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Conserved domains on  [gi|4758504|ref|NP_004484.1|]
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3-hydroxyacyl-CoA dehydrogenase type-2 isoform 1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
9-261 2.34e-163

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: 455.98  E-value: 2.34e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKkLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05371   1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAK-LGDNCRFVPVDVTSEKDVKAALALAKAKFGRLDIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   89 VNCAGIAVASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAY 168
Cdd:cd05371  80 VNCAGIAVAAKTYNKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNEPDQGGERGVIINTASVAAFEGQIGQAAY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  169 SASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENPFLNG 248
Cdd:cd05371 160 SASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEKVRDFLAKQVPFPSRLGDPAEYAHLVQHIIENPYLNG 239
                       250
                ....*....|...
gi 4758504  249 EVIRLDGAIRMQP 261
Cdd:cd05371 240 EVIRLDGAIRMPP 252
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
7-260 1.67e-59

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


:

Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 191.18  E-value: 1.67e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504     7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGG----EAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:PRK05557   2 SLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGaealVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    83 GRVDVAVNCAGIAvasktyNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdqgGQRGVIINTASVAAFEGQ 162
Cdd:PRK05557  82 GGVDILVNNAGIT------RDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMK------QRSGRIINISSVVGLMGN 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   163 VGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFPsRLGDPAEYAHLVQ--AI 240
Cdd:PRK05557 150 PGQANYAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDVKEAILAQIPLG-RLGQPEEIASAVAflAS 228
                        250       260
                 ....*....|....*....|
gi 4758504   241 IENPFLNGEVIRLDGAIRMQ 260
Cdd:PRK05557 229 DEAAYITGQTLHVNGGMVMG 248
 
Name Accession Description Interval E-value
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
9-261 2.34e-163

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: 455.98  E-value: 2.34e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKkLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05371   1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAK-LGDNCRFVPVDVTSEKDVKAALALAKAKFGRLDIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   89 VNCAGIAVASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAY 168
Cdd:cd05371  80 VNCAGIAVAAKTYNKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNEPDQGGERGVIINTASVAAFEGQIGQAAY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  169 SASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENPFLNG 248
Cdd:cd05371 160 SASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEKVRDFLAKQVPFPSRLGDPAEYAHLVQHIIENPYLNG 239
                       250
                ....*....|...
gi 4758504  249 EVIRLDGAIRMQP 261
Cdd:cd05371 240 EVIRLDGAIRMPP 252
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-255 1.27e-30

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


Pssm-ID: 180617  Cd Length: 235  Bit Score: 115.06  E-value: 1.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    12 VAVITGGASGLGLATAERLVGQGASAVLLDLpnsggeAQAKKLGNNCVFAPADVTSEkdvqtaLALAKGKFGRVDVAVNC 91
Cdd:PRK06550   7 TVLITGAASGIGLAQARAFLAQGAQVYGVDK------QDKPDLSGNFHFLQLDLSDD------LEPLFDWVPSVDILCNT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    92 AGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQAAYSAS 171
Cdd:PRK06550  75 AGILDDYKPL-----LDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLER------KSGIIINMCSIASFVAGGGGAAYTAS 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   172 KGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTS--LPEKVCNFLASQVPFpSRLGDPAEYAHLV------QAiien 243
Cdd:PRK06550 144 KHALAGFTKQLALDYAKDGIQVFGIAPGAVKTPMTAAdfEPGGLADWVARETPI-KRWAEPEEVAELTlflasgKA---- 218
                        250
                 ....*....|..
gi 4758504   244 PFLNGEVIRLDG 255
Cdd:PRK06550 219 DYMQGTIVPIDG 230
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyses the ...
14-170 3.56e-14

KR domain; This enzymatic domain is part of bacterial polyketide synthases and 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: 254956  Cd Length: 181  Bit Score: 67.55  E-value: 3.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504     14 VITGGASGLGLATAERLVGQGASAVLL----DLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:pfam08659   4 LVTGGLGGLGLELARWLAERGARHLVLlsrsGAPDPEAEALLAELearGAEVTVVACDVSDRDAVRALLAEIRADGPPLR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504     87 VAVNCAGIavasktynLKKG--QTHTLEDFQRVLDVNLMGTFNVIRLVAGEmgqnEPDqggqrgVIINTASVAAFEGQVG 164
Cdd:pfam08659  84 GVIHAAGV--------LRDAllANMTAEDFARVLAPKVTGAWNLHEATRDR----PLD------FFVLFSSIAGVLGSPG 145

                  ....*.
gi 4758504    165 QAAYSA 170
Cdd:pfam08659 146 QANYAA 151
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
14-170 6.75e-13

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  Cd Length: 180  Bit Score: 63.66  E-value: 6.75e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504      14 VITGGASGLGLATAERLVGQGASAVLL----DLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARRLVLlsrsGPDAPGAAALLAELeaaGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504      87 VAVNCAGIAvasktyNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEmgqnEPDqggqrgVIINTASVAAFEGQVGQA 166
Cdd:smart00822  84 GVIHAAGVL------DDGVLASLTPERFAAVLAPKAAGAWNLHELTADL----PLD------FFVLFSSIAGVLGSPGQA 147

                   ....
gi 4758504     167 AYSA 170
Cdd:smart00822 148 NYAA 151
PLN00015 PLN00015
protochlorophyllide reductase
14-163 8.22e-04

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 38.53  E-value: 8.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    14 VITGGASGLGLATAERLVGQGASAVLLDLPN-SGGEAQAKKLG---NNCVFAPADVTSEKDVQTALALAKGKFGRVDVAV 89
Cdd:PLN00015   1 IITGASSGLGLATAKALAETGKWHVVMACRDfLKAERAAKSAGmpkDSYTVMHLDLASLDSVRQFVDNFRRSGRPLDVLV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4758504    90 NCAgiAVASKTynlKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnePDQGGQRGVII-----NTASVAafeGQV 163
Cdd:PLN00015  81 CNA--AVYLPT---AKEPTFTADGFELSVGTNHLGHFLLSRLLLDDLKK--SDYPSKRLIIVgsitgNTNTLA---GNV 149
Sepiapterin_reductase TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
12-203 3.96e-03

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  Cd Length: 256  Bit Score: 36.43  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504     12 VAVITGGASGLGLATAERLV----GQGASAVLLD-----LPNSGGEAQAKKLGNNCVFAPADVTSEKDVQ--TALALAKG 80
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAkclkSPGSVLVLSArndeaLRQLKAEIGAERSGLRVVRVSLDLGAEAGLEqlLKALRELP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504     81 K---FGRVDVAVNcagiavASKTYNLKKGQTHtLEDFQRVLDVNLMGTFNVIRLVAgEMGQNEPDQGGQRGVIINTASVA 157
Cdd:TIGR01500  82 RpkgLQRLLLINN------AGTLGDVSKGFVD-LSDSTQVQNYWALNLTSMLCLTS-SVLKAFKDSPGLNRTVVNISSLC 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 4758504    158 AFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGT 203
Cdd:TIGR01500 154 AIQPFKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDT 199
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
7-260 1.67e-59

