEVIALTDNRLYGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGS-MLTCkAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK08017  79 FNNAGFGVYGPLSTISRQQMEQQFSTNFFGThQLTM-LLLPAMLPHGEGRIVMTS----------SVMGLISTPGRGAYA 147

                        170       180
                 ....*....|....*....|....*....
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08017 148 ASKYALEAWSDALRMELRHSGIKVSLIEP 176

PRK08703

SDR family oxidoreductase;

2-188

4.20e-08

SDR family oxidoreductase;

Pssm-ID: 169556 [Multi-domain] Cd Length: 239 Bit Score: 51.47 E-value: 4.20e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKA------AAGdlGGDHLAFSCDVAKEHDvqNTFEEL----- 70
Cdd:PRK08703   6 DKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKvydaivEAG--HPEPFAIRFDLMSAEE--KEFEQFaatia 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  71 EKHLGRVNFLVNAAGINRDGLLVRTKT-EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRRemllhkrsivGL 149
Cdd:PRK08703  82 EATQGKLDGIVHCAGYFYALSPLDFQTvAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESH----------GE 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 578809569 150 KGNSGQSVYSASKGGLVGFSRALAKEVAR-KKIRVNVVAP 188
Cdd:PRK08703 152 TPKAYWGGFGASKAALNYLCKVAADEWERfGNLRANVLVP 191

PRK12748

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

1-188

4.69e-08

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

Pssm-ID: 237189 [Multi-domain] Cd Length: 256 Bit Score: 51.61 E-value: 4.69e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSR--GIGRAVAQLMARKGYR------------LAVIARNLEGA--KAAAGDLGGDHLAFSCDVAKEHDVQ 64
Cdd:PRK12748   4 MKKIALVTGASRlnGIGAAVCRRLAAKGIDifftywspydktMPWGMHDKEPVllKEEIESYGVRCEHMEIDLSQPYAPN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  65 NTFEELEKHLGRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkr 144
Cdd:PRK12748  84 RVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINL----------- 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809569 145 sivglkgNSGQSV--------YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12748 153 -------TSGQSLgpmpdelaYAATKGAIEAFTKSLAPELAEKGITVNAVNP 197

type2_17beta_HSD-like_SDR_c

cd09805

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...

5-188

1.36e-07

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187665 [Multi-domain] Cd Length: 281 Bit Score: 50.35 E-value: 1.36e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   5 CAVF--GGSRGIGRAVAQLMARKGYRL--AVIARNLEGAK----AAAGDLGGDHLafscDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd09805    1 KAVLitGCDSGFGNLLAKKLDSLGFTVlaGCLTKNGPGAKelrrVCSDRLRTLQL----DVTKPEQIKRAAQWVKEHVGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNF--LVNAAGIN---RDGLLvrTKTEDMVSQLHTNLLGSMLTCKAaMRTMIQQQGGSIVNVGhrremllhkrSIVGLKG 151
Cdd:cd09805   77 KGLwgLVNNAGILgfgGDEEL--LPMDDYRKCMEVNLFGTVEVTKA-FLPLLRRAKGRVVNVS----------SMGGRVP 143

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 578809569 152 NSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd09805  144 FPAGGAYCASKAAVEAFSDSLRRELQPWGVKVSIIEP 180

pter_reduc_Leis

TIGR02685

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...

4-188

2.05e-07

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.

Pssm-ID: 131732 [Multi-domain] Cd Length: 267 Bit Score: 49.93 E-value: 2.05e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569    4 VCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAK---AAAGDLGGDHLAFSC--DVAKEHDVQNTFEEL----EKHL 74
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAAstlAAELNARRPNSAVTCqaDLSNSATLFSRCEAIidacFRAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   75 GRVNFLVNAAGINRDGLLVRTKTEDMVSQLHT------NLLGSMLTCKAAM-RTMIQQQGGSivnvghRREMLLHKRSIV 147
Cdd:TIGR02685  83 GRCDVLVNNASAFYPTPLLRGDAGEGVGDKKSlevqvaELFGSNAIAPYFLiKAFAQRQAGT------RAEQRSTNLSIV 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578809569  148 GL------KGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:TIGR02685 157 NLcdamtdQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAP 203

KR_FAS_SDR_x

cd05274

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...

