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Conserved domains on  [gi|928185501|ref|XP_013967336|]
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sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating [Canis lupus familiaris]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
28-354 1.91e-173

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


The actual alignment was detected with superfamily member cd09813:

Pssm-ID: 451247 [Multi-domain]  Cd Length: 335  Bit Score: 485.33  E-value: 1.91e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  28 CTVIGGSGFLGQHMVEQLLARG-YTVNVFDMRQGFDN-----PRVQFFLGDLCSQQDLYPAL--KGVSTVFHCASPPPSS 99
Cdd:cd09813    2 CLVVGGSGFLGRHLVEQLLRRGnPTVHVFDIRPTFELdpsssGRVQFHTGDLTDPQDLEKAFneKGPNVVFHTASPDHGS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 100 NNkELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKNGTEDLPYAMKPIDYYTETKILQERAVLDANDPKR 179
Cdd:cd09813   82 ND-DLYYKVNVQGTRNVIEACRKCGVKKLVYTSSASVVFNGQDIINGDESLPYPDKHQDAYNETKALAEKLVLKANDPES 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 180 NFLTMAIRPHGIFGPRDPQLVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHGHILAAEHLSQD---TAVSGKAFHIT 256
Cdd:cd09813  161 GLLTCALRPAGIFGPGDRQLVPGLLKAAKNGKTKFQIGDGNNLFDFTYVENVAHAHILAADALLSSshaETVAGEAFFIT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 257 NDEPIPFWTFLSRILTGLNYEA-PKYHIPYWVAYYLALLVSLLVMLLSPViqlqPTFTPMRVALAGTFHYYSCERARKVM 335
Cdd:cd09813  241 NDEPIYFWDFARAIWEGLGYERpPSIKLPRPVALYLASLLEWTCKVLGKE----PTFTPFRVALLCSTRYFNIEKAKKRL 316
                        330
                 ....*....|....*....
gi 928185501 336 GYRPLVTMDDAIERTVQSF 354
Cdd:cd09813  317 GYTPVVTLEEGIERTLQWF 335
 
Name Accession Description Interval E-value
3b-HSD-NSDHL-like_SDR_e cd09813
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This ...
28-354 1.91e-173

human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This subgroup includes human NSDHL and related proteins. These proteins have the characteristic active site tetrad of extended SDRs, and also have a close match to their NAD(P)-binding motif. Human NSDHL is a 3beta-hydroxysteroid dehydrogenase (3 beta-HSD) which functions in the cholesterol biosynthetic pathway. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. Mutations in the gene encoding NSDHL cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. This subgroup also includes an unusual bifunctional [3beta-hydroxysteroid dehydrogenase (3b-HSD)/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187673 [Multi-domain]  Cd Length: 335  Bit Score: 485.33  E-value: 1.91e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  28 CTVIGGSGFLGQHMVEQLLARG-YTVNVFDMRQGFDN-----PRVQFFLGDLCSQQDLYPAL--KGVSTVFHCASPPPSS 99
Cdd:cd09813    2 CLVVGGSGFLGRHLVEQLLRRGnPTVHVFDIRPTFELdpsssGRVQFHTGDLTDPQDLEKAFneKGPNVVFHTASPDHGS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 100 NNkELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKNGTEDLPYAMKPIDYYTETKILQERAVLDANDPKR 179
Cdd:cd09813   82 ND-DLYYKVNVQGTRNVIEACRKCGVKKLVYTSSASVVFNGQDIINGDESLPYPDKHQDAYNETKALAEKLVLKANDPES 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 180 NFLTMAIRPHGIFGPRDPQLVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHGHILAAEHLSQD---TAVSGKAFHIT 256
Cdd:cd09813  161 GLLTCALRPAGIFGPGDRQLVPGLLKAAKNGKTKFQIGDGNNLFDFTYVENVAHAHILAADALLSSshaETVAGEAFFIT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 257 NDEPIPFWTFLSRILTGLNYEA-PKYHIPYWVAYYLALLVSLLVMLLSPViqlqPTFTPMRVALAGTFHYYSCERARKVM 335
Cdd:cd09813  241 NDEPIYFWDFARAIWEGLGYERpPSIKLPRPVALYLASLLEWTCKVLGKE----PTFTPFRVALLCSTRYFNIEKAKKRL 316
                        330
                 ....*....|....*....
gi 928185501 336 GYRPLVTMDDAIERTVQSF 354
Cdd:cd09813  317 GYTPVVTLEEGIERTLQWF 335
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
30-284 1.37e-71

3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerisation of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 224.55  E-value: 1.37e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501   30 VIGGSGFLGQHMVEQLLARG--YTVNVFDMRQG-------FDNPRVQFFLGDLCSQQDLYPALKGVSTVFH--CASPPPS 98
Cdd:pfam01073   2 VTGGGGFLGRHIIKLLVREGelKEVRVFDLRESpelledfSKSNVIKYIQGDVTDKDDLDNALEGVDVVIHtaSAVDVFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501   99 SNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIF---EGVNIKNGTEDLPYAMKPIDYYTETKILQERAVLDAN 175
Cdd:pfam01073  82 KYTFDEIMKVNVKGTQNVLEACVKAGVRVLVYTSSAEVVGpnsYGQPILNGDEETPYESTHQDAYPRSKAIAEKLVLKAN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  176 D-PKRN---FLTMAIRPHGIFGPRDPQLVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHGHILAAEHL---SQDTAV 248
Cdd:pfam01073 162 GrPLKNggrLYTCALRPAGIYGEGDRLLVPFIVNLAKLGLAKFKTGDDNNLSDRVYVGNVAWAHILAARALqdpKKMSSI 241
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 928185501  249 SGKAFHITNDEPI-PFWTFLSRILTGLNYEAPKYHIP 284
Cdd:pfam01073 242 AGNAYFIYDDTPVqSYDDFNRTLLKSLGYDLPSISLP 278
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
30-354 5.24e-52

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 223528 [Multi-domain]  Cd Length: 314  Bit Score: 175.13  E-value: 5.24e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFD---MRQGFDNPRVQFFLGDLCSQQDLYPALKGVS-TVFHCASPPPS----SNN 101
Cdd:COG0451    5 VTGGAGFIGSHLVERLLAAGHDVRGLDrlrDGLDPLLSGVEFVVLDLTDRDLVDELAKGVPdAVIHLAAQSSVpdsnASD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 102 KELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKNGTEDLPYAmKPIDYYTETKILQERAVLDANDpKRNF 181
Cdd:COG0451   85 PAEFLDVNVDGTLNLLEAARAAGVKRFVFASSVSVVYGDPPPLPIDEDLGPP-RPLNPYGVSKLAAEQLLRAYAR-LYGL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 182 LTMAIRPHGIFGPRDP-----QLVPILIEAARKGKMKFMI-GNGENLVDFTFVENVVHGHILAAEHLsqdtavSGKAFHI 255
Cdd:COG0451  163 PVVILRPFNVYGPGDKpdlssGVVSAFIRQLLKGEPIIVIgGDGSQTRDFVYVDDVADALLLALENP------DGGVFNI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 256 TNDE-PIPFWTFLSRILTGLNYEAPKYHIpywvayylallvsllvmllspviqlqptFTPMRVALAGTFHYYSCERARKV 334
Cdd:COG0451  237 GSGTaEITVRELAEAVAEAVGSKAPLIVY----------------------------IPLGRRGDLREGKLLDISKARAA 288
                        330       340
                 ....*....|....*....|
gi 928185501 335 MGYRPLVTMDDAIERTVQSF 354
Cdd:COG0451  289 LGWEPKVSLEEGLADTLEWL 308
PLN02240 PLN02240
UDP-glucose 4-epimerase
30-201 7.97e-13

UDP-glucose 4-epimerase


Pssm-ID: 177883 [Multi-domain]  Cd Length: 352  Bit Score: 68.45  E-value: 7.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFDmrqGFDNP------RVQ-----------FFLGDLCSQQDLYP--ALKGVSTVF 90
Cdd:PLN02240  10 VTGGAGYIGSHTVLQLLLAGYKVVVID---NLDNSseealrRVKelagdlgdnlvFHKVDLRDKEALEKvfASTRFDAVI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  91 HCA---SPPPSSNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKnGTEDLP-YAMKPidyYTETKIL 166
Cdd:PLN02240  87 HFAglkAVGESVAKPLLYYDNNLVGTINLLEVMAKHGCKKLVFSSSATVYGQPEEVP-CTEEFPlSATNP---YGRTKLF 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 928185501 167 QERAVLD--ANDPK------RNFLTMAIRPHGIFGpRDPQLVP 201
Cdd:PLN02240 163 IEEICRDihASDPEwkiillRYFNPVGAHPSGRIG-EDPKGIP 204
 