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 191.18  E-value: 1.67e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504     7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGG----EAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:PRK05557   2 SLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGaealVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    83 GRVDVAVNCAGIAvasktyNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdqgGQRGVIINTASVAAFEGQ 162
Cdd:PRK05557  82 GGVDILVNNAGIT------RDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMK------QRSGRIINISSVVGLMGN 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   163 VGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFPsRLGDPAEYAHLVQ--AI 240
Cdd:PRK05557 150 PGQANYAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDVKEAILAQIPLG-RLGQPEEIASAVAflAS 228
                        250       260
                 ....*....|....*....|
gi 4758504   241 IENPFLNGEVIRLDGAIRMQ 260
Cdd:PRK05557 229 DEAAYITGQTLHVNGGMVMG 248
FabG COG1028
Dehydrogenases with different specificities (related to short-chain alcohol dehydrogenases) ...
12-258 4.25e-49

Dehydrogenases with different specificities (related to short-chain alcohol dehydrogenases) [Secondary metabolites biosynthesis, transport, and catabolism / General function prediction only]


Pssm-ID: 223959 [Multi-domain]  Cd Length: 251  Bit Score: 164.22  E-value: 4.25e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQA------KKLGNNCVFAPADVTS-EKDVQTALALAKGKFGR 84
Cdd:COG1028   7 VALVTGASSGIGRAIARALAREGARVVVAARRSEEEAAEAlaaaikEAGGGRAAAVAADVSDdEESVEALVAAAEEEFGR 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   85 VDVAVNCAGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdqggQRGVIINTASVAAFEGQVG 164
Cdd:COG1028  87 IDILVNNAGIAGPDAPL-----EELTEEDWDRVIDVNLLGAFLLTRAALPLM---------KKQRIVNISSVAGLGGPPG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  165 QAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCN---FLASQVPFPsRLGDPAEYAHLVQAII 241
Cdd:COG1028 153 QAAYAASKAALIGLTKALALELAPRGIRVNAVAPGYIDTPMTAALESAELEalkRLAARIPLG-RLGTPEEVAAAVAFLA 231
                       250       260
                ....*....|....*....|
gi 4758504  242 ---ENPFLNGEVIRLDGAIR 258
Cdd:COG1028 232 sdeAASYITGQTLPVDGGLL 251
3-oxoacyl-_reductase_FabG TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
13-257 3.69e-46

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 156.21  E-value: 3.69e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504     13 AVITGGASGLGLATAERLVGQGASAVLLDLPNSGG----EAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGaeevVEELKALGVKALGVVLDVSDREDVKAVVEEIEEELGTIDIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504     89 VNCAGIAVASKTYNLKKgqthtlEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRGVIINTASVAAFEGQVGQAAY 168
Cdd:TIGR01830  81 VNNAGITRDNLLMRMKE------EDWDAVIDTNLTGVFNLTQAVLRIM------IKQRSGRIINISSVVGLMGNAGQANY 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    169 SASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFpSRLGDPAEYAHLVQ--AIIENPFL 246
Cdd:TIGR01830 149 AASKAGVIGFTKSLAKELASRNITVNAVAPGFIDTDMTDKLSEKVKKKILSQIPL-GRFGQPEEVANAVAflASDEASYI 227
                         250
                  ....*....|.
gi 4758504    247 NGEVIRLDGAI 257
Cdd:TIGR01830 228 TGQVIHVDGGM 238
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
12-179 2.11e-28

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


Pssm-ID: 249592 [Multi-domain]  Cd Length: 167  Bit Score: 107.25  E-value: 2.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504     12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAK------KLGNNCVFAPADVTSEKDVQTALALAKGKFGRV 85
Cdd:pfam00106   2 TVLITGGTGGLGLALARWLAAEGARHLVLVSRRGDAPGAAElvaeleALGAEVTVAACDVADRDALAALLAALPAALGPL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504     86 DVAVNCAGI---AVASKTynlkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEmgqnepdqggQRGVIINTASVAAFEGQ 162
Cdd:pfam00106  82 DGVVHNAGVlddGPLEEL---------TPERFERVLAPKVTGAWNLHELTRDL----------DLGAFVLFSSVAGVLGS 142
                         170
                  ....*....|....*..
gi 4758504    163 VGQAAYSASKGGIVGMT 179
Cdd:pfam00106 143 PGQANYAAANAALDALA 159
PLN02253 PLN02253
xanthoxin dehydrogenase
5-211 3.10e-28

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 109.53  E-value: 3.10e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504     5 CRSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGN--NCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:PLN02253  13 SQRLLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGepNVCFFHCDVTVEDDVSRAVDFTVDKF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    83 GRVDVAVNCAGIAvASKTYNLKKgqtHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQ 162
Cdd:PLN02253  93 GTLDIMVNNAGLT-GPPCPDIRN---VELSEFEKVFDVNVKGVFLGMKHAARIMIPL------KKGSIVSLCSVASAIGG 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 4758504   163 VGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPL-LTSLPE 211
Cdd:PLN02253 163 LGPHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALaLAHLPE 212
 
Name Accession Description Interval E-value
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
9-261 2.34e-163

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: 455.98  E-value: 2.34e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKkLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05371   1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAK-LGDNCRFVPVDVTSEKDVKAALALAKAKFGRLDIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   89 VNCAGIAVASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAY 168
Cdd:cd05371  80 VNCAGIAVAAKTYNKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNEPDQGGERGVIINTASVAAFEGQIGQAAY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  169 SASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENPFLNG 248
Cdd:cd05371 160 SASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEKVRDFLAKQVPFPSRLGDPAEYAHLVQHIIENPYLNG 239
                       250
                ....*....|...
gi 4758504  249 EVIRLDGAIRMQP 261
Cdd:cd05371 240 EVIRLDGAIRMPP 252
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
13-254 2.41e-61

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: 195.20  E-value: 2.41e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   13 AVITGGASGLGLATAERLVGQGASAVLLDLPNSGGE--AQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVN 90
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAelAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   91 CAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRGVIINTASVAAFEGQVGQAAYSA 170
Cdd:cd05233  81 NAGIARPGPLEEL------TDEDWDRVLDVNLTGVFLLTRAALPHM------KKQGGGRIVNISSVAGLRPLPGQAAYAA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  171 SKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENP--FLNG 248
Cdd:cd05233 149 SKAALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAAIPLGRLGTPEEVAEAVVFLASDEasYITG 228

                ....*.
gi 4758504  249 EVIRLD 254
Cdd:cd05233 229 QVIPVD 234
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
12-255 7.82e-55

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: 178.90  E-value: 7.82e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEA---QAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05333   2 VALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAEtveEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDIL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   89 VNCAGIAVASKTYNLKKgqthtlEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQAAY 168
Cdd:cd05333  82 VNNAGITRDNLLMRMSE------EDWDAVINVNLTGVFNVTQAVIRAMIKR------RSGRIINISSVVGLIGNPGQANY 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  169 SASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFpSRLGDPAEYAHLVQAIIENP--FL 246
Cdd:cd05333 150 AASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPL-GRLGTPEEVANAVAFLASDDasYI 228

                ....*....
gi 4758504  247 NGEVIRLDG 255
Cdd:cd05333 229 TGQVLHVNG 237
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
7-257 5.01e-50