9-172

4.13e-07

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187582 [Multi-domain] Cd Length: 375 Bit Score: 49.30 E-value: 4.13e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   9 GGSRGIGRAVAQLMARKGYR-LAVIARN-----LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKhLGRVNFLVN 82
Cdd:cd05274  157 GGLGGLGLLVARWLAARGARhLVLLSRRgpaprAAARAALLRAGGARVSVVRCDVTDPAALAALLAELAA-GGPLAGVIH 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCkAAMRtmiqqqggsivnvGHRREMLLHKRSIVGLKGNSGQSVYSASK 162
Cdd:cd05274  236 AAGVLRDALLAELTPAAFAAVLAAKVAGALNLH-ELTP-------------DLPLDFFVLFSSVAALLGGAGQAAYAAAN 301

                        170
                 ....*....|
gi 578809569 163 GGLVGFSRAL 172
Cdd:cd05274  302 AFLDALAAQR 311

PRK10538

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...

7-188

4.57e-07

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;

Pssm-ID: 182531 [Multi-domain] Cd Length: 248 Bit Score: 48.60 E-value: 4.57e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGI 86
Cdd:PRK10538   5 VTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVNNAGL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  87 NRdGL--LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGG 164
Cdd:PRK10538  85 AL-GLepAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIG----------STAGSWPYAGGNVYGATKAF 153

                        170       180
                 ....*....|....*....|....
gi 578809569 165 LVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK10538 154 VRQFSLNLRTDLHGTAVRVTDIEP 177

PRK07806

SDR family oxidoreductase;

2-85

1.19e-06

SDR family oxidoreductase;

Pssm-ID: 181126 [Multi-domain] Cd Length: 248 Bit Score: 47.41 E-value: 1.19e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN----LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK07806   6 GKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQkaprANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREEFGGL 85


                 ....*....
gi 578809569  78 NFLV-NAAG 85
Cdd:PRK07806  86 DALVlNASG 94

PRK12747

short chain dehydrogenase; Provisional

3-188

2.86e-06

short chain dehydrogenase; Provisional

Pssm-ID: 183719 [Multi-domain] Cd Length: 252 Bit Score: 46.61 E-value: 2.86e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFE----ELEKHL 74
Cdd:PRK12747   5 KVALVTGASRGIGRAIAKRLANDGALVAIhYGNRKEEAEETVYEIqsnGGSAFSIGANLESLHGVEALYSsldnELQNRT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  75 GRVNF--LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGHRREMLLHKRSIvglkgn 152
Cdd:PRK12747  85 GSTKFdiLINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRISLPDFI------ 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 578809569 153 sgqsVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12747 157 ----AYSMTKGAINTMTFTLAKQLGARGITVNAILP 188

PRK12742

SDR family oxidoreductase;

7-188

7.65e-06

SDR family oxidoreductase;

Pssm-ID: 183714 [Multi-domain] Cd Length: 237 Bit Score: 45.13 E-value: 7.65e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLA-VIARNLEGAKAAAGDLGGDhlAFSCDVAKEHDVQNTFEELekhlGRVNFLVNAAG 85
Cdd:PRK12742  11 VLGGSRGIGAAIVRRFVTDGANVRfTYAGSKDAAERLAQETGAT--AVQTDSADRDAVIDVVRKS----GALDILVVNAG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  86 INRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrsivGLKGN----SGQSVYSAS 161
Cdd:PRK12742  85 IAVFGDALELDADDIDRLFKINIHAPYHASVEAARQM--PEGGRIIIIG-------------SVNGDrmpvAGMAAYAAS 149

                        170       180
                 ....*....|....*....|....*..
gi 578809569 162 KGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12742 150 KSALQGMARGLARDFGPRGITINVVQP 176