Name Accession Description Interval E-value
3b-HSD-NSDHL-like_SDR_e cd09813
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This ...
28-354 1.91e-173

human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This subgroup includes human NSDHL and related proteins. These proteins have the characteristic active site tetrad of extended SDRs, and also have a close match to their NAD(P)-binding motif. Human NSDHL is a 3beta-hydroxysteroid dehydrogenase (3 beta-HSD) which functions in the cholesterol biosynthetic pathway. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. Mutations in the gene encoding NSDHL cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. This subgroup also includes an unusual bifunctional [3beta-hydroxysteroid dehydrogenase (3b-HSD)/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187673 [Multi-domain]  Cd Length: 335  Bit Score: 485.33  E-value: 1.91e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  28 CTVIGGSGFLGQHMVEQLLARG-YTVNVFDMRQGFDN-----PRVQFFLGDLCSQQDLYPAL--KGVSTVFHCASPPPSS 99
Cdd:cd09813    2 CLVVGGSGFLGRHLVEQLLRRGnPTVHVFDIRPTFELdpsssGRVQFHTGDLTDPQDLEKAFneKGPNVVFHTASPDHGS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 100 NNkELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKNGTEDLPYAMKPIDYYTETKILQERAVLDANDPKR 179
Cdd:cd09813   82 ND-DLYYKVNVQGTRNVIEACRKCGVKKLVYTSSASVVFNGQDIINGDESLPYPDKHQDAYNETKALAEKLVLKANDPES 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 180 NFLTMAIRPHGIFGPRDPQLVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHGHILAAEHLSQD---TAVSGKAFHIT 256
Cdd:cd09813  161 GLLTCALRPAGIFGPGDRQLVPGLLKAAKNGKTKFQIGDGNNLFDFTYVENVAHAHILAADALLSSshaETVAGEAFFIT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 257 NDEPIPFWTFLSRILTGLNYEA-PKYHIPYWVAYYLALLVSLLVMLLSPViqlqPTFTPMRVALAGTFHYYSCERARKVM 335
Cdd:cd09813  241 NDEPIYFWDFARAIWEGLGYERpPSIKLPRPVALYLASLLEWTCKVLGKE----PTFTPFRVALLCSTRYFNIEKAKKRL 316
                        330
                 ....*....|....*....
gi 928185501 336 GYRPLVTMDDAIERTVQSF 354
Cdd:cd09813  317 GYTPVVTLEEGIERTLQWF 335
3b-HSD-like_SDR_e cd05241
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ...
28-354 2.07e-101

3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187552 [Multi-domain]  Cd Length: 331  Bit Score: 302.43  E-value: 2.07e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  28 CTVIGGSGFLGQHMVEQLLARGYT-VNVFDMR------QGFDNPRVQFFLGDLCSQQDLYPALKGVSTVFHCASPPPSSN 100
Cdd:cd05241    2 VLVTGGSGFFGERLVKQLLERGGTyVRSFDIAppgealSAWQHPNIEFLKGDITDRNDVEQALSGADCVFHTAAIVPLAG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 101 NKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKNGTEDLPYAMKPIDYYTETKILQERAVLDANDPKrN 180
Cdd:cd05241   82 PRDLYWEVNVGGTQNVLDACQRCGVQKFVYTSSSSVIFGGQNIHNGDETLPYPPLDSDMYAETKAIAEIIVLEANGRD-D 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 181 FLTMAIRPHGIFGPRDPQLVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHGHILAAEHLSQDTAVSGKAFHITNDEP 260
Cdd:cd05241  161 LLTCALRPAGIFGPGDQGLVPILFEWAEKGLVKFVFGRGNNLVDFTYVHNLAHAHILAAAALVKGKTISGQTYFITDAEP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 261 IPFWTFLSRILTGLNY-EAPKYHIPYWVAYYLALLVSLLVMLLSPViqlqPTFTPMRVALAGTFHYYSCERARKVMGYRP 339
Cdd:cd05241  241 HNMFELLRPVWKALGFgSRPKIRLSGPLAYCAALLSELVSFMLGPY----FVFSPFYVRALVTPMYFSIAKAQKDLGYAP 316
                        330
                 ....*....|....*
gi 928185501 340 LVTMDDAIERTVQSF 354
Cdd:cd05241  317 RYSNEEGLIETLNWY 331
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
30-284 1.37e-71

3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerisation of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 224.55  E-value: 1.37e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501   30 VIGGSGFLGQHMVEQLLARG--YTVNVFDMRQG-------FDNPRVQFFLGDLCSQQDLYPALKGVSTVFH--CASPPPS 98
Cdd:pfam01073   2 VTGGGGFLGRHIIKLLVREGelKEVRVFDLRESpelledfSKSNVIKYIQGDVTDKDDLDNALEGVDVVIHtaSAVDVFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501   99 SNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIF---EGVNIKNGTEDLPYAMKPIDYYTETKILQERAVLDAN 175
Cdd:pfam01073  82 KYTFDEIMKVNVKGTQNVLEACVKAGVRVLVYTSSAEVVGpnsYGQPILNGDEETPYESTHQDAYPRSKAIAEKLVLKAN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  176 D-PKRN---FLTMAIRPHGIFGPRDPQLVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHGHILAAEHL---SQDTAV 248
Cdd:pfam01073 162 GrPLKNggrLYTCALRPAGIYGEGDRLLVPFIVNLAKLGLAKFKTGDDNNLSDRVYVGNVAWAHILAARALqdpKKMSSI 241
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 928185501  249 SGKAFHITNDEPI-PFWTFLSRILTGLNYEAPKYHIP 284
Cdd:pfam01073 242 AGNAYFIYDDTPVqSYDDFNRTLLKSLGYDLPSISLP 278
3b-HSD_like_1_SDR_e cd09812
3beta-hydroxysteroid dehydrogenase (3b-HSD)-like, subgroup1, extended (e) SDRs; An ...
30-348 2.16e-57

3beta-hydroxysteroid dehydrogenase (3b-HSD)-like, subgroup1, extended (e) SDRs; An uncharacterized subgroup of the 3b-HSD-like extended-SDR family. Proteins in this subgroup have the characteristic active site tetrad and NAD(P)-binding motif of extended-SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187672 [Multi-domain]  Cd Length: 339  Bit Score: 189.64  E-value: 2.16e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFDMRQGFDN--PRVQFFLGDLCSQQDLYPALKGVSTVFHCASPPPSSN---NKEL 104
Cdd:cd09812    4 ITGGGGYFGFRLGCALAKSGVHVILFDIRRPQQElpEGIKFIQADVRDLSQLEKAVAGVDCVFHIASYGMSGReqlNREL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 105 FYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKNGTEDLPYAmkP----IDYYTETKILQERAVLDAN----D 176
Cdd:cd09812   84 IEEINVRGTENIIQVCVRRRVPRLIYTSTFNVIFGGQPIRNGDESLPYL--PldlhVDHYSRTKSIAEQLVLKANnmplP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 177 PKRNFL-TMAIRPHGIFGPRDPQLVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHGHILAAEHLSQDTA--VSGKAF 253
Cdd:cd09812  162 NNGGVLrTCALRPAGIYGPGEQRHLPRIVSYIEKGLFMFVYGDPKSLVEFVHVDNLVQAHILAAEALTTAKGyiASGQAY 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 254 HITNDEPIPFWTFLSRILTGLNYEAPKYHIPYWVAYYLALLVSLLVMLLSPVIQLQPTFTPMRVALAGTFHYYSCERARK 333
Cdd:cd09812  242 FISDGRPVNNFEFFRPLVEGLGYSFPSLRLPLSLVYFFAFLTEMVHFALGPICNFQPLLTRTEVYKTGVTHYFSIEKARA 321
                        330
                 ....*....|....*.
gi 928185501 334 VMGYRP-LVTMDDAIE 348
Cdd:cd09812  322 ELGYEPqPFDLQDAVE 337
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
30-354 1.04e-53

uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 179.40  E-value: 1.04e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVF--DMRQ--GFDNPRVQFFLGDLCSQQDLYPALKGVSTVFHCAS-PPPSSNNKEL 104
Cdd:cd05228    3 VTGATGFLGSNLVRALLAQGYRVRALvrSGSDavLLDGLPVEVVEGDLTDAASLAAAMKGCDRVFHLAAfTSLWAKDRKE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 105 FYRVNYIGTKNVIETCKEAGVQKLILTSSASVIfegvNIKNGT---EDLPYAMKPI--DYYtETKILQERAVLDANDPKR 179
Cdd:cd05228   83 LYRTNVEGTRNVLDAALEAGVRRVVHTSSIAAL----GGPPDGridETTPWNERPFpnDYY-RSKLLAELEVLEAAAEGL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 180 nFLTMaIRPHGIFGPRD--PQLVPILIEAARKGKMKFMIGNGENLVDftfVENVVHGHILAAEHlsqdtavsGKA--FHI 255
Cdd:cd05228  158 -DVVI-VNPSAVFGPGDegPTSTGLDVLDYLNGKLPAYPPGGTSFVD---VRDVAEGHIAAMEK--------GRRgeRYI 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 256 TNDEPIPFWTFLSRI--LTGLNyeAPKYHIPYWVAYylalLVSLLVMLLSPVIQLQPTFTPMRVALAGTFHYYSCERARK 333
Cdd:cd05228  225 LGGENLSFKQLFETLaeITGVK--PPRRTIPPWLLK----AVAALSELKARLTGKPPLLTPRTARVLRRNYLYSSDKARR 298
                        330       340
                 ....*....|....*....|.
gi 928185501 334 VMGYRPlVTMDDAIERTVQSF 354
Cdd:cd05228  299 ELGYSP-RPLEEALRDTLAWL 318
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
30-354 5.24e-52