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: 166.40  E-value: 5.01e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:cd05341   2 RLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFGRLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   87 VAVNCAGIAVasktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnePDQGGqrGVIINTASVAAFEGQVGQA 166
Cdd:cd05341  82 VLVNNAGILT------GGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPM----KEAGG--GSIINMSSIEGLVGDPALA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  167 AYSASKGGIVGMTLPIARDLAPI--GIRVMTIAPGLFGTPLLTSLPEKVcnfLASQVPFPS---RLGDPAEYAHLVQAII 241
Cdd:cd05341 150 AYNASKGAVRGLTKSAALECATQgyGIRVNSVHPGYIYTPMTDELLIAQ---GEMGNYPNTpmgRAGEPDEIAYAVVYLA 226
                       250
                ....*....|....*...
gi 4758504  242 --ENPFLNGEVIRLDGAI 257
Cdd:cd05341 227 sdESSFVTGSELVVDGGY 244
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
12-255 6.65e-44

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: 150.53  E-value: 6.65e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEA---QAKKLGNNCVFAPADVTSeKDVQTALAL-AKGKFGRVDV 87
Cdd:cd05323   2 VAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAaelQAINPKVKATFVQCDVTS-WEQLAAAFKkAIEKFGRVDI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   88 AVNCAGIAVASKTYNLKKGQthtlEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdQGGQRGVIINTASVAAFEGQVGQAA 167
Cdd:cd05323  81 LINNAGILDEKSYLFAGKLP----PPWEKTIDVNLTGVINTTYLALHYMDKN---KGGKGGVIVNIGSVAGLYPAPQFPV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  168 YSASKGGIVGMTlpiaRDLAPI-----GIRVMTIAPGLFGTPLLTSLPEKVCNFLASQvPFPSrlgdPAEYAHLVQAIIE 242
Cdd:cd05323 154 YSASKHGVVGFT----RSLADLleyktGVRVNAICPGFTNTPLLPDLVAKEAEMLPSA-PTQS----PEVVAKAIVYLIE 224
                       250
                ....*....|...
gi 4758504  243 NPFLNGEVIRLDG 255
Cdd:cd05323 225 DDEKNGAIWIVDG 237
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
10-256 1.63e-43

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: 149.46  E-value: 1.63e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAV 89
Cdd:cd05345   5 GKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFGRLDILV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   90 NCAGIavaskTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRGVIINTASVAAFEGQVGQAAYS 169
Cdd:cd05345  85 NNAGI-----THRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHM------EEQGGGVIINIASTAGLRPRPGLTWYN 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  170 ASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSL-----PEKVCNFLASqVPFpSRLGDPAEYAH--LVQAIIE 242
Cdd:cd05345 154 ASKGWVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFmgedtPENRAKFRAT-IPL-GRLSTPDDIANaaLYLASDE 231
                       250
                ....*....|....
gi 4758504  243 NPFLNGEVIRLDGA 256
Cdd:cd05345 232 ASFITGVALEVDGG 245
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
12-259 4.52e-41

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: 143.29  E-value: 4.52e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNsggEAQAKKL-------GNNCVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:cd05366   4 VAIITGAAQGIGRAIAERLAADGFNIVLADLNL---EEAAKSTiqeiseaGYNAVAVGADVTDKDDVEALIDQAVEKFGS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   85 VDVAVNCAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepDQGGQRGVIINTASVAAFEGQVG 164
Cdd:cd05366  81 FDVMVNNAGIAPITPL------LTITEEDLKKVYAVNVFGVLFGIQAAARQF-----KKLGHGGKIINASSIAGVQGFPN 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  165 QAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCN-----------FLASQVPFpSRLGDPAEY 233
Cdd:cd05366 150 LGAYSASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVGEiagkpegegfaEFSSSIPL-GRLSEPEDV 228
                       250       260
                ....*....|....*....|....*...
gi 4758504  234 AHLVQ--AIIENPFLNGEVIRLDGAIRM 259
Cdd:cd05366 229 AGLVSflASEDSDYITGQTILVDGGMVY 256
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
9-261 2.56e-39

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: 138.67  E-value: 2.56e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    9 KGLVAVITGGASGLGLATAERLVGQGAsAVLLDLpNSGGEA------QAKKLGNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:cd05358   2 KGKVALVTGASSGIGKAIAIRLATAGA-NVVVNY-RSKEDAaeevveEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   83 GRVDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEpdqggQRGVIINTASVAAFEGQ 162
Cdd:cd05358  80 GTLDILVNNAGLQGDASSHEM------TLEDWNKVIDVNLTGQFLCAREAIKRFRKSK-----IKGKIINMSSVHEKIPW 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  163 VGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPL---LTSLPEKVCNFLaSQVPFPsRLGDPAEYAHLVQA 239
Cdd:cd05358 149 PGHVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPInaeAWDDPEQRADLL-SLIPMG-RIGEPEEIAAAAAW 226
                       250       260
                ....*....|....*....|....
gi 4758504  240 II--ENPFLNGEVIRLDGAIRMQP 261
Cdd:cd05358 227 LAsdEASYVTGTTLFVDGGMTLYP 250
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
7-257 5.98e-38

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: 134.79  E-value: 5.98e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAK---KLGNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:cd05347   2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQlieKEGVEATAFTCDVSDEEAIKAAVEAIEEDFG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   84 RVDVAVNCAGIAvasktyNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAAFEGQV 163
Cdd:cd05347  82 KIDILVNNAGII------RRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIK----QGH--GKIINICSLLSELGGP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  164 GQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPL---LTSLPEKVcNFLASQVPFpSRLGDPAEyahLVQAI 240
Cdd:cd05347 150 PVPAYAASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMteaVVADPEFN-DDILKRIPA-GRWGQPED---LVGAA 224
                       250       260
                ....*....|....*....|..
gi 4758504  241 I-----ENPFLNGEVIRLDGAI 257
Cdd:cd05347 225 VflasdASDYVNGQIIFVDGGW 246
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
9-255 7.39e-37

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  Cd Length: 249  Bit Score: 132.19  E-value: 7.39e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCV-FAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:cd05326   3 DGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDIsFVHCDVTVEADVRAAVDTAVARFGRLDI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   88 AVNCAGIAVASKTYNLKkgqtHTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRGVIINTASVAAFEGQVGQAA 167
Cdd:cd05326  83 MFNNAGVLGAPCYSILE----TSLEEFERVLDVNVYGAFLGTKHAARVM------IPAKKGSIVSVASVAGVVGGLGPHA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  168 YSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLT-------SLPEKVCNFLASQVPFPSRLGDPAEyAHLVQAI 240
Cdd:cd05326 153 YTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTagfgvedEAIEEAVRGAANLKGTALRPEDIAA-AVLYLAS 231
                       250
                ....*....|....*
gi 4758504  241 IENPFLNGEVIRLDG 255
Cdd:cd05326 232 DDSRYVSGQNLVVDG 246
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
9-234 9.75e-36

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: 129.33  E-value: 9.75e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQ-----AKKLGNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:cd05355  25 KGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEDDAEetkklIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEFG 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   84 RVDVAVNCAGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqrGVIINTASVAAFEGQV 163
Cdd:cd05355 105 KLDILVNNAAYQHPQESI-----EDITTEQLEKTFRTNIFSMFYLTKAALPHLKKG--------SSIINTTSVTAYKGSP 171
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758504  164 GQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTS--LPEKVCNFlASQVPfPSRLGDPAEYA 234
Cdd:cd05355 172 HLLDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIPSsfPEEKVSEF-GSQVP-MGRAGQPAEVA 242
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
12-255 6.45e-35