PRK08339

short chain dehydrogenase; Provisional

11-191

9.99e-06

short chain dehydrogenase; Provisional

Pssm-ID: 169389 [Multi-domain] Cd Length: 263 Bit Score: 44.85 E-value: 9.99e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  11 SRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGG----DHLAFSCDVAKEHDVQNTFEELeKHLGRVNFLVNAAGI 86
Cdd:PRK08339  17 SKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSesnvDVSYIVADLTKREDLERTVKEL-KNIGEPDIFFFSTGG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVnvghRREMLLHKRSIVGLkgnSGQSVYSASKGGLV 166
Cdd:PRK08339  96 PKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRII----YSTSVAIKEPIPNI---ALSNVVRISMAGLV 168

                        170       180
                 ....*....|....*....|....*
gi 578809569 167 gfsRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK08339 169 ---RTLAKELGPKGITVNGIMPGII 190

PRK07023

SDR family oxidoreductase;

7-188

1.05e-05

SDR family oxidoreductase;

Pssm-ID: 180796 [Multi-domain] Cd Length: 243 Bit Score: 44.62 E-value: 1.05e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGA-KAAAGDLGGDHLafsCDVAKEHDVQ-----NTFEELEKHLGRVnFL 80
Cdd:PRK07023   6 VTGHSRGLGAALAEQLLQPGIAVLGVARSRHPSlAAAAGERLAEVE---LDLSDAAAAAawlagDLLAAFVDGASRV-LL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  81 VNAAGINRDGLLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMIQQQggsivnvgHRRemLLHKRSIVGLKGNSGQSVYS 159
Cdd:PRK07023  82 INNAGTVEPIGPLATLDAAAIARaVGLNVAAPLMLTAALAQAASDAA--------ERR--ILHISSGAARNAYAGWSVYC 151

                        170       180
                 ....*....|....*....|....*....
gi 578809569 160 ASKGGLVGFSRALAKEvARKKIRVNVVAP 188
Cdd:PRK07023 152 ATKAALDHHARAVALD-ANRALRIVSLAP 179

PRK08862

SDR family oxidoreductase;

10-188

1.62e-05

SDR family oxidoreductase;

Pssm-ID: 236342 [Multi-domain] Cd Length: 227 Bit Score: 43.94 E-value: 1.62e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  10 GSRgIGRAVAQLMARKGYRLAVIARNLEGAKA---AAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV-NFLVNAAG 85
Cdd:PRK08862  14 GSV-LGRTISCHFARLGATLILCDQDQSALKDtyeQCSALTDNVYSFQLKDFSQESIRHLFDAIEQQFNRApDVLVNNWT 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  86 INRDGLLVRTKTEDMVSQLHTNLLGSMLT----CKAAMRTmiQQQGGSIVNVGHRREmlLHKRSIVglkgnsgqsvySAS 161
Cdd:PRK08862  93 SSPLPSLFDEQPSESFIQQLSSLASTLFTygqvAAERMRK--RNKKGVIVNVISHDD--HQDLTGV-----------ESS 157

                        170       180
                 ....*....|....*....|....*..
gi 578809569 162 KGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08862 158 NALVSGFTHSWAKELTPFNIRVGGVVP 184

PLN02780

ketoreductase/ oxidoreductase

7-191

1.67e-05

ketoreductase/ oxidoreductase

Pssm-ID: 166421 [Multi-domain] Cd Length: 320 Bit Score: 44.47 E-value: 1.67e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH---------LAFSCDVAKE-HDVQNTFEELEkhlgr 76
Cdd:PLN02780  58 VTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYsktqiktvvVDFSGDIDEGvKRIKETIEGLD----- 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  77 VNFLVNAAGINRD-GLLVRTKTEDMVSQL-HTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREMLLHKRSIVglkgnsg 154
Cdd:PLN02780 133 VGVLINNVGVSYPyARFFHEVDEELLKNLiKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVIPSDPLY------- 205

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 578809569 155 qSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PLN02780 206 -AVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYV 241

haloalcohol_DH_SDR_c-like

cd05361

haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...