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 223528 [Multi-domain]  Cd Length: 314  Bit Score: 175.13  E-value: 5.24e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFD---MRQGFDNPRVQFFLGDLCSQQDLYPALKGVS-TVFHCASPPPS----SNN 101
Cdd:COG0451    5 VTGGAGFIGSHLVERLLAAGHDVRGLDrlrDGLDPLLSGVEFVVLDLTDRDLVDELAKGVPdAVIHLAAQSSVpdsnASD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 102 KELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKNGTEDLPYAmKPIDYYTETKILQERAVLDANDpKRNF 181
Cdd:COG0451   85 PAEFLDVNVDGTLNLLEAARAAGVKRFVFASSVSVVYGDPPPLPIDEDLGPP-RPLNPYGVSKLAAEQLLRAYAR-LYGL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 182 LTMAIRPHGIFGPRDP-----QLVPILIEAARKGKMKFMI-GNGENLVDFTFVENVVHGHILAAEHLsqdtavSGKAFHI 255
Cdd:COG0451  163 PVVILRPFNVYGPGDKpdlssGVVSAFIRQLLKGEPIIVIgGDGSQTRDFVYVDDVADALLLALENP------DGGVFNI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 256 TNDE-PIPFWTFLSRILTGLNYEAPKYHIpywvayylallvsllvmllspviqlqptFTPMRVALAGTFHYYSCERARKV 334
Cdd:COG0451  237 GSGTaEITVRELAEAVAEAVGSKAPLIVY----------------------------IPLGRRGDLREGKLLDISKARAA 288
                        330       340
                 ....*....|....*....|
gi 928185501 335 MGYRPLVTMDDAIERTVQSF 354
Cdd:COG0451  289 LGWEPKVSLEEGLADTLEWL 308
3b-HSD_HSDB1_like_SDR_e cd09811
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ...
28-352 1.19e-50

human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs; This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187671 [Multi-domain]  Cd Length: 354  Bit Score: 172.69  E-value: 1.19e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  28 CTVIGGSGFLGQHMVEQLLARGYT---VNVFDMRQG---------FDNP-RVQFFLGDLCSQQDLYPALKGVSTVFHCAS 94
Cdd:cd09811    2 CLVTGGGGFLGQHIIRLLLERKEElkeIRVLDKAFGpeliehfekSQGKtYVTDIEGDIKDLSFLFRACQGVSVVIHTAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  95 ------PPpssnNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVI---FEGVNIKNGTEDLPYAMKPIDYYTETKI 165
Cdd:cd09811   82 ivdvfgPP----NYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAgpnFKGRPIFNGVEDTPYEDTSTPPYASSKL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 166 LQERAVLDAND-PKRN---FLTMAIRPHGIFGPRDPQLVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHGHILAAEH 241
Cdd:cd09811  158 LAENIVLNANGaPLKQggyLVTCALRPMYIYGEGSHFLTEIFDFLLTNNGWLFPRIKGSGVNPLVYVGNVAWAHILAAKA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 242 LSQ-DTAVSGKAFHITNDEPIPFWTFLSRILT---GLNYEAPKYHIPYWVAYYLALLVSLLVMLLSPVIQLQPTFTPMRV 317
Cdd:cd09811  238 LQVpDKAIRGQFYFISDDTPHNSYSDFNYELLkelGLRLKTSWWYVPLFLLYFLAFLLEIVSFLLRPYVKYRPRYNRHAV 317
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 928185501 318 ALAGTFHYYSCERARKVMGYRPLVTMDDAIERTVQ 352
Cdd:cd09811  318 ALTNSMFTFSYLKAQRHFGYMPLFSWEESKERTAK 352
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
27-354 6.29e-38

UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187566 [Multi-domain]  Cd Length: 304  Bit Score: 137.74  E-value: 6.29e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  27 KCTVIGGSGFLGQHMVEQLLARGYTVNVFD-MRQGFD------NPRVQFFLGDLCSQQDLYPALKGVSTVFHCA---SPP 96
Cdd:cd05256    1 RVLVTGGAGFIGSHLVERLLERGHEVIVLDnLSTGKKenlpevKPNVKFIEGDIRDDELVEFAFEGVDYVFHQAaqaSVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  97 PSSNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKNGTEDLPYAMKPidyYTETKILQER-AVLDAN 175
Cdd:cd05256   81 RSIEDPIKDHEVNVLGTLNLLEAARKAGVKRFVYASSSSVYGDPPYLPKDEDHPPNPLSP---YAVSKYAGELyCQVFAR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 176 DPKrnFLTMAIRPHGIFGPR-DPQ-----LVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHGHILAAEhlsqdTAVS 249
Cdd:cd05256  158 LYG--LPTVSLRYFNVYGPRqDPNggyaaVIPIFIERALKGEPPTIYGDGEQTRDFTYVEDVVEANLLAAT-----AGAG 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 250 GKAFHITNDEPIPFWTFLSRILTGLNYEapkyhipywvayylallvsllvmllspviqLQPTFTPMRVA-----LAGTfh 324
Cdd:cd05256  231 GEVYNIGTGKRTSVNELAELIREILGKE------------------------------LEPVYAPPRPGdvrhsLADI-- 278
                        330       340       350
                 ....*....|....*....|....*....|
gi 928185501 325 yyscERARKVMGYRPLVTMDDAIERTVQSF 354
Cdd:cd05256  279 ----SKAKKLLGWEPKVSFEEGLRLTVEWF 304
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
30-255 5.36e-36

extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 212494 [Multi-domain]  Cd Length: 200  Bit Score: 129.73  E-value: 5.36e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFDMRqgfdnprvqfflgdlcsqqdlypalkgvSTVFHCA---SPPPSSNNKELFY 106
Cdd:cd08946    3 VTGGAGFIGSHLVRRLLERGHEVVVIDRL----------------------------DVVVHLAalvGVPASWDNPDEDF 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 107 RVNYIGTKNVIETCKEAGVQKLILTSSASViFEGVNIKNGTEdlPYAMKPIDYYTETKILQERAVLDANDpKRNFLTMAI 186
Cdd:cd08946   55 ETNVVGTLNLLEAARKAGVKRFVYASSASV-YGSPEGLPEEE--ETPPRPLSPYGVSKLAAEHLLRSYGE-SYGLPVVIL 130
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928185501 187 RPHGIFGPRDPQ----LVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHGHILAAEhlsqDTAVSGKAFHI 255
Cdd:cd08946  131 RLANVYGPGQRPrldgVVNDFIRRALEGKPLTVFGGGNQTRDFIHVDDVVRAILHALE----NPLEGGGVYNI 199
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
30-255 6.11e-35

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 127.80  E-value: 6.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501   30 VIGGSGFLGQHMVEQLLARGYTVNVFDMRQGFDNP----RVQFFLGDLCSQQDL--YPALKGVSTVFHCA---SPPPSSN 100
Cdd:pfam01370   3 VTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASNTarlaDLRFVEGDLTDRDALekLLADVRPDAVIHLAavgGVGASIE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  101 NKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVI--FEGVNIKNGTEDLPYAmkPIDYYTETKILQERAVLDANDpK 178
Cdd:pfam01370  83 DPEDFIEANVLGTLNLLEAARKAGVKRFLFASSSEVYgdGAEIPQEETTLTGPLA--PNSPYAAAKLAGEWLVLAYAA-A 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  179 RNFLTMAIRPHGIFGPRDPQ-----LVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHGHILAAEHLsqdtAVSGKAF 253
Cdd:pfam01370 160 YGLRAVILRLFNVYGPGDNEgfvsrVIPALIRRILEGKPILLWGDGTQRRDFLYVDDVARAILLALEHG----AVKGEIY 235