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: 126.87  E-value: 6.45e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL-----GNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:cd05330   5 VVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALleiapDAEVLLIKADVSDEAQVEAYVDATVEQFGRID 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   87 VAVNCAGIavaSKTYNLKkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAAFEGQVGQA 166
Cdd:cd05330  85 GFFNNAGI---EGKQNLT--EDFGADEFDKVVSINLRGVFYGLEKVLKVMRE----QGS--GMIVNTASVGGIRGVGNQS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  167 AYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSL--------PEKVCNFLASQVPFpSRLGDPAEYAHLVQ 238
Cdd:cd05330 154 GYAAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSlkqlgpenPEEAGEEFVSVNPM-KRFGEPEEVAAVVA 232
                       250
                ....*....|....*....
gi 4758504  239 AII--ENPFLNGEVIRLDG 255
Cdd:cd05330 233 FLLsdDAGYVNAAVVPIDG 251
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
12-251 1.43e-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: 125.81  E-value: 1.43e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   12 VAVITGGASGLGLATAERLVGQG----ASA-VLLDLPNSGGE--AQAKKLgnncvfaPADVTSEKDVQTALALAKGKFGR 84
Cdd:cd05374   2 VVLITGCSSGIGLALALALAAQGyrviATArNPDKLESLGELlnDNLEVL-------ELDVTDEESIKAAVKEVIERFGR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   85 VDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAAFEGQVG 164
Cdd:cd05374  75 IDVLVNNAGYGLFGPLEET------SIEEVRELFEVNVFGPLRVTRAFLPLMRK----QGS--GRIVNVSSVAGLVPTPF 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  165 QAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTplltslpekvcNFLASQVPFPSRLGDPAEYAHLVQAIIENP 244
Cdd:cd05374 143 LGPYCASKAALEALSESLRLELAPFGIKVTIIEPGPVRT-----------GFADNAAGSALEDPEISPYAPERKEIKENA 211

                ....*..
gi 4758504  245 FLNGEVI 251
Cdd:cd05374 212 AGVGSNP 218
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
7-232 1.48e-34

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: 125.91  E-value: 1.48e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL----GNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:cd05352   5 SLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELakkyGVKTKAYKCDVSSQESVEKTFKQIQKDF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   83 GRVDVAVNCAGIAVAsktynlKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAafeGQ 162
Cdd:cd05352  85 GKIDILIANAGITVH------KPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQ------GKGSLIITASMS---GT 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4758504  163 VG-----QAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFpSRLGDPAE 232
Cdd:cd05352 150 IVnrpqpQAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKKWESYIPL-KRIALPEE 223
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
10-204 4.32e-34

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: 4.32e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL-------GNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:cd08939   1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIeaeanasGQKVSYISADLSDYEEVEQAFAQAVEKG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   83 GRVDVAVNCAGIAVAsktynlKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPdqggqrGVIINTASVAAFEGQ 162
Cdd:cd08939  81 GPPDLVVNCAGISIP------GLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRP------GHIVFVSSQAALVGI 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 4758504  163 VGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTP 204
Cdd:cd08939 149 YGYSAYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTP 190
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
8-255 8.82e-33

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: 121.06  E-value: 8.82e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    8 VKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFGGLDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   88 AVNCAGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnePDQGGqrGVIINTASVAAFEGQVGQAA 167
Cdd:cd08944  81 LVNNAGAMHLTPAI-----IDTDLAVWDQTMAINLRGTFLCCRHAAPRM----IARGG--GSIVNLSSIAGQSGDPGYGA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  168 YSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTS-LPE-----KVCNFLASQVPFPSRLGDPAEYAHLVQAII 241
Cdd:cd08944 150 YGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAkLAGfegalGPGGFHLLIHQLQGRLGRPEDVAAAVVFLL 229
                       250
                ....*....|....*.
gi 4758504  242 --ENPFLNGEVIRLDG 255
Cdd:cd08944 230 sdDASFITGQVLCVDG 245
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
9-255 1.44e-32

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: 120.46  E-value: 1.44e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    9 KGLVAVITGGASGLGLATAERLVGQGASaVLLDLPNSGGEAQA-----KKLGNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:cd05362   2 AGKVALVTGASRGIGRAIAKRLARDGAS-VVVNYASSKAAAEEvvaeiEAAGGKAIAVQADVSDPSQVARLFDAAEKAFG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   84 RVDVAVNCAGIAVasktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqrGVIINTASVAAFEGQV 163
Cdd:cd05362  81 GVDILVNNAGVML------KKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDG--------GRIINISSSLTAAYTP 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  164 GQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPL-LTSLPEKVCNFLASQVPFpSRLGDPAEYAHLVQAII- 241
Cdd:cd05362 147 NYGAYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMfYAGKTEEAVEGYAKMSPL-GRLGEPEDIAPVVAFLAs 225
                       250
                ....*....|....*
gi 4758504  242 -ENPFLNGEVIRLDG 255
Cdd:cd05362 226 pDGRWVNGQVIRANG 240
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
12-261 1.77e-32

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: 120.04  E-value: 1.77e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQA---KKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETAnnvRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   89 VNCAGIAvasktyNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQAAY 168
Cdd:cd05339  81 INNAGVV------SGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLER------NHGHIVTIASVAGLISPAGLADY 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  169 SASKGGIVG----MTLPIARDLAPiGIRVMTIAPGLFGTPLltslpekvcnFLASQVPFPSrLGDPAEYAHLVQAIIENP 244
Cdd:cd05339 149 CASKAAAVGfhesLRLELKAYGKP-GIKTTLVCPYFINTGM----------FQGVKTPRPL-LAPILEPEYVAEKIVRAI 216
                       250
                ....*....|....*..
gi 4758504  245 FLNGEVIRLDGAIRMQP 261
Cdd:cd05339 217 LTNQQMLYLPFYAYFLP 233
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
7-256 6.23e-32

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: 119.48  E-value: 6.23e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:cd08935   2 SLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEItalGGRAIALAADVLDRASLERAREEIVAQFG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   84 RVDVAVNCAG-----IAVASKTYNLKKGQTH---TLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRGVIINTAS 155
Cdd:cd08935  82 TVDILINGAGgnhpdATTDPEHYEPETEQNFfdlDEEGWEFVFDLNLNGSFLPSQVFGKDM------LEQKGGSIINISS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  156 VAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSL-------PEKVCNFLASQVPFpSRLG 228
Cdd:cd08935 156 MNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLlinpdgsYTDRSNKILGRTPM-GRFG 234
                       250       260       270
                ....*....|....*....|....*....|.
gi 4758504  229 DPAEYAHLVQAIIENP---FLNGEVIRLDGA 256
Cdd:cd08935 235 KPEELLGALLFLASEKassFVTGVVIPVDGG 265
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
7-199 1.13e-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  Cd Length: 250  Bit Score: 115.50  E-value: 1.13e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDL-------PNSGGEAQA-----KKLGNNCVFAPADVT-SEKDVQT 73
Cdd:cd05353   2 RFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLggdrkgsGKSSSAADKvvdeiKAAGGKAVANYDSVEdGEKIVKT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   74 ALAlakgKFGRVDVAVNCAGIAVASKTYNLKKgqthtlEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINT 153
Cdd:cd05353  82 AID----AFGRVDILVNNAGILRDRSFAKMSE------EDWDLVMRVHLKGSFKVTRAAWPYMRKQ------KFGRIINT 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 4758504  154 ASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPG 199
Cdd:cd05353 146 SSAAGLYGNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA 191
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-255 1.27e-30