60-188

1.78e-05

haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. Haloalcohol dehalogenase show low sequence similarity to short-chain dehydrogenases/reductases (SDRs). Like the SDRs, haloalcohol dehalogenases have a conserved catalytic triad (Ser-Tyr-Lys/Arg), and form a Rossmann fold. However, the normal classical SDR NAD(P)-binding motif (TGXXGXG) and NAD-binding function is replaced with a halide binding site, allowing the enzyme to catalyze a dehalogenation reaction. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187619 [Multi-domain] Cd Length: 242 Bit Score: 44.10 E-value: 1.78e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  60 EHDVQNTFEELEKHLGRVNFLVNAAGINRD-GLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrre 138
Cdd:cd05361   56 EQKPEELVDAVLQAGGAIDVLVSNDYIPRPmNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFI----- 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 578809569 139 mllhkRSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05361  131 -----TSAVPKKPLAYNSLYGPARAAAVALAESLAKELSRDNILVYAIGP 175

PRK08340

SDR family oxidoreductase;

7-85

1.90e-05

SDR family oxidoreductase;

Pssm-ID: 169390 [Multi-domain] Cd Length: 259 Bit Score: 44.03 E-value: 1.90e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG--GDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAA 84
Cdd:PRK08340   5 VTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKeyGEVYAVKADLSDKDDLKNLVKEAWELLGGIDALVWNA 84


                 .
gi 578809569  85 G 85
Cdd:PRK08340  85 G 85

WcaG

COG0451

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];

7-120

2.07e-05

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];

Pssm-ID: 440220 [Multi-domain] Cd Length: 295 Bit Score: 44.20 E-value: 2.07e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLafscdvakEHDVQNtFEELEKHLGRVNFLVNAAGI 86
Cdd:COG0451    4 VTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGVEFV--------RGDLRD-PEALAAALAGVDAVVHLAAP 74

                         90       100       110
                 ....*....|....*....|....*....|....
gi 578809569  87 nrdgllVRTKTEDMVSQLHTNLLGSMLTCKAAMR 120
Cdd:COG0451   75 ------AGVGEEDPDETLEVNVEGTLNLLEAARA 102

PRK08690

enoyl-[acyl-carrier-protein] reductase FabI;

11-203

2.30e-05

enoyl-[acyl-carrier-protein] reductase FabI;

Pssm-ID: 169553 [Multi-domain] Cd Length: 261 Bit Score: 43.80 E-value: 2.30e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  11 SRGIGRAVAQLMARKGYRLA---VIARNLEGAKAAAGDLGGDhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGIN 87
Cdd:PRK08690  17 ERSIAYGIAKACREQGAELAftyVVDKLEERVRKMAAELDSE-LVFRCDVASDDEINQVFADLGKHWDGLDGLVHSIGFA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  88 -RDGL---LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHrremLLHKRSIvglkgnSGQSVYSASKG 163
Cdd:PRK08690  96 pKEALsgdFLDSISREAFNTAHEISAYSLPALAKAARPMMRGRNSAIVALSY----LGAVRAI------PNYNVMGMAKA 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 578809569 164 GLVGFSRALAKEVARKKIRVNVVA--PVTILVWSLFCTFASI 203
Cdd:PRK08690 166 SLEAGIRFTAACLGKEGIRCNGISagPIKTLAASGIADFGKL 207

PRK06603

enoyl-[acyl-carrier-protein] reductase FabI;

14-203

5.97e-05

enoyl-[acyl-carrier-protein] reductase FabI;

Pssm-ID: 168626 [Multi-domain] Cd Length: 260 Bit Score: 42.69 E-value: 5.97e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  14 IGRAVAQLMARKG------YRLAVIARNLegaKAAAGDLGGDHLAfSCDVAKEHDVQNTFEELEKHLGRVNFLVNA-AGI 86
Cdd:PRK06603  22 ISWAIAQLAKKHGaelwftYQSEVLEKRV---KPLAEEIGCNFVS-ELDVTNPKSISNLFDDIKEKWGSFDFLLHGmAFA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  87 NRD---GLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGHR-REMLLHKRSIVGLkgnsgqsvysaSK 162
Cdd:PRK06603  98 DKNelkGRYVDTSLENFHNSLHISCYSLLELSRSAEALM--HDGGSIVTLTYYgAEKVIPNYNVMGV-----------AK 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 578809569 163 GGLVGFSRALAKEVARKKIRVNVVA--PVTILVWSLFCTFASI 203
Cdd:PRK06603 165 AALEASVKYLANDMGENNIRVNAISagPIKTLASSAIGDFSTM 207