                  ..
gi 928185501  254 HI 255
Cdd:pfam01370 236 NI 237
FR_SDR_e cd08958
flavonoid reductase (FR), extended (e) SDRs; This subgroup contains FRs of the extended ...
30-243 2.59e-28

flavonoid reductase (FR), extended (e) SDRs; This subgroup contains FRs of the extended SDR-type and related proteins. These FRs act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites; they have the characteristic active site triad of the SDRs (though not the upstream active site Asn) and a NADP-binding motif that is very similar to the typical extended SDR motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187661 [Multi-domain]  Cd Length: 293  Bit Score: 111.51  E-value: 2.59e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVN--------------VFDMrQGFDNpRVQFFLGDLCSQQDLYPALKGVSTVFHCASP 95
Cdd:cd08958    3 VTGASGFIGSWLVKRLLQRGYTVRatvrdpgdekkvahLLEL-EGAKE-RLKLFKADLLDYGSFDAAIDGCDGVFHVASP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  96 P---PSSNNKELF-YRVNyiGTKNVIETCKEAG-VQKLILTSSASVIFEGVNIKNGTE-------DLPYAMKPIDYYTET 163
Cdd:cd08958   81 VdfdSEDPEEEMIePAVK--GTLNVLEACAKAKsVKRVVFTSSVAAVVWNPNRGEGKVvdescwsDLDFCKKTKLWYALS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 164 KILQERAVLDANdpKRNFLTMA-IRPHGIFGPRDPQLVPILIEAArkgkMKFMIGNGENLVDFTF----VENVVHGHILA 238
Cdd:cd08958  159 KTLAEKAAWEFA--EENGLDLVtVNPSLVVGPFLQPSLNSSSQLI----LSLLKGNAEMYQNGSLalvhVDDVADAHILL 232

                 ....*
gi 928185501 239 AEHLS 243
Cdd:cd08958  233 YEKPS 237
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
30-286 7.62e-26

aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 105.04  E-value: 7.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVN--VFDM----------RQGFDNPRVQFFLGDLCSQQDLY-PALKGVSTVFHCASPP 96
Cdd:cd05227    4 VTGATGFIASHIVEQLLKAGYKVRgtVRSLsksaklkallKAAGYNDRLEFVIVDDLTAPNAWdEALKGVDYVIHVASPF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  97 PSSN--NKELFYRVNYIGTKNVIETCKEAG-VQKLILTSSASVIFEGVNIKNG--------TEDLPYAMKPIDYYTETKI 165
Cdd:cd05227   84 PFTGpdAEDDVIDPAVEGTLNVLEAAKAAGsVKRVVLTSSVAAVGDPTAEDPGkvfteedwNDLTISKSNGLDAYIASKT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 166 LQERA---VLDANDPKRNFLTMAirPHGIFGP-RDPQLVPILIEAARK---GKMKFMIGN-GENLVDftfVENVVHGHIL 237
Cdd:cd05227  164 LAEKAaweFVKENKPKFELITIN--PGYVLGPsLLADELNSSNELINKlldGKLPAIPPNlPFGYVD---VRDVADAHVR 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 928185501 238 AAEHlsqdTAVSGKAFHITNDepiPFWTflSRILTGLNYEAPKYHIPYW 286
Cdd:cd05227  239 ALES----PEAAGQRFIVSAG---PFSF--QEIADLLREEFPQLTAPFP 278
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
30-353 8.76e-26

UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially conserves the characteristic active site tetrad and NAD-binding motif of the extended SDRs, and has been identified as possible UDP-glucose 4-epimerase (aka UDP-galactose 4-epimerase), a homodimeric member of the extended SDR family. UDP-glucose 4-epimerase catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187574 [Multi-domain]  Cd Length: 300  Bit Score: 105.09  E-value: 8.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFDMR---QGFDNPRVQFFLGDLCSQQDLYPALKGVSTVFHCAS---PPPSSNNKE 103
Cdd:cd05264    4 IVGGNGFIGSHLVDALLEEGPQVRVFDRSippYELPLGGVDYIKGDYENRADLESALVGIDTVIHLASttnPATSNKNPI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 104 LFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFeGVnikngTEDLPYA----MKPIDYYTETKILQERaVLDANDPKR 179
Cdd:cd05264   84 LDIQTNVAPTVQLLEACAAAGIGKIIFASSGGTVY-GV-----PEQLPISesdpTLPISSYGISKLAIEK-YLRLYQYLY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 180 NFLTMAIRPHGIFGPRdpQ-------LVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHGhILAAEHLSQDTAVsgka 252
Cdd:cd05264  157 GLDYTVLRISNPYGPG--QrpdgkqgVIPIALNKILRGEPIEIWGDGESIRDYIYIDDLVEA-LMALLRSKGLEEV---- 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 253 FHITNDEPIPFWTFLSRILTGLNYEAPKYHIPywvayylallvsllvmllspviqlQPTFTPMRVALagtfhyySCERAR 332
Cdd:cd05264  230 FNIGSGIGYSLAELIAEIEKVTGRSVQVIYTP------------------------ARTTDVPKIVL-------DISRAR 278
                        330       340
                 ....*....|....*....|.
gi 928185501 333 KVMGYRPLVTMDDAIERTVQS 353
Cdd:cd05264  279 AELGWSPKISLEDGLEKTWQW 299
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
30-355 1.38e-25

Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme involved in the modification of outer membrane protein lipid A of gram-negative bacteria. It is a bifunctional enzyme that catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid and N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-l-arabinose; its NAD-dependent decaboxylating activity is in the C-terminal 360 residues. This subgroup belongs to the extended SDR family, however the NAD binding motif is not a perfect match and the upstream Asn of the canonical active site tetrad is not conserved. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187567 [Multi-domain]  Cd Length: 316  Bit Score: 104.69  E-value: 1.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFDMRQGF---------DNPRVQFFLGDLCSQQDLYPALKGVSTVFHCAS---PPP 97
Cdd:cd05257    4 VTGADGFIGSHLTERLLREGHEVRALDIYNSFnswglldnaVHDRFHFISGDVRDASEVEYLVKKCDVVFHLAAliaIPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  98 SSNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKNgTEDLP--YAMKPIDYYTETKILQERAVLD-A 174
Cdd:cd05257   84 SYTAPLSYVETNVFGTLNVLEAACVLYRKRVVHTSTSEVYGTAQDVPI-DEDHPllYINKPRSPYSASKQGADRLAYSyG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 175 NDPKRNFLTmaIRPHGIFGPR--DPQLVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHGHILAAEHLSqdtaVSGKA 252
Cdd:cd05257  163 RSFGLPVTI--IRPFNTYGPRqsARAVIPTIISQRAIGQRLINLGDGSPTRDFNFVKDTARGFIDILDAIE----AVGEI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 253 FHITNDEPIPFWTFLSRILTGLNYEAPKyhIPYwvayylallvsllvmllSPVIQLQPTFTPM--RVALAGtfhyysceR 330
Cdd:cd05257  237 INNGSGEEISIGNPAVELIVEELGEMVL--IVY-----------------DDHREYRPGYSEVerRIPDIR--------K 289
                        330       340
                 ....*....|....*....|....*
gi 928185501 331 ARKVMGYRPLVTMDDAIERTVQSFH 355
Cdd:cd05257  290 AKRLLGWEPKYSLRDGLRETIEWFK 314
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
29-193 2.60e-24

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 97.86  E-value: 2.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  29 TVIGGSGFLGQHMVEQLLARGYTVNVFDMRQ----GFDNPRVQFFLGDLCSQQDLYPALKGVSTVFHCASPPPSSnnkEL 104
Cdd:cd05226    2 LILGATGFIGRALARELLEQGHEVTLLVRNTkrlsKEDQEPVAVVEGDLRDLDSLSDAVQGVDVVIHLAGAPRDT---RD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 105 FYRVNYIGTKNVIETCKEAGVQKLILTSSASVifegvnikNGTEDLPYAMKPIDYYTETKILQERAVLDANDPkrnflTM 184
Cdd:cd05226   79 FCEVDVEGTRNVLEAAKEAGVKHFIFISSLGA--------YGDLHEETEPSPSSPYLAVKAKTEAVLREASLP-----YT 145

                 ....*....
gi 928185501 185 AIRPHGIFG 193
Cdd:cd05226  146 IVRPGVIYG 154
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
30-261 1.61e-23

UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of archaeal and bacterial proteins, and has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187545 [Multi-domain]  Cd Length: 305  Bit Score: 98.91  E-value: 1.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFD---------MRQGFDNPRVQFFLGDLCSQQDLyPALKGVSTVFHCASPPP--- 97
Cdd:cd05234    4 VTGGAGFIGSHLVDRLLEEGNEVVVVDnlssgrrenIEPEFENKAFRFVKRDLLDTADK-VAKKDGDTVFHLAANPDvrl 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  98 SSNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKngTEDLpYAMKPIDYYTETKILQErAVLDANDP 177
Cdd:cd05234   83 GATDPDIDLEENVLATYNVLEAMRANGVKRIVFASSSTVYGEAKVIP--TPED-YPPLPISVYGASKLAAE-ALISAYAH 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 178 KRNFLTMAIRPHGIFGPRDPQ-LVPILIEAARKG-KMKFMIGNGENLVDFTFVENVVHGHILAAEHLSQDTAVsgkaFHI 255
Cdd:cd05234  159 LFGFQAWIFRFANIVGPRSTHgVIYDFINKLKRNpNELEVLGDGRQRKSYLYVSDCVDAMLLAWEKSTEGVNI----FNL 234