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


Pssm-ID: 180617  Cd Length: 235  Bit Score: 115.06  E-value: 1.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    12 VAVITGGASGLGLATAERLVGQGASAVLLDLpnsggeAQAKKLGNNCVFAPADVTSEkdvqtaLALAKGKFGRVDVAVNC 91
Cdd:PRK06550   7 TVLITGAASGIGLAQARAFLAQGAQVYGVDK------QDKPDLSGNFHFLQLDLSDD------LEPLFDWVPSVDILCNT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    92 AGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQAAYSAS 171
Cdd:PRK06550  75 AGILDDYKPL-----LDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLER------KSGIIINMCSIASFVAGGGGAAYTAS 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   172 KGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTS--LPEKVCNFLASQVPFpSRLGDPAEYAHLV------QAiien 243
Cdd:PRK06550 144 KHALAGFTKQLALDYAKDGIQVFGIAPGAVKTPMTAAdfEPGGLADWVARETPI-KRWAEPEEVAELTlflasgKA---- 218
                        250
                 ....*....|..
gi 4758504   244 PFLNGEVIRLDG 255
Cdd:PRK06550 219 DYMQGTIVPIDG 230
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
10-257 1.44e-30

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: 115.06  E-value: 1.44e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELragGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   87 VAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQA 166
Cdd:cd05344  81 ILVNNAGGPPPGPFAEL------TDEDWLEAFDLKLLSVIRIVRAVLPGMKER------GWGRIVNISSLTVKEPEPNLV 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  167 AYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSL-----------PEKVCNFLASQVPFpSRLGDPAEYAH 235
Cdd:cd05344 149 LSNVARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTERVRRLlearaekegisVEEAEKEVASQIPL-GRVGKPEELAA 227
                       250       260
                ....*....|....*....|....*
gi 4758504  236 LVqAIIENP---FLNGEVIRLDGAI 257
Cdd:cd05344 228 LI-AFLASEkasYITGQAILVDGGL 251
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
12-259 4.15e-30

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: 114.10  E-value: 4.15e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPN----SGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:cd05337   3 VAIVTGASRGIGRAIATELAARGFDIAINDLPDddqaTEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   88 AVNCAGIAVASKTYNLKKgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAA 167
Cdd:cd05337  83 LVNNAGIAVRPRGDLLDL----TEDSFDRLIAINLRGPFFLTQAVARRMVEQPDRFDGPHRSIIFVTSINAYLVSPNRGE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  168 YSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLAS-QVPFPsRLGDPAEYAHLVQAIIEN--P 244
Cdd:cd05337 159 YCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKYDELIAAgLVPIR-RWGQPEDIAKAVRTLASGllP 237
                       250
                ....*....|....*
gi 4758504  245 FLNGEVIRLDGAIRM 259
Cdd:cd05337 238 YSTGQPINIDGGLSM 252
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
12-259 1.21e-29

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: 112.55  E-value: 1.21e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNS-GGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVN 90
Cdd:cd05349   2 VVLVTGASRGLGAAIARSFAREGARVVVNYYRSTeSAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTIVN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   91 CAGIAVASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQAAYSA 170
Cdd:cd05349  82 NALIDFPFDPDQRKTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKER------GSGRVINIGTNLFQNPVVPYHDYTT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  171 SKGGIVGMTLPIARDLAPIGIRVMTIAPGLFG-TPLLTSLPEKVCNFLASQVPFpSRLGDPAEYAHLVQ--AIIENPFLN 247
Cdd:cd05349 156 AKAALLGFTRNMAKELGPYGITVNMVSGGLLKvTDASAATPKEVFDAIAQTTPL-GKVTTPQDIADAVLffASPWARAVT 234
                       250
                ....*....|..
gi 4758504  248 GEVIRLDGAIRM 259
Cdd:cd05349 235 GQNLVVDGGLVM 246
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
10-257 1.76e-29

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: 111.90  E-value: 1.76e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAV 89
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRIDVLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   90 NCAGIAvasktyNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqRGVIINTASVAAFEGQVGQAAYS 169
Cdd:cd09761  81 NNAARG------SKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKN-------KGRIINIASTRAFQSEPDSEAYA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  170 ASKGGIVGMTLPIARDLAPiGIRVMTIAPGLFGTpllTSLPEKVCNFLA----SQVPfPSRLGDPAEYAHLVQAIIENP- 244
Cdd:cd09761 148 ASKGGLVALTHALAMSLGP-DIRVNCISPGWINT---TEQQEFTAAPLTqedhAQHP-AGRVGTPKDIANLVLFLCQQDa 222
                       250
                ....*....|....
gi 4758504  245 -FLNGEVIRLDGAI 257
Cdd:cd09761 223 gFITGETFIVDGGM 236
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
9-256 6.50e-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: 110.75  E-value: 6.50e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    9 KGLVAVITGGASGLGLATAERLVGQGASAVLL--DLPNSggEAQAKKL----GNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:cd05369   2 KGKVAFITGGGTGIGKAIAKAFAELGASVAIAgrKPEVL--EAAAEEIssatGGRAHPIQCDVRDPEAVEAAVDETLKEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   83 GRVDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAgemgqNEPDQGGQRGVIINTASVAAFEGQ 162
Cdd:cd05369  80 GKIDILINNAAGNFLAPAESL------SPNGFKTVIDIDLNGTFNTTKAVG-----KRLIEAKHGGSILNISATYAYTGS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  163 VGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPG-LFGTPLLTSL--PEKVCNFLASQVPFpSRLGDPAEYAHLVqA 239
Cdd:cd05369 149 PFQVHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAPGpIPTTEGMERLapSGKSEKKMIERVPL-GRLGTPEEIANLA-L 226
                       250       260
                ....*....|....*....|
gi 4758504  240 IIENP---FLNGEVIRLDGA 256
Cdd:cd05369 227 FLLSDaasYINGTTLVVDGG 246
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
1-232 3.26e-28

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: 109.16  E-value: 3.26e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    1 MAAACRsVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNN----CVFAPADVTSEKDVQTALA 76
Cdd:cd08933   1 MASGLR-YADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAgpgsCKFVPCDVTKEEDIKTLIS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   77 LAKGKFGRVDVAVNCAGIAVASKTYNlkkgqTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqRGVIINTASV 156
Cdd:cd08933  80 VTVERFGRIDCLVNNAGWHPPHQTTD-----ETSAQEFRDLLNLNLISYFLASKYALPHLRKS-------QGNIINLSSL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  157 AAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLAS-----QVPFPSRLGDPA 231
Cdd:cd08933 148 VGSIGQKQAAPYVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEELAAQTPDTLATikegeLAQLLGRMGTEA 227

                .
gi 4758504  232 E 232
Cdd:cd08933 228 E 228
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
7-259 3.33e-28