PRK08159

enoyl-[acyl-carrier-protein] reductase FabI;

43-191

6.85e-05

enoyl-[acyl-carrier-protein] reductase FabI;

Pssm-ID: 181260 [Multi-domain] Cd Length: 272 Bit Score: 42.43 E-value: 6.85e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  43 AGDLGGDhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGINR----DGLLVRTKTEDMVSQLHTNLLGSMLTCKAA 118
Cdd:PRK08159  56 AAELGAF-VAGHCDVTDEASIDAVFETLEKKWGKLDFVVHAIGFSDkdelTGRYVDTSRDNFTMTMDISVYSFTAVAQRA 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578809569 119 MRTMiqQQGGSIVNV---GHRREMllhkrsivglkgnSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK08159 135 EKLM--TDGGSILTLtyyGAEKVM-------------PHYNVMGVAKAALEASVKYLAVDLGPKNIRVNAISAGPI 195

DR_C-13_KR_SDR_c_like

cd08951

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...

9-188

8.01e-05

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187654 [Multi-domain] Cd Length: 260 Bit Score: 42.09 E-value: 8.01e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKhLGRVNFLVNAAGINR 88
Cdd:cd08951   14 GSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSSLAETRKLADQVNA-IGRFDAVIHNAGILS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  89 DGlLVRTKTEDMVSQLHTNLLGS-MLTCKAA-------MRTMIQQQGGSIVNvghrrEMLLHKRsivglkGNSGQSVYSA 160
Cdd:cd08951   93 GP-NRKTPDTGIPAMVAVNVLAPyVLTALIRrpkrliyLSSGMHRGGNASLD-----DIDWFNR------GENDSPAYSD 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 578809569 161 SKgglvGFSRALAKEVAR--KKIRVNVVAP 188
Cdd:cd08951  161 SK----LHVLTLAAAVARrwKDVSSNAVHP 186

PRK08594

enoyl-[acyl-carrier-protein] reductase FabI;

12-191

8.49e-05

enoyl-[acyl-carrier-protein] reductase FabI;

Pssm-ID: 236308 [Multi-domain] Cd Length: 257 Bit Score: 42.02 E-value: 8.49e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  12 RGIGRAVAQLMARKGYRLAVI---ARNLEGAKAAAGDLGG-DHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA-AGI 86
Cdd:PRK08594  19 RSIAWGIARSLHNAGAKLVFTyagERLEKEVRELADTLEGqESLLLPCDVTSDEEITACFETIKEEVGVIHGVAHCiAFA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  87 NRD---GLLVRTKTEDMVsqLHTNLLGSMLT--CKAAMRTMiqQQGGSIVNVGHrremllhkrsIVGLKGNSGQSVYSAS 161
Cdd:PRK08594  99 NKEdlrGEFLETSRDGFL--LAQNISAYSLTavAREAKKLM--TEGGSIVTLTY----------LGGERVVQNYNVMGVA 164

                        170       180       190
                 ....*....|....*....|....*....|
gi 578809569 162 KGGLVGFSRALAKEVARKKIRVNVVAPVTI 191
Cdd:PRK08594 165 KASLEASVKYLANDLGKDGIRVNAISAGPI 194

PRK08416

enoyl-ACP reductase;

3-187

9.40e-05

enoyl-ACP reductase;

Pssm-ID: 181417 [Multi-domain] Cd Length: 260 Bit Score: 42.07 E-value: 9.40e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLA-VIARNLEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK08416   9 KTLVISGGTRGIGKAIVYEFAQSGVNIAfTYNSNVEEANKIAEDLeqkyGIKAKAYPLNILEPETYKELFKKIDEDFDRV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  78 NFLVNAAGINRD------GLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkrsivglkG 151
Cdd:PRK08416  89 DFFISNAIISGRavvggyTKFMRLKPKGLNNIYTATVNAFVVGAQEAAKRMEKVGGGSIISL-----------------S 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 578809569 152 NSGQSVY-------SASKGGLVGFSRALAKEVARKKIRVNVVA 187
Cdd:PRK08416 152 STGNLVYienyaghGTSKAAVETMVKYAATELGEKNIRVNAVS 194

Sacchrp_dh_NADP

pfam03435

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...