                 ....*.
gi 928185501 256 TNDEPI 261
Cdd:cd05234  235 GNDDTI 240
GalE COG1087
UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];
30-257 7.41e-23

UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224012 [Multi-domain]  Cd Length: 329  Bit Score: 97.24  E-value: 7.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFD-----MRQGFDNPRVQFFLGDLCSQQDLYPALK--GVSTVFHCA---SPPPSS 99
Cdd:COG1087    5 VTGGAGYIGSHTVRQLLKTGHEVVVLDnlsngHKIALLKLQFKFYEGDLLDRALLTAVFEenKIDAVVHFAasiSVGESV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 100 NNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKNgTEDLPyaMKPIDYYTETKILQERAVLDANdpKR 179
Cdd:COG1087   85 QNPLKYYDNNVVGTLNLIEAMLQTGVKKFIFSSTAAVYGEPTTSPI-SETSP--LAPINPYGRSKLMSEEILRDAA--KA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 180 NFLTMAI-R--------PHGIFGPRDP---QLVPILIEAARKGKMKFMI-GN------GENLVDFTFVENVVHGHILAAE 240
Cdd:COG1087  160 NPFKVVIlRyfnvagacPDGTLGQRYPgatLLIPVAAEAALGKRDKLFIfGDdydtkdGTCIRDYIHVDDLADAHVLALK 239
                        250
                 ....*....|....*..
gi 928185501 241 HLSQdtavsGKAFHITN 257
Cdd:COG1087  240 YLKE-----GGSNNIFN 251
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
30-257 5.30e-22

UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187558 [Multi-domain]  Cd Length: 323  Bit Score: 94.91  E-value: 5.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFD-----MRQGFD---NPRVQFFLGDLCSQQDLYPALK--GVSTVFHCA---SPP 96
Cdd:cd05247    4 VTGGAGYIGSHTVVELLEAGYDVVVLDnlsngHREALPrieKIRIEFYEGDIRDRAALDKVFAehKIDAVIHFAalkAVG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  97 PSSNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKNgTEDLPyaMKPIDYYTETKILQERAVLD--- 173
Cdd:cd05247   84 ESVQKPLKYYDNNVVGTLNLLEAMRAHGVKNFVFSSSAAVYGEPETVPI-TEEAP--LNPTNPYGRTKLMVEQILRDlak 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 174 ANDPK----RNFLTMAIRPHGIFG--PRDPQ-LVPILIEAARKGKMKFMI-GN------GENLVDFTFVENVVHGHILAA 239
Cdd:cd05247  161 APGLNyvilRYFNPAGAHPSGLIGedPQIPNnLIPYVLQVALGRREKLAIfGDdyptpdGTCVRDYIHVVDLADAHVLAL 240
                        250
                 ....*....|....*...
gi 928185501 240 EHLSqdtavSGKAFHITN 257
Cdd:cd05247  241 EKLE-----NGGGSEIYN 253
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
30-261 8.45e-22

Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187573 [Multi-domain]  Cd Length: 293  Bit Score: 93.97  E-value: 8.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFdMRQGFDN-------------PRVQFFLGDLC------SQQDLYPALKGVSTVF 90
Cdd:cd05263    3 VTGGTGFLGRHLVKRLLENGFKVLVL-VRSESLGeaherieeagleaDRVRVLEGDLTqpnlglSAAASRELAGKVDHVI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  91 HCASPPPSSNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKNGTEDLP-YAMKpiDYYTETKILQER 169
Cdd:cd05263   82 HCAASYDFQAPNEDAWRTNIDGTEHVLELAARLDIQRFHYVSTAYVAGNREGNIRETELNPgQNFK--NPYEQSKAEAEQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 170 AVLDAndPKRNFLTmAIRPHGIFGP----RDPQLVPI--LIEAARK-GKMKFMIGNGENLVDFTFVENVVHGHILAAEHL 242
Cdd:cd05263  160 LVRAA--ATQIPLT-VYRPSIVVGDsktgRIEKIDGLyeLLNLLAKlGRWLPMPGNKGARLNLVPVDYVADAIVYLSKKP 236
                        250
                 ....*....|....*....
gi 928185501 243 SQDtavsGKAFHITNDEPI 261
Cdd:cd05263  237 EAN----GQIFHLTDPTPQ 251
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
27-284 8.03e-20

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 87.35  E-value: 8.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  27 KCTVIGGSGFLGQHMVEQLLARGYTVNVFD--MRQGFDNPRVQFFLGDLCSQQDLYPALKGVS--TVFHCASPPPSSnnk 102
Cdd:cd05265    2 KILIIGGTRFIGKALVEELLAAGHDVTVFNrgRTKPDLPEGVEHIVGDRNDRDALEELLGGEDfdVVVDTIAYTPRQ--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 103 elfyrvnyigTKNVIETCKEAgVQKLILTSSASVIfeGVNIKNGTEDLPYAMKPID------YYTETKILQERAVLDAnd 176
Cdd:cd05265   79 ----------VERALDAFKGR-VKQYIFISSASVY--LKPGRVITESTPLREPDAVglsdpwDYGRGKRAAEDVLIEA-- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 177 PKRNFltMAIRPHGIFGPRDPQ-LVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHGHILAAEHlsqDTAVsGKAFHI 255
Cdd:cd05265  144 AAFPY--TIVRPPYIYGPGDYTgRLAYFFDRLARGRPILVPGDGHSLVQFIHVKDLARALLGAAGN---PKAI-GGIFNI 217
                        250       260
                 ....*....|....*....|....*....
gi 928185501 256 TNDEPIPFWTFLSRILTGLNYEAPKYHIP 284
Cdd:cd05265  218 TGDEAVTWDELLEACAKALGKEAEIVHVE 246
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
27-288 1.02e-19

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 87.69  E-value: 1.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  27 KCTVIGGSGFLGQHMVEQLLARGYTVNVF---------DMRQGfDNPRVQFFLGDLCSQQDLYPALKGVSTVFHCA-SPP 96
Cdd:cd05271    2 VVTVFGATGFIGRYVVNRLAKRGSQVIVPyrceayarrLLVMG-DLGQVLFVEFDLRDDESIRKALEGSDVVINLVgRLY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  97 PSSNNKelFYRVNYIGTKNVIETCKEAGVQKLILTSSAsvifeGVNIKNGTEdlpyamkpidyYTETKILQERAVLDAnd 176
Cdd:cd05271   81 ETKNFS--FEDVHVEGPERLAKAAKEAGVERLIHISAL-----GADANSPSK-----------YLRSKAEGEEAVREA-- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 177 pkrnFLTMAI-RPHGIFGPRDpQLVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHghilAAEHLSQDTAVSGKAFHI 255
Cdd:cd05271  141 ----FPEATIvRPSVVFGRED-RFLNRFAKLLAFLPFPPLIGGGQTKFQPVYVGDVAE----AIARALKDPETEGKTYEL 211
                        250       260       270
                 ....*....|....*....|....*....|...
gi 928185501 256 TNDEPIPFWTFLSRILTGLNYEAPKYHIPYWVA 288
Cdd:cd05271  212 VGPKVYTLAELVELLRRLGGRKRRVLPLPLWLA 244
NAD_binding_10 pfam13460
NAD(P)H-binding;
32-171 2.68e-17

NAD(P)H-binding;


Pssm-ID: 433226 [Multi-domain]  Cd Length: 183  Bit Score: 78.80  E-value: 2.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501   32 GGSGFLGQHMVEQLLARGYTVNVF-----DMRQGFDNPRVQFFLGDLCSQQDLYPALKGVSTVFHCASPPPSSNNkelfy 106
Cdd:pfam13460   1 GATGKIGRLLVKQLLARGHEVTALvrnpeKLADLEDHPGVEVVDGDVLDPDDLAEALKGQDAVISALGGGGTDEE----- 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928185501  107 rvnyiGTKNVIETCKEAGVQKLILTSSAsvifeGVNIKNGTEDLPYAMKPIDYYTETKILQERAV 171
Cdd:pfam13460  76 -----GAKNIIDAAKAAGVKRFILVSSL-----GVGDEVPGPFGPWNKEMLGPYLAAKRAAEELL 130
AR_like_SDR_e cd05193
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This ...
30-289 3.26e-17

aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This subgroup contains aldehyde reductase and flavonoid reductase of the extended SDR-type and related proteins. Proteins in this subgroup have a complete SDR-type active site tetrad and a close match to the canonical extended SDR NADP-binding motif. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187536 [Multi-domain]  Cd Length: 295  Bit Score: 80.74  E-value: 3.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVN--------------VFDMRQGfdNPRVQFFLGDLCSQQDLYPALKGVSTVFHCASP 95
Cdd:cd05193    3 VTGASGFVASHVVEQLLERGYKVRatvrdpskvkkvnhLLDLDAK--PGRLELAVADLTDEQSFDEVIKGCAGVFHVATP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  96 PP-SSNNKELFYRVNYIGTKNVIETCKEAG-VQKLILTSSASVIfeGVNIKNGT------------EDLPYAMKPIDYYT 161
Cdd:cd05193   81 VSfSSKDPNEVIKPAIGGTLNALKAAAAAKsVKRFVLTSSAGSV--LIPKPNVEgivldekswnleEFDSDPKKSAWVYA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 162 ETKILQERAVLDANDpKRNFLTMAIRPHGIFGP-RDPQLVPILIEAARKGKMKFMIGNGENLVD---FTFVENVVHGHIL 237
Cdd:cd05193  159 ASKTLAEKAAWKFAD-ENNIDLITVIPTLTIGTiFDSETPSSSGWAMSLITGNEGVSPALALIPpgyYVHVVDICLAHIG 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 928185501 238 AAEHLSQDTAVSGKAFHITndepipfwtfLSRILTGLNYEAPKYHIPYWVAY 289
Cdd:cd05193  238 CLELPIARGRYICTAGNFD----------WNTLLKTLRKKYPSYTFPTDFPD 279
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
30-133 6.92e-17