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832  Cd Length: 247  Bit Score: 108.55  E-value: 3.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504     7 SVKGLVAVITGGASGLGLATAERLVGQGASAVL-LDLPNSGGEAQAKKLGNN---CVFAPADVTSEKDVQTALALAKGKF 82
Cdd:PRK12935   3 QLNGKVAIVTGGAKGIGKAITVALAQEGAKVVInYNSSKEAAENLVNELGKEghdVYAVQADVSKVEDANRLVEEAVNHF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    83 GRVDVAVNCAGIavaSKTYNLKKGQThtlEDFQRVLDVNLMGTFNVIRLVAGEMGQNEpdqggqRGVIINTASVAAFEGQ 162
Cdd:PRK12935  83 GKVDILVNNAGI---TRDRTFKKLNR---EDWERVIDVNLSSVFNTTSAVLPYITEAE------EGRIISISSIIGQAGG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   163 VGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPfPSRLGDPAEYAH-LVQAII 241
Cdd:PRK12935 151 FGQTNYSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEEVRQKIVAKIP-KKRFGQADEIAKgVVYLCR 229
                        250
                 ....*....|....*...
gi 4758504   242 ENPFLNGEVIRLDGAIRM 259
Cdd:PRK12935 230 DGAYITGQQLNINGGLYM 247
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
9-255 3.50e-28

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: 108.33  E-value: 3.50e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLpnSGGEAQAKKLGNNCVFAPADVTSEKDVQTALAlakgKFGRVDVA 88
Cdd:cd05368   1 DGKVALITAAAQGIGRAIALAFAREGANVIATDI--NEEKLKELERGPGITTRVLDVTDKEQVAALAK----EEGRIDVL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   89 VNCAGIAVASKTYNLKKgqthtlEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAA-FEGQVGQAA 167
Cdd:cd05368  75 FNCAGFVHHGSILDCED------DDWDFAMNLNVRSMYLMIKAVLPKMLA----RKD--GSIINMSSVASsIKGVPNRFV 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  168 YSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSL------PEKVCNFLASQVPFpSRLGDPAEYAHLVQ--A 239
Cdd:cd05368 143 YSTTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLEERiqaqpdPEEALKAFAARQPL-GRLATPEEVAALAVylA 221
                       250
                ....*....|....*.
gi 4758504  240 IIENPFLNGEVIRLDG 255
Cdd:cd05368 222 SDESAYVTGTAVVIDG 237
PRK07069 PRK07069
short chain dehydrogenase; Validated
13-257 3.58e-28

short chain dehydrogenase; Validated


Pssm-ID: 180822  Cd Length: 251  Bit Score: 108.64  E-value: 3.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    13 AVITGGASGLGLATAERLVGQGASAVLLDLPN-SGGEAQAKKLGNNC----VFA-PADVTSEKDVQTALALAKGKFGRVD 86
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINDaAGLDAFAAEINAAHgegvAFAaVQDVTDEAQWQALLAQAADAMGGLS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    87 VAVNCAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPdqggqrGVIINTASVAAFEGQVGQA 166
Cdd:PRK07069  82 VLVNNAGVGSFGAI------EQIELDEWRRVMAINVESIFLGCKHALPYLRASQP------ASIVNISSVAAFKAEPDYT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   167 AYSASKGGIVGMTLPIARDLAP--IGIRVMTIAPGLFGTPLLTSL-----PEKVCNFLASQVPFpSRLGDPAEYAHLV-- 237
Cdd:PRK07069 150 AYNASKAAVASLTKSIALDCARrgLDVRCNSIHPTFIRTGIVDPIfqrlgEEEATRKLARGVPL-GRLGEPDDVAHAVly 228
                        250       260
                 ....*....|....*....|
gi 4758504   238 QAIIENPFLNGEVIRLDGAI 257
Cdd:PRK07069 229 LASDESRFVTGAELVIDGGI 248
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
9-205 3.84e-28

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: 108.69  E-value: 3.84e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLpnsGGEAQAKKL--------GNNCVFAPADVTSEKDVQTALALAKG 80
Cdd:cd08940   1 KGKVALVTGSTSGIGLGIARALAAAGANIVLNGF---GDAAEIEAVraglaakhGVKVLYHGADLSKPAAIEDMVAYAQR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   81 KFGRVDVAVNCAGIA-VASKTynlkkgqTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAF 159
Cdd:cd08940  78 QFGGVDILVNNAGIQhVAPIE-------DFPTEKWDAIIALNLSAVFHTTRLALPHMKKQ------GWGRIINIASVHGL 144
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 4758504  160 EGQVGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPL 205
Cdd:cd08940 145 VASANKSAYVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPL 190
PRK07832 PRK07832
short chain dehydrogenase; Provisional
13-206 5.90e-28

short chain dehydrogenase; Provisional


Pssm-ID: 181139  Cd Length: 272  Bit Score: 108.59  E-value: 5.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    13 AVITGGASGLGLATAERLVGQGASAVLLDLPNSGGE---AQAKKLGNNCVFAPA-DVTsekDVQTALALAK---GKFGRV 85
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAqtvADARALGGTVPEHRAlDIS---DYDAVAAFAAdihAAHGSM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    86 DVAVNCAGIAVASKTYNLkkgqTHtlEDFQRVLDVNLMGTFNVIRLVAGEMgqnepDQGGQRGVIINTASVAAFEGQVGQ 165
Cdd:PRK07832  80 DVVMNIAGISAWGTVDRL----TH--EQWRRMVDVNLMGPIHVIETFVPPM-----VAAGRGGHLVNVSSAAGLVALPWH 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 4758504   166 AAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLL 206
Cdd:PRK07832 149 AAYSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLV 189
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
9-204 2.91e-27

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: 106.07  E-value: 2.91e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQA--KKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:cd08937   3 EGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAeiLAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   87 VAVNCAGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQvgQA 166
Cdd:cd08937  83 VLINNVGGTIWAKPY-----EHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLER------QQGVIVNVSSIATRGIY--RI 149
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 4758504  167 AYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTP 204
Cdd:cd08937 150 PYSAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAP 187
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
8-259 1.31e-26

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  Cd Length: 254  Bit Score: 104.24  E-value: 1.31e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    8 VKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWGSIDI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   88 AVNCAGIavasktYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGqnepdQGGQRGVIINTASVAAFEGQVGQAA 167
Cdd:cd05363  81 LVNNAAL------FDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMI-----AQGRGGKIINMASQAGRRGEALVGV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  168 YSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNF-----------LASQVPFpSRLGDPAEY--A 234
Cdd:cd05363 150 YCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGEHWDGVDAKFARYenrprgekkrlVGEAVPF-GRMGRAEDLtgM 228
                       250       260
                ....*....|....*....|....*
gi 4758504  235 HLVQAIIENPFLNGEVIRLDGAIRM 259
Cdd:cd05363 229 AIFLASTDADYIVAQTYNVDGGNWM 253
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
9-255 2.12e-26

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: 103.57  E-value: 2.12e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL----GNNCVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:cd08930   1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELtnlyKNRVIALELDITSKESIKELIESYLEKFGR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   85 VDVAVNCAGIAV---ASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASV----- 156
Cdd:cd08930  81 IDILINNAYPSPkvwGSRFEEF------PYEQWNEVLNVNLGGAFLCSQAFIKLFKKQ------GKGSIINIASIygvia 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  157 AAFE-----GQVGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGlfgtPLLTSLPEKVCNFLASQVPFpSRLGDPA 231
Cdd:cd08930 149 PDFRiyentQMYSPVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPG----GILNNQPSEFLEKYTKKCPL-KRMLNPE 223
                       250       260
                ....*....|....*....|....*....
gi 4758504  232 EYAHlvqAII-----ENPFLNGEVIRLDG 255
Cdd:cd08930 224 DLRG---AIIfllsdASSYVTGQNLVIDG 249
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
12-211 6.91e-26