10-94

9.49e-05

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.

Pssm-ID: 397480 [Multi-domain] Cd Length: 120 Bit Score: 40.27 E-value: 9.49e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   10 GSRGIGRAVAQLMARKG--YRLAVIARNLEGAKAAAGDLGGDHLafscdVAKEHDVQNTFEELEKHLGRVNFLVNAAGIN 87
Cdd:pfam03435   5 GAGSVGQGVAPLLARHFdvDRITVADRTLEKAQALAAKLGGVRF-----IAVAVDADNYEAVLAALLKEGDLVVNLSPPT 79


                  ....*..
gi 578809569   88 RDGLLVR 94
Cdd:pfam03435  80 LSLDVLK 86

LPOR_like_SDR_c_like

cd09810

light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...

7-116

1.27e-04

light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical SDR-like subgroup containing LPOR and related proteins. Protochlorophyllide (Pchlide) reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187670 [Multi-domain] Cd Length: 311 Bit Score: 41.73 E-value: 1.27e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIA-RNLEGAKAAAGDLG---GDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd09810    6 ITGASSGLGLAAAKALARRGEWHVVMAcRDFLKAEQAAQEVGmpkDSYSVLHCDLASLDSVRQFVDNFRRTGRPLDALVC 85

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 578809569  83 AAGINRDGLLVRTKTEDMVSQ-LHTNLLGSMLTCK 116
Cdd:cd09810   86 NAAVYLPTAKEPRFTADGFELtVGVNHLGHFLLTN 120

PRK06196

oxidoreductase; Provisional

3-137

1.28e-04

oxidoreductase; Provisional

Pssm-ID: 235736 [Multi-domain] Cd Length: 315 Bit Score: 41.59 E-value: 1.28e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAfSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK06196  27 KTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGIDGVEVV-MLDLADLESVRAFAERFLDSGRRIDILIN 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809569  83 AAGINRDGLlvrTKTED-MVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNV---GHRR 137
Cdd:PRK06196 106 NAGVMACPE---TRVGDgWEAQFATNHLGHFALVNLLWPALAAGAGARVVALssaGHRR 161

PRK06197

short chain dehydrogenase; Provisional

3-136

1.52e-04

short chain dehydrogenase; Provisional

Pssm-ID: 235737 [Multi-domain] Cd Length: 306 Bit Score: 41.55 E-value: 1.52e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK06197  17 RVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARItaatpGADVTLQELDLTSLASVRAAADALRAAYPRI 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578809569  78 NFLVNAAGINrdgLLVRTKTEDMVS-QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNV---GHR 136
Cdd:PRK06197  97 DLLINNAGVM---YTPKQTTADGFElQFGTNHLGHFALTGLLLDRLLPVPGSRVVTVssgGHR 156

NDUFA9_like_SDR_a

cd05271

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...

3-89

1.57e-04

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.

Pssm-ID: 187579 [Multi-domain] Cd Length: 273 Bit Score: 41.46 E-value: 1.57e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAA--AGDLGGdHLAFSCDVAkehdvqnTFEELEKHLGRVNFL 80
Cdd:cd05271    1 MVVTVFGATGFIGRYVVNRLAKRGSQVIVPYRCEAYARRLlvMGDLGQ-VLFVEFDLR-------DDESIRKALEGSDVV 72


                 ....*....
gi 578809569  81 VNAAGINRD 89
Cdd:cd05271   73 INLVGRLYE 81

PRK07102

SDR family oxidoreductase;

7-188

1.93e-04

SDR family oxidoreductase;

Pssm-ID: 180838 [Multi-domain] Cd Length: 243 Bit Score: 41.06 E-value: 1.93e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFScdvakEHDVqNTFEE----LEKHLGRVNF 79
Cdd:PRK07102   6 IIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLrarGAVAVSTH-----ELDI-LDTAShaafLDSLPALPDI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK07102  80 VLIAVGTLGDQAACEADPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGIS----------SVAGDRGRASNYVYG 149