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: 102.62  E-value: 6.91e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd08945   5 VALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELreaGVEADGRTCDVRSVPEIEALVAAAVARYGPIDVL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   89 VNCAGiavasktyNLKKGQTHTLED--FQRVLDVNLMGTFNVIR--LVAGEMGQNEpdqggqRGVIINTASVAAFEGQVG 164
Cdd:cd08945  85 VNNAG--------RSGGGATAELADelWLDVVETNLTGVFRVTKevLKAGGMLERG------TGRIINIASTGGKQGVVH 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 4758504  165 QAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPE 211
Cdd:cd08945 151 AAPYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMAASVRE 197
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
13-209 1.11e-25

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: 101.78  E-value: 1.11e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   13 AVITGGASGLGLATAERLVGQGASAVLLDLPnsggEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVNCA 92
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVIALDLP----FVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDALVNCA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   93 GIavasktynLKKGQTHTL--EDFQRVLDVNLMGTFNVIRLVAGEMgqnePDQGGqrGVIINTASVAAFEGQVGQAAYSA 170
Cdd:cd05331  77 GV--------LRPGATDPLstEDWEQTFAVNVTGVFNLLQAVAPHM----KDRRT--GAIVTVASNAAHVPRISMAAYGA 142
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 4758504  171 SKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSL 209
Cdd:cd05331 143 SKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAMQRTL 181
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
12-204 1.66e-25

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: 100.92  E-value: 1.66e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQA---KKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05360   2 VVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELArevRELGGEAIAVVADVADAAQVERAADTAVERFGRIDTW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   89 VNCAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdqgGQRGVIINTASVAAFEGQVGQAAY 168
Cdd:cd05360  82 VNNAGVAVFGRF------EDVTPEEFRRVFDVNYLGHVYGTLAALPHLRR------RGGGALINVGSLLGYRSAPLQAAY 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 4758504  169 SASKGGIVGMT----LPIARDLAPigIRVMTIAPGLFGTP 204
Cdd:cd05360 150 SASKHAVRGFTeslrAELAHDGAP--ISVTLVQPTAMNTP 187
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
12-208 4.33e-25

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: 99.95  E-value: 4.33e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQA---KKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05365   1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAaaiQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   89 VNCAGIAVASKtynlkKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQAAY 168
Cdd:cd05365  81 VNNAGGGGPKP-----FDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKA------GGGAILNISSMSSENKNVRIAAY 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 4758504  169 SASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTS 208
Cdd:cd05365 150 GSSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDALAS 189
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
10-198 6.52e-25

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: 99.39  E-value: 6.52e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGE--AQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:cd08943   1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEkvAEAAQGGPRALGVQCDVTSEAQVQSAFEQAVLEFGGLDI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   88 AVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqgGQRGVIINTASVAAFEGQVGQAA 167
Cdd:cd08943  81 VVSNAGIATSSPIAET------SLEDWNRSMDINLTGHFLVSREAFRIMKSQ-----GIGGNIVFNASKNAVAPGPNAAA 149
                       170       180       190
                ....*....|....*....|....*....|.
gi 4758504  168 YSASKGGIVGMTLPIARDLAPIGIRVMTIAP 198
Cdd:cd08943 150 YSAAKAAEAHLARCLALEGGEDGIRVNTVNP 180
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
9-255 7.34e-25

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: 99.41  E-value: 7.34e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL------GNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:cd05364   2 SGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSClqagvsEKKILLVVADLTEEEGQDRIISTTLAKF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   83 GRVDVAVNCAGIAVASKtynlkkGQTHTLEDFQRVLDVNLMGTFNVIRLVAgemgqnePDQGGQRGVIINTASVAAFEGQ 162
Cdd:cd05364  82 GRLDILVNNAGILAKGG------GEDQDIEEYDKVMNLNLRAVIYLTKLAV-------PHLIKTKGEIVNVSSVAGGRSF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  163 VGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTS--LPE----KVCNFLASQVPFpSRLGDPAEYAHL 236
Cdd:cd05364 149 PGVLYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRmgMPEeqyiKFLSRAKETHPL-GRPGTVDEVAEA 227
                       250       260
                ....*....|....*....|.
gi 4758504  237 VQAIIENP--FLNGEVIRLDG 255
Cdd:cd05364 228 IAFLASDAssFITGQLLPVDG 248
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
9-209 8.00e-25

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  Cd Length: 257  Bit Score: 99.46  E-value: 8.00e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAK----KLGNNCVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:cd05322   1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADeinaEYGEKAYGFGADATNEQSVIALSKGVDEIFKR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   85 VDVAVNCAGIAVASKTYNLKkgqthtLEDFQRVLDVNLMGTFnvirLVAGEMGQNEPDQGGQRGVI-INTASvaafeGQV 163
Cdd:cd05322  81 VDLLVYSAGIAKSAKITDFE------LGDFDRSLQVNLVGYF----LCAREFSKLMIRDGIQGRIIqINSKS-----GKV 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 4758504  164 G---QAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPG-LFGTPLLTSL 209
Cdd:cd05322 146 GskhNSGYSAAKFGGVGLTQSLALDLAEHGITVNSLMLGnLLKSPMFQSL 195
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
7-255 8.05e-25

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: 99.45  E-value: 8.05e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKF- 82
Cdd:cd05329   3 NLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWrekGFKVEGSVCDVSSRSERQELMDTVASHFg 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   83 GRVDVAVNCAGIAVAsktynlKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQ 162
Cdd:cd05329  83 GKLNILVNNAGTNIR------KEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKAS------GNGNIVFISSVAGVIAV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  163 VGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSL---PEKVCNFLaSQVPFpSRLGDPAEYAHLVqA 239
Cdd:cd05329 151 PSGAPYGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPViqqKENLDKVI-ERTPL-KRFGEPEEVAALV-A 227
                       250
                ....*....|....*....
gi 4758504  240 IIENP---FLNGEVIRLDG 255
Cdd:cd05329 228 FLCMPaasYITGQIIAVDG 246
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
9-257 9.64e-25

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: 99.35  E-value: 9.64e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05348   3 KGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGKLDCF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   89 VNCAGIAvaskTYNLKKGQT--HTLED-FQRVLDVNLMGTFNVIRLVAGEMGQNEpdqggqrGVIINTASVAAFEGQVGQ 165
Cdd:cd05348  83 IGNAGIW----DYSTSLVDIpeEKLDEaFDELFHINVKGYILGAKAALPALYATE-------GSVIFTVSNAGFYPGGGG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  166 AAYSASKGGIVGMTLPIARDLAPIgIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFP---------SRLGDPAEY--A 234
Cdd:cd05348 152 PLYTASKHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTDLRGPASLGQGETSISTPPLDdmlksilplGFAPEPEDYtgA 230
                       250       260
                ....*....|....*....|....
gi 4758504  235 HLVQAIIENP-FLNGEVIRLDGAI 257
Cdd:cd05348 231 YVFLASRGDNrPATGTVINYDGGM 254
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
13-203 7.06e-24

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: 96.04  E-value: 7.06e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   13 AVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVNCA 92
Cdd:cd08929   3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVNNA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   93 GIAVasktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAgemgqnEPDQGGQRGVIINTASVAAFEGQVGQAAYSASK 172
Cdd:cd08929  83 GVGV------MKPVEELTPEEWRLVLDTNLTGAFYCIHKAA------PALLRRGGGTIVNVGSLAGKNAFKGGAAYNASK 150
                       170       180       190
                ....*....|....*....|....*....|.
gi 4758504  173 GGIVGMTLPIARDLAPIGIRVMTIAPGLFGT 203
Cdd:cd08929 151 FGLLGLSEAAMLDLREANIRVVNVMPGSVDT 181
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
13-203 1.65e-23

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: 95.42  E-value: 1.65e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   13 AVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNN----CVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05346   3 VLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKfpvkVLPLQLDVSDRESIEAALENLPEEFRDIDIL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   89 VNCAGIAVAsktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEpdqggqRGVIINTASVAAFEGQVGQAAY 168
Cdd:cd05346  83 VNNAGLALG-----LDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARN------QGHIINLGSIAGRYPYAGGNVY 151
                       170       180       190
                ....*....|....*....|....*....|....*
gi 4758504  169 SASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGT 203
Cdd:cd05346 152 CATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVET 186
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
12-251 1.18e-22

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: 92.81  E-value: 1.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFaPADVTSEKDVQTALALAKGKFGRVDVAVNC 91
Cdd:cd08932   2 VALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSASGGDVEAV-PYDARDPEDARALVDALRDRFGRIDVLVHN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   92 AGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRGVIINTASVAAFEGQVGQAAYSAS 171
Cdd:cd08932  81 AGIGRPTTLREG------SDAELEAHFSINVIAPAELTRALLPAL------REAGSGRVVFLNSLSGKRVLAGNAGYSAS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  172 KGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEkvcnflaSQVPFPSRLGDPAEYAHLVQAIIENPFLNGEVI 251
Cdd:cd08932 149 KFALRALAHALRQEGWDHGVRVSAVCPGFVDTPMAQGLTL-------VGAFPPEEMIQPKDIANLVRMVIELPENITSVA 221
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
12-256 1.23e-22

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: 92.73  E-value: 1.23e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   12 VAVITGGASGLGLATAERLVGQGAsAVLLDLPNSGGEAQA-----KKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:cd05357   2 VALVTGAAKRIGRAIAEALAAEGY-RVVVHYNRSEAEAQRlkdelNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   87 VAVNCAGIAVASKTynlkkGQThTLEDFQRVLDVNLMGTFNVIRLVAGEMGqnepdqGGQRGVIINTASVAAFEGQVGQA 166
Cdd:cd05357  81 VLVNNASAFYPTPL-----GQG-SEDAWAELFGINLKAPYLLIQAFARRLA------GSRNGSIINIIDAMTDRPLTGYF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504  167 AYSASKGGIVGMTLPIARDLAPiGIRVMTIAPGLfgTPLLTSLPEKVCNFLASQVPFpSRLGDPAEYAHLVQAIIENPFL 246
Cdd:cd05357 149 AYCMSKAALEGLTRSAALELAP-NIRVNGIAPGL--ILLPEDMDAEYRENALRKVPL-KRRPSAEEIADAVIFLLDSNYI 224
                       250
                ....*....|
gi 4758504  247 NGEVIRLDGA 256
Cdd:cd05357 225 TGQIIKVDGG 234
PRK06947 PRK06947
glucose-1-dehydrogenase; Provisional
12-241 1.77e-22

glucose-1-dehydrogenase; Provisional


Pssm-ID: 180771  Cd Length: 248  Bit Score: 92.56  E-value: 1.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    12 VAVITGGASGLGLATAeRLVGQGASAVLLdlpNSGGEAQAKKL---------GNNCVFApADVTSEKDVQTALALAKGKF 82
Cdd:PRK06947   4 VVLITGASRGIGRATA-VLAAARGWSVGI---NYARDAAAAEEtadavraagGRACVVA-GDVANEADVIAMFDAVQSAF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    83 GRVDVAVNCAGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepDQGGQRGVIINTASVAAFEGQ 162
Cdd:PRK06947  79 GRLDALVNNAGIVAPSMPL-----ADMDAARLRRMFDTNVLGAYLCAREAARRLST---DRGGRGGAIVNVSSIASRLGS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   163 VGQAA-YSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTS--LPEKVCNfLASQVPfpsrLGDPAEYAHLVQA 239
Cdd:PRK06947 151 PNEYVdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHASggQPGRAAR-LGAQTP----LGRAGEADEVAET 225

                 ..
gi 4758504   240 II 241
Cdd:PRK06947 226 IV 227
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
15-208 5.17e-22

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  Cd Length: 227  Bit Score: 90.97  E-value: 5.17e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   15 ITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLG-NNCVFAPADVTSEKDVQTALA-LAKGKFGRVDVAVNCA 92
Cdd:cd08931   5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGaENVVAGALDVTDRAAWAAALAdFAAATGGRLDALFNNA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   93 GIavasktynLKKGQTHT--LEDFQRVLDVNLMGTFNVIRlVAGEMGQNEPdqGGQrgvIINTASVAAFEGQVGQAAYSA 170
Cdd:cd08931  85 GV--------GRGGPFEDvpLAAHDRMVDINVKGVLNGAY-AALPYLKATP--GAR---VINTASSSAIYGQPDLAVYSA 150
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 4758504  171 SKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTS 208
Cdd:cd08931 151 TKFAVRGLTEALDVEWARHGIRVADVWPWFVDTPILTK 188
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
10-205 5.63e-22

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: 91.06  E-value: 5.63e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:cd08934   3 GKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELeaeGGKALVLELDVTDEQQVDAAVERTVEALGRLD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   87 VAVNCAGIAVasktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQA 166
Cdd:cd08934  83 ILVNNAGIML------LGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLR------NKGTIVNISSVAGRVAVRNSA 150
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 4758504  167 AYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPL 205
Cdd:cd08934 151 VYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTEL 189
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
1-257 1.04e-21

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040  Cd Length: 255  Bit Score: 90.60  E-value: 1.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504     1 MAAACRSVKGLVAVITGGASGLGLATAERLVGQGASAVLldlpN-------SGGEAQAKKLGNNCVFAPADVTSEKDVQT 73
Cdd:PRK07523   1 MSLNLFDLTGRRALVTGSSQGIGYALAEGLAQAGAEVIL----NgrdpaklAAAAESLKGQGLSAHALAFDVTDHDAVRA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504    74 ALALAKGKFGRVDVAVNCAGIAVASKtynlkkgqthtLEDF-----QRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRG 148
Cdd:PRK07523  77 AIDAFEAEIGPIDILVNNAGMQFRTP-----------LEDFpadafERLLRTNISSVFYVGQAVARHM------IARGAG 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758504   149 VIINTASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSL--PEKVCNFLASQVPfPSR 226
Cdd:PRK07523 140 KIINIASVQSALARPGIAPYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAALvaDPEFSAWLEKRTP-AGR 218
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 4758504   227 LGDPAEyahLVQAII-----ENPFLNGEVIRLDGAI 257
Cdd:PRK07523 219 WGKVEE---LVGACVflasdASSFVNGHVLYVDGGI 251
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
12-253 5.99e-21

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 fat