                        170       180
                 ....*....|....*....|....*....
gi 578809569 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07102 150 SAKAALTAFLSGLRNRLFKSGVHVLTVKP 178

PRK05993

SDR family oxidoreductase;

1-188

2.61e-04

SDR family oxidoreductase;

Pssm-ID: 180343 [Multi-domain] Cd Length: 277 Bit Score: 40.78 E-value: 2.61e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAaagdLGGDHL-AFSCDVAKEHDVQNTFEE-LEKHLGRVN 78
Cdd:PRK05993   3 MKRSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAA----LEAEGLeAFQLDYAEPESIAALVAQvLELSGGRLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLG-SMLTCKA--AMRTmiqQQGGSIVnvghrremllHKRSIVGLKGNSGQ 155
Cdd:PRK05993  79 ALFNNGAYGQPGAVEDLPTEALRAQFEANFFGwHDLTRRVipVMRK---QGQGRIV----------QCSSILGLVPMKYR 145

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809569 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK05993 146 GAYNASKFAIEGLSLTLRMELQGSGIHVSLIEP 178

3alpha_HSD_SDR_c

cd05328

alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...

6-188

2.73e-04

alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, which catalyzes the NAD-dependent oxidoreduction of hydroxysteroids, is a dimeric member of the classical SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187589 [Multi-domain] Cd Length: 250 Bit Score: 40.56 E-value: 2.73e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   6 AVFGGSRGIGRAVAQLMARKGYRlaVIARNLEGAKAAAgDLGgdhlafscdvAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:cd05328    3 VITGAASGIGAATAELLEDAGHT--VIGIDLREADVIA-DLS----------TPEGRAAAIADVLARCSGVLDGLVNCAG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  86 INrdgllVRTKTEDMVSqlhTNLLGSMLTCKAAMRTMIQQQGGSIVNVG-------HRREMLLHK----------RSIVG 148
Cdd:cd05328   70 VG-----GTTVAGLVLK---VNYFGLRALMEALLPRLRKGHGPAAVVVSsiagagwAQDKLELAKalaagtearaVALAE 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 578809569 149 LKGNSGQSVYSASKGGLVGFSRALAKE-VARKKIRVNVVAP 188
Cdd:cd05328  142 HAGQPGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAP 182

PRK05884

SDR family oxidoreductase;

7-188

1.59e-03

SDR family oxidoreductase;

Pssm-ID: 135642 [Multi-domain] Cd Length: 223 Bit Score: 38.25 E-value: 1.59e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDhlAFSCDVAKEHDVQNTFEELEKHLgrvNFLVN---- 82
Cdd:PRK05884   5 VTGGDTDLGRTIAEGFRNDGHKVTLVGARRDDLEVAAKELDVD--AIVCDNTDPASLEEARGLFPHHL---DTIVNvpap 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  83 --AAGINRDGLLVRTKTEdMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVghrremllhkrsiVGLKGNSGqSVYSA 160
Cdd:PRK05884  80 swDAGDPRTYSLADTANA-WRNALDATVLSAVLTVQSVGDHL--RSGGSIISV-------------VPENPPAG-SAEAA 142

                        170       180
                 ....*....|....*....|....*...
gi 578809569 161 SKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK05884 143 IKAALSNWTAGQAAVFGTRGITINAVAC 170

YwnB

COG2910

Putative NADH-flavin reductase [General function prediction only];

6-46

1.85e-03

Putative NADH-flavin reductase [General function prediction only];

Pssm-ID: 442154 [Multi-domain] Cd Length: 205 Bit Score: 37.91 E-value: 1.85e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 578809569   6 AVFGGSRGIGRAVAQLMARKGYRLAVIARN-------LEGAKAAAGDL 46
Cdd:COG2910    3 AVIGATGRVGSLIVREALARGHEVTALVRNpeklpdeHPGLTVVVGDV 50

PRK08655

prephenate dehydrogenase; Provisional

6-63

3.39e-03

prephenate dehydrogenase; Provisional

Pssm-ID: 236326 [Multi-domain] Cd Length: 437 Bit Score: 37.66 E-value: 3.39e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 578809569   6 AVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDV 63
Cdd:PRK08655   4 SIIGGTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKELGVEYANDNIDAAKDADI 61

NAD_bind_H4MPT_DH

cd01078

NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...

2-43

3.73e-03

NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.

Pssm-ID: 133446 [Multi-domain] Cd Length: 194 Bit Score: 36.99 E-value: 3.73e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 578809569   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA 43
Cdd:cd01078   28 GKTAVVLGGTGPVGQRAAVLLAREGARVVLVGRDLERAQKAA 69

COG5322

Predicted amino acid dehydrogenase [General function prediction only];

6-50

4.31e-03

Predicted amino acid dehydrogenase [General function prediction only];

Pssm-ID: 444114 [Multi-domain] Cd Length: 362 Bit Score: 37.13 E-value: 4.31e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 578809569   6 AVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH 50
Cdd:COG5322  155 AVVGATGSIGSVCARLLAREVKRLTLVARNLERLEELAEEILRNP 199

PRK06953

SDR family oxidoreductase;

7-165

7.12e-03

SDR family oxidoreductase;

Pssm-ID: 180774 [Multi-domain] Cd Length: 222 Bit Score: 36.20 E-value: 7.12e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAkAAAGDLGGDhlAFSCDVAKEHDVQNTFEELEKHlgRVNFLVNAAGI 86
Cdd:PRK06953   6 IVGASRGIGREFVRQYRADGWRVIATARDAAAL-AALQALGAE--ALALDVADPASVAGLAWKLDGE--ALDAAVYVAGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569  87 --NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMrTMIQQQGGSIVNVGHRREmllhkrSIVGLKGNSGQsVYSASKGG 164
Cdd:PRK06953  81 ygPRTEGVEPITREDFDAVMHTNVLGPMQLLPILL-PLVEAAGGVLAVLSSRMG------SIGDATGTTGW-LYRASKAA 152


                 .
gi 578809569 165 L 165
Cdd:PRK06953 153 L 153

PRK06997

enoyl-[acyl-carrier-protein] reductase FabI;

11-85

7.14e-03

enoyl-[acyl-carrier-protein] reductase FabI;

Pssm-ID: 180789 [Multi-domain] Cd Length: 260 Bit Score: 36.34 E-value: 7.14e-03

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578809569  11 SRGIGRAVAQLMARKGYRLA---VIARNLEGAKAAAGDLGGDhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:PRK06997  17 NRSIAYGIAKACKREGAELAftyVGDRFKDRITEFAAEFGSD-LVFPCDVASDEQIDALFASLGQHWDGLDGLVHSIG 93

DHRS-12_like_SDR_c-like

cd09808

human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...

7-91

9.65e-03

human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like SDRs; Classical SDR-like subgroup containing human DHRS-12/FLJ13639, the 36K protein of zebrafish CNS myelin, and related proteins. DHRS-12/FLJ13639 is expressed in neurons and oligodendrocytes in the human cerebral cortex. Proteins in this subgroup share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187668 [Multi-domain] Cd Length: 255 Bit Score: 36.03 E-value: 9.65e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFS--CDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:cd09808    6 ITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIeteSGNQNIFLhiVDMSDPKQVWEFVEEFKEEGKKLHVLI 85

                         90
                 ....*....|....*..
gi 578809569  82 NAAG-------INRDGL 91
Cdd:cd09808   86 NNAGcmvnkreLTEDGL 102

PRK06940

short chain dehydrogenase; Provisional

1-86

9.92e-03

short chain dehydrogenase; Provisional

Pssm-ID: 180766 [Multi-domain] Cd Length: 275 Bit Score: 36.15 E-value: 9.92e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809569   1 MDKVCAVFGgSRGIGRAVAQLMArKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKhLGRV 77
Cdd:PRK06940   1 MKEVVVVIG-AGGIGQAIARRVG-AGKKVLLADYNEENLEAAAKTLreaGFDVSTQEVDVSSRESVKALAATAQT-LGPV 77


                 ....*....
gi 578809569  78 NFLVNAAGI 86
Cdd:PRK06940  78 TGLVHTAGV 86

Blast search parameters

Data Source:	Precalculated data, version = cdd.v.3.21
Preset Options:	Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01