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 78.05  E-value: 6.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVF----DMRQGFDNPRVQFFLGDLCSQQDLYPALKGVSTVFHCASPPPSSnnKELF 105
Cdd:cd05243    4 VVGATGKVGRHVVRELLDRGYQVRALvrdpSQAEKLEAAGAEVVVGDLTDAESLAAALEGIDAVISAAGSGGKG--GPRT 81
                         90       100
                 ....*....|....*....|....*...
gi 928185501 106 YRVNYIGTKNVIETCKEAGVQKLILTSS 133
Cdd:cd05243   82 EAVDYDGNINLIDAAKKAGVKRFVLVSS 109
GME-like_SDR_e cd05273
Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup ...
30-241 3.05e-16

Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup of NDP-sugar epimerase/dehydratases are extended SDRs; they have the characteristic active site tetrad, and an NAD-binding motif: TGXXGXX[AG], which is a close match to the canonical NAD-binding motif. Members include Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME) which catalyzes the epimerization of two positions of GDP-alpha-D-mannose to form GDP-beta-L-galactose. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187581 [Multi-domain]  Cd Length: 328  Bit Score: 78.68  E-value: 3.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFDMRQ-GF---DNPRVQFFLGDLCSQQDLYPALKGVSTVFHCASPPP-----SSN 100
Cdd:cd05273    5 VTGAGGFIGSHLAERLKAEGHYVRGADWKSpEHmtqPTDDDEFHLVDLREMENCLKATEGVDHVFHLAADMGgmgyiQSN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 101 NKELFYRvNYIGTKNVIETCKEAGVQKLILTSSASV----IFEGVNIKNGTEDLPYAMKPIDYYTETKILQERAvLDAND 176
Cdd:cd05273   85 HAVIMYN-NTLINFNMLEAARINGVERFLFASSACVypefKQLETTVVRLREEDAWPAEPQDAYGWEKLATERL-CQHYN 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928185501 177 PKRNFLTMAIRPHGIFGPRD----------PQLVPILIEAARKGKMKfMIGNGENLVDFTFVENVVHGHILAAEH 241
Cdd:cd05273  163 EDYGIETRIVRFHNIYGPRGtwdggrekapAAMCRKVATAKDGDRFE-IWGDGLQTRSFTYIDDCVEGLRRLMES 236
SDR_a3 cd05229
atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a ...
29-287 5.25e-16

atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a glycine-rich NAD(P)-binding motif consensus that is very similar to the extended SDRs, GXXGXXG. Generally, this group has poor conservation of the active site tetrad, However, individual sequences do contain matches to the YXXXK active site motif, and generally Tyr or Asn in place of the upstream Ser found in most SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187540 [Multi-domain]  Cd Length: 302  Bit Score: 77.37  E-value: 5.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  29 TVIGGSGFLGQHMVEQLLARGYTVNVFDMRQGFD--NPRVQFFLGDLCSQQDLYPALKGVSTVFHCASpPPSSNNKELFY 106
Cdd:cd05229    3 HVLGASGPIGREVARELRRRGWDVRLVSRSGSKLawLPGVEIVAADAMDASSVIAAARGADVIYHCAN-PAYTRWEELFP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 107 RVnyigTKNVIETCKEAGVqKLILTSsaSVIFEGVNIKN-GTEDLPyaMKPIDYYTETKILQERAVLDANDpKRNFLTMA 185
Cdd:cd05229   82 PL----MENVVAAAEANGA-KLVLPG--NVYMYGPQAGSpITEDTP--FQPTTRKGRIRAEMEERLLAAHA-KGDIRALI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 186 IRPHGIFGPRDPQ-LVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHGHILAAEhlsQDTAvSGKAFHITNDEPIPFW 264
Cdd:cd05229  152 VRAPDFYGPGAINsWLGAALFAILQGKTAVFPGNLDTPHEWTYLPDVARALVTLAE---EPDA-FGEAWHLPGAGAITTR 227
                        250       260
                 ....*....|....*....|....
gi 928185501 265 TFLSRILTGLNYEaPKYH-IPYWV 287
Cdd:cd05229  228 ELIAIAARAAGRP-PKVRvIPKWT 250
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
30-260 7.37e-16

UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187543 [Multi-domain]  Cd Length: 303  Bit Score: 77.01  E-value: 7.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTV--NVfDMRQGFDNPRVQFFLGDLCSQQDLYPalkGVSTVFHCAS-----PPPSSNNK 102
Cdd:cd05232    4 VTGANGFIGRALVDKLLSRGEEVriAV-RNAENAEPSVVLAELPDIDSFTDLFL---GVDAVVHLAArvhvmNDQGADPL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 103 ELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKNGTEDLPyaMKPIDYYTETKILQERAVLDANdPKRNFL 182
Cdd:cd05232   80 SDYRKVNTELTRRLARAAARQGVKRFVFLSSVKVNGEGTVGAPFDETDP--PAPQDAYGRSKLEAERALLELG-ASDGME 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 183 TMAIRPHGIFGPRDPQLVPILIEAARKGK--MKFMIGNGENLVdftFVENVVHGHILAAEHlsqdTAVSGKAFHITNDEP 260
Cdd:cd05232  157 VVILRPPMVYGPGVRGNFARLMRLIDRGLplPPGAVKNRRSLV---SLDNLVDAIYLCISL----PKAANGTFLVSDGPP 229
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
32-350 4.67e-15

GDP-mannose 4,6 dehydratase;


Pssm-ID: 435301 [Multi-domain]  Cd Length: 327  Bit Score: 74.89  E-value: 4.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501   32 GGSGFLGQHMVEQLLARGYTVNVFDMR-------------QGFDNPRVQFFLGDLCSQQDLYPALKGVS--TVFHCA--- 93
Cdd:pfam16363   4 GITGQDGSYLAELLLEKGYEVHGIVRRsssfntgrlehlyDDHLNGNLVLHYGDLTDSSNLVRLLAEVQpdEIYNLAaqs 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501   94 SPPPSSNNKELFYRVNYIGTKNVIETCKEAGVQ---KLILTSSASViFegvniknG-------TEDLPYAmkPIDYYTET 163
Cdd:pfam16363  84 HVDVSFEQPEYTADTNVLGTLRLLEAIRSLGLEkkvRFYQASTSEV-Y-------GkvqevpqTETTPFY--PRSPYAAA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  164 KILQEravldandpkrnFLTMAIR-PHGIF----------GPR-----DPQLVPILIEAARKGKMKFMI-GNGENLVDFT 226
Cdd:pfam16363 154 KLYAD------------WIVVNYReSYGLFacngilfnheSPRrgerfVTRKITRGVARIKLGKQEKLYlGNLDAKRDWG 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  227 FVENVVHGHILAAEHLSQDTAVSG------------KAFHITNDEPipfwTFLSRILTGLNYEAPKYHIPYwvayylall 294
Cdd:pfam16363 222 HARDYVEAMWLMLQQDKPDDYVIAtgethtvrefveKAFLELGLTI----TWEGKGEIGYFKASGKVHVLI--------- 288
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 928185501  295 vsllvmllspviqlqpTFTPMRVALAgTFHYYSCERARKVMGYRPLVTMDDAIERT 350
Cdd:pfam16363 289 ----------------DPRYFRPGEV-DRLLGDPSKAKEELGWKPKVSFEELVREM 327
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
30-261 9.72e-15

dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 73.43  E-value: 9.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVnvfdmrQGFDNPRVQFFLGDLcsqQDLYPALKGVST-----VFHCA---SPPPSSNN 101
Cdd:cd05254    4 ITGATGMLGRALVRLLKERGYEV------IGTGRSRASLFKLDL---TDPDAVEEAIRDykpdvIINCAaytRVDKCESD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 102 KELFYRVNYIGTKNVIETCKEAGVqKLILTSSASViFEGVNIKNGTEDLPyamKPIDYYTETKILQERAVLDANDpkrNF 181
Cdd:cd05254   75 PELAYRVNVLAPENLARAAKEVGA-RLIHISTDYV-FDGKKGPYKEEDAP---NPLNVYGKSKLLGEVAVLNANP---RY 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 182 LTmaIRPHGIFGPrdpqlvpilieaarkgkmkfmIGNGENLVDfTFVE--------NVVHGHI--------LAA--EHLS 243
Cdd:cd05254  147 LI--LRTSWLYGE---------------------LKNGENFVE-WMLRlaaerkevNVVHDQIgsptyaadLADaiLELI 202
                        250
                 ....*....|....*...
gi 928185501 244 QDTAVSGkAFHITNDEPI 261
Cdd:cd05254  203 ERNSLTG-IYHLSNSGPI 219
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
30-352 3.65e-13

UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid 4-epimerase, an extended SDR, which catalyzes the conversion of UDP-alpha-D-glucuronic acid to UDP-alpha-D-galacturonic acid. This group has the SDR's canonical catalytic tetrad and the TGxxGxxG NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187563 [Multi-domain]  Cd Length: 332  Bit Score: 69.29  E-value: 3.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFDMRQGFDNPRVQ--------------FFLGDLCSQQDLYPALKGVST--VFHCA 93
Cdd:cd05253    5 VTGAAGFIGFHVAKRLLERGDEVVGIDNLNDYYDVRLKearlellgksggfkFVKGDLEDREALRRLFKDHEFdaVIHLA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  94 SPPP---SSNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIfeGVNIKNGTEDLPYAMKPIDYYTETKilqera 170
Cdd:cd05253   85 AQAGvrySLENPHAYVDSNIVGFLNLLELCRHFGVKHLVYASSSSVY--GLNTKMPFSEDDRVDHPISLYAATK------ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 171 vldandpKRNFLtMA-------------IRPHGIFGP--RdPQLVPIL-IEAARKGKMKFMIGNGENLVDFTFVENVVHG 234
Cdd:cd05253  157 -------KANEL-MAhtyshlygipttgLRFFTVYGPwgR-PDMALFLfTKAILEGKPIDVFNDGNMSRDFTYIDDIVEG 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 235 HILAAEHLSQ-DTAVSGKA------------FHITNDEPIPFWTFLSRILTGLNYEAPKYHIPywvayylallvsllvml 301
Cdd:cd05253  228 VVRALDTPAKpNPNWDAEApdpstssapyrvYNIGNNSPVKLMDFIEALEKALGKKAKKNYLP----------------- 290
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 928185501 302 lspviqLQPTFTPmrvalagtFHYYSCERARKVMGYRPLVTMDDAIERTVQ 352
Cdd:cd05253  291 ------MQKGDVP--------ETYADISKLQRLLGYKPKTSLEEGVKRFVE 327
PLN02240 PLN02240
UDP-glucose 4-epimerase
30-201 7.97e-13

UDP-glucose 4-epimerase


Pssm-ID: 177883 [Multi-domain]  Cd Length: 352  Bit Score: 68.45  E-value: 7.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFDmrqGFDNP------RVQ-----------FFLGDLCSQQDLYP--ALKGVSTVF 90
Cdd:PLN02240  10 VTGGAGYIGSHTVLQLLLAGYKVVVID---NLDNSseealrRVKelagdlgdnlvFHKVDLRDKEALEKvfASTRFDAVI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  91 HCA---SPPPSSNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKnGTEDLP-YAMKPidyYTETKIL 166
Cdd:PLN02240  87 HFAglkAVGESVAKPLLYYDNNLVGTINLLEVMAKHGCKKLVFSSSATVYGQPEEVP-CTEEFPlSATNP---YGRTKLF 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 928185501 167 QERAVLD--ANDPK------RNFLTMAIRPHGIFGpRDPQLVP 201
Cdd:PLN02240 163 IEEICRDihASDPEwkiillRYFNPVGAHPSGRIG-EDPKGIP 204
UDP_G4E_3_SDR_e cd05240
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ...
30-194 1.18e-12

UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial subgroup are identified as possible sugar epimerases, such as UDP-glucose 4 epimerase. However, while the NAD(P)-binding motif is fairly well conserved, not all members retain the canonical active site tetrad of the extended SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187551 [Multi-domain]  Cd Length: 306  Bit Score: 67.78  E-value: 1.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLA--RGYTVNVFDMRQ-GFDNPRVQFFLGDLCSQQ-DLYPALKGVSTVFHCASPPPSSNNKELF 105
Cdd:cd05240    3 VTGAAGGLGRLLARRLAAspRVIGVDGLDRRRpPGSPPKVEYVRLDIRDPAaADVFREREADAVVHLAFILDPPRDGAER 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 106 YRVNYIGTKNVIETCKEAGVQKLILTSSASVIfeGVNIKNG---TEDLPYAMKPIDYYTETKILQERAV--LDANDPKRN 180
Cdd:cd05240   83 HRINVDGTQNVLDACAAAGVPRVVVTSSVAVY--GAHPDNPaplTEDAPLRGSPEFAYSRDKAEVEQLLaeFRRRHPELN 160
                        170
                 ....*....|....
gi 928185501 181 flTMAIRPHGIFGP 194
Cdd:cd05240  161 --VTVLRPATILGP 172
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
30-135 3.55e-12

CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that catalyzes the conversion of CDP-D-paratose to CDP-D-tyvelose, the last step in tyvelose biosynthesis. This subgroup is a member of the extended SDR subfamily, with a characteristic active site tetrad and NAD-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187568 [Multi-domain]  Cd Length: 337  Bit Score: 66.54  E-value: 3.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFD--MRQGFDNPR-----------VQFFLGDLCSQQDLYPALKGVSTVFHCASPP 96
Cdd:cd05258    5 ITGGAGFIGSNLARFFLKQGWEVIGFDnlMRRGSFGNLawlkanredggVRFVHGDIRNRNDLEDLFEDIDLIIHTAAQP 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 928185501  97 P---SSNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSAS 135
Cdd:cd05258   85 SvttSASSPRLDFETNALGTLNVLEAARQHAPNAPFIFTSTN 126
BVR-B_like_SDR_a cd05244
biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; ...
27-171 6.91e-12

biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187555 [Multi-domain]  Cd Length: 207  Bit Score: 63.80  E-value: 6.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  27 KCTVIGGSGFLGQHMVEQLLARGYTVNVFDMRQGF---DNPRVQFFLGDLCSQQDLYPALKGVSTVFHCASPPPSSNNKE 103
Cdd:cd05244    1 KIAIIGATGRTGSAIVREALARGHEVTALVRDPAKlpaEHEKLKVVQGDVLDLEDVKEALEGQDAVISALGTRNDLSPTT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928185501 104 LFYRvnyiGTKNVIETCKEAGVQKLILTSSASV--IFEGVNIKNGTEDLPYAMKPI--DYYTETKILQERAV 171
Cdd:cd05244   81 LHSE----GTRNIVSAMKAAGVKRLIVVGGAGSldDRPKVTLVLDTLLFPPALRRVaeDHARMLKVLRESGL 148
PLN00198 PLN00198
anthocyanidin reductase; Provisional
25-284 1.08e-11

anthocyanidin reductase; Provisional


Pssm-ID: 215100 [Multi-domain]  Cd Length: 338  Bit Score: 65.29  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  25 ASKCTVIGGSGFLGQHMVEQLLARGYTVNVfDMRQGFDNPRV------------QFFLGDLCSQQDLYPALKGVSTVFHC 92
Cdd:PLN00198   9 KKTACVIGGTGFLASLLIKLLLQKGYAVNT-TVRDPENQKKIahlralqelgdlKIFGADLTDEESFEAPIAGCDLVFHV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  93 ASPP--PSSNNKELFYRVNYIGTKNVIETC-KEAGVQKLILTSSASVIfeGVNIKNGT---------EDLPY--AMKPID 158
Cdd:PLN00198  88 ATPVnfASEDPENDMIKPAIQGVHNVLKACaKAKSVKRVILTSSAAAV--SINKLSGTglvmneknwTDVEFltSEKPPT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 159 Y-YTETKILQERAVLD-ANDPKRNFLTmaIRPHGIFGPRDPQLVPILIEAArkgkMKFMIGNgENLVD------------ 224
Cdd:PLN00198 166 WgYPASKTLAEKAAWKfAEENNIDLIT--VIPTLMAGPSLTSDIPSSLSLA----MSLITGN-EFLINglkgmqmlsgsi 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 928185501 225 -FTFVENVVHGHILAAEhlsQDTAvSGKAFHITNDEPIPfwtflsRILTGLNYEAPKYHIP 284
Cdd:PLN00198 239 sITHVEDVCRAHIFLAE---KESA-SGRYICCAANTSVP------ELAKFLIKRYPQYQVP 289
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
32-241 4.96e-11

GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, catalyzes the NADP(H)-dependent conversion of GDP-(D)-mannose to GDP-4-keto, 6-deoxy-(D)-mannose in the fucose biosynthesis pathway. These proteins have the canonical active site triad and NAD-binding pattern, however the active site Asn is often missing and may be substituted with Asp. A Glu residue has been identified as an important active site base. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187570 [Multi-domain]  Cd Length: 316  Bit Score: 63.00  E-value: 4.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  32 GGSGFLGQHMVEQLLARGYTVNVFDMRQG-----------FDNPRVQFFLGDLCSQQDLYPALKGVS--TVFHCAS---P 95
Cdd:cd05260    6 GITGQDGSYLAEFLLEKGYEVHGIVRRSSsfntdridhlyINKDRITLHYGDLTDSSSLRRAIEKVRpdEIYHLAAqshV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  96 PPSSNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFeGVNIKNG-TEDLP-YAMKPidyYTETKILQEravld 173
Cdd:cd05260   86 KVSFDDPEYTAEVNAVGTLNLLEAIRILGLDARFYQASSSEEY-GKVQELPqSETTPfRPRSP---YAVSKLYAD----- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 174 andpkrnFLTMAIR-PHGIF----------GP-RDPQLVP--ILIEAAR--KGKM-KFMIGNGENLVDFTFVENVVHGHI 236
Cdd:cd05260  157 -------WITRNYReAYGLFavngrlfnheGPrRGETFVTrkITRQVARikAGLQpVLKLGNLDAKRDWGDARDYVEAYW 229

                 ....*
gi 928185501 237 LAAEH 241
Cdd:cd05260  230 LLLQQ 234
PLN02662 PLN02662
cinnamyl-alcohol dehydrogenase family protein
30-240 6.95e-11

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178268 [Multi-domain]  Cd Length: 322  Bit Score: 62.42  E-value: 6.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVfDMRQGFD-------------NPRVQFFLGDLCSQQDLYPALKGVSTVFHCASPp 96
Cdd:PLN02662   9 VTGASGYIASWLVKLLLQRGYTVKA-TVRDPNDpkktehllaldgaKERLHLFKANLLEEGSFDSVVDGCEGVFHTASP- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  97 pssnnkeLFYRVN----------YIGTKNVIETC-KEAGVQKLILTSS-ASVIFEGvniKNGTEDL----------PYAM 154
Cdd:PLN02662  87 -------FYHDVTdpqaelidpaVKGTLNVLRSCaKVPSVKRVVVTSSmAAVAYNG---KPLTPDVvvdetwfsdpAFCE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 155 KPIDYYTETKILQERAVLdaNDPKRNFLTM-AIRPHGIFGprdPQLVPIL---IEAARKgkmkfMIGNGENLVDFTF--- 227
Cdd:PLN02662 157 ESKLWYVLSKTLAEEAAW--KFAKENGIDMvTINPAMVIG---PLLQPTLntsAEAILN-----LINGAQTFPNASYrwv 226
                        250
                 ....*....|....
gi 928185501 228 -VENVVHGHILAAE 240
Cdd:PLN02662 227 dVRDVANAHIQAFE 240
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
30-272 7.34e-11

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 223774 [Multi-domain]  Cd Length: 275  Bit Score: 61.84  E-value: 7.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVF--------DMRQGfdnprVQFFLGDLCSQQDLYPALKGVSTVFHCaspPPSSNN 101
Cdd:COG0702    5 VTGATGFVGGAVVRELLARGHEVRAAvrnpeaaaALAGG-----VEVVLGDLRDPKSLVAGAKGVDGVLLI---SGLLDG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 102 KELFYRVNYIGTKNVIETCKeAGVQKLILTSSAsvifeGVNIKNGTEdlpyamkpidyYTETKILQERAVLDANDPkrnf 181
Cdd:COG0702   77 SDAFRAVQVTAVVRAAEAAG-AGVKHGVSLSVL-----GADAASPSA-----------LARAKAAVEAALRSSGIP---- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 182 lTMAIRPHGIFGPRDPQLVPIlIEAARKGKMKFMIGNgENLVDftfVENVVHGHILAAEHlsqdTAVSGKAFHITNDEPI 261
Cdd:COG0702  136 -YTTLRRAAFYLGAGAAFIEA-AEAAGLPVIPRGIGR-LSPIA---VDDVAEALAAALDA----PATAGRTYELAGPEAL 205
                        250
                 ....*....|.
gi 928185501 262 PFWTFLSRILT 272
Cdd:COG0702  206 TLAELASGLDY 216
PRK10675 PRK10675
UDP-galactose-4-epimerase; Provisional
30-257 8.25e-11

UDP-galactose-4-epimerase; Provisional


Pssm-ID: 182639 [Multi-domain]  Cd Length: 338  Bit Score: 62.52  E-value: 8.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFD-------------MRQGFDNPRvqFFLGDLCSQQDLYPAL--KGVSTVFHCAS 94
Cdd:PRK10675   5 VTGGSGYIGSHTCVQLLQNGHDVVILDnlcnskrsvlpviERLGGKHPT--FVEGDIRNEALLTEILhdHAIDTVIHFAG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  95 PPP--SSNNKEL-FYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKNgTEDLPYAMkPIDYYTETKILQERAV 171
Cdd:PRK10675  83 LKAvgESVQKPLeYYDNNVNGTLRLISAMRAANVKNLIFSSSATVYGDQPKIPY-VESFPTGT-PQSPYGKSKLMVEQIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 172 LDAN--DPK------RNFLTMAIRPHGIFGpRDPQ-----LVPILIEAARKGKMKFMI-GNGENLVDFTFVENVVHGHIL 237
Cdd:PRK10675 161 TDLQkaQPDwsiallRYFNPVGAHPSGDMG-EDPQgipnnLMPYIAQVAVGRRDSLAIfGNDYPTEDGTGVRDYIHVMDL 239
                        250       260
                 ....*....|....*....|.
gi 928185501 238 AAEHLSQDTAVSGKA-FHITN 257
Cdd:PRK10675 240 ADGHVAAMEKLANKPgVHIYN 260
PLN02166 PLN02166
dTDP-glucose 4,6-dehydratase
27-242 9.01e-11

dTDP-glucose 4,6-dehydratase


Pssm-ID: 165812 [Multi-domain]  Cd Length: 436  Bit Score: 62.72  E-value: 9.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  27 KCTVIGGSGFLGQHMVEQLLARGYTVNVFD---------MRQGFDNPRVQFFLGDLCSqqdlyPALKGVSTVFH--C-AS 94
Cdd:PLN02166 122 RIVVTGGAGFVGSHLVDKLIGRGDEVIVIDnfftgrkenLVHLFGNPRFELIRHDVVE-----PILLEVDQIYHlaCpAS 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  95 PPPSSNNKELFYRVNYIGTKNVIETCKEAGVqKLILTSSASVIfegvnikngTEDLPYAMKPIdYYTETKILQERAVLDa 174
Cdd:PLN02166 197 PVHYKYNPVKTIKTNVMGTLNMLGLAKRVGA-RFLLTSTSEVY---------GDPLEHPQKET-YWGNVNPIGERSCYD- 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 175 nDPKRNFLTMAIRPH-------------GIFGPR----DPQLVPILI-EAARKGKMKfMIGNGENLVDFTFVENVVHG-- 234
Cdd:PLN02166 265 -EGKRTAETLAMDYHrgagvevriarifNTYGPRmcldDGRVVSNFVaQTIRKQPMT-VYGDGKQTRSFQYVSDLVDGlv 342

                 ....*...
gi 928185501 235 HILAAEHL 242
Cdd:PLN02166 343 ALMEGEHV 350
PLN02206 PLN02206
UDP-glucuronate decarboxylase
27-242 1.47e-10

UDP-glucuronate decarboxylase


Pssm-ID: 177856 [Multi-domain]  Cd Length: 442  Bit Score: 62.31  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  27 KCTVIGGSGFLGQHMVEQLLARGYTVNVFD---------MRQGFDNPRVQFFLGDLCSqqdlyPALKGVSTVFH--C-AS 94
Cdd:PLN02206 121 RVVVTGGAGFVGSHLVDRLMARGDSVIVVDnfftgrkenVMHHFSNPNFELIRHDVVE-----PILLEVDQIYHlaCpAS 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  95 PPPSSNNKELFYRVNYIGTKNVIETCKEAGVqKLILTSSASVIFEGVNIKNgTEDLPYAMKPIDY---YTETKILQERAV 171
Cdd:PLN02206 196 PVHYKFNPVKTIKTNVVGTLNMLGLAKRVGA-RFLLTSTSEVYGDPLQHPQ-VETYWGNVNPIGVrscYDEGKRTAETLT 273
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928185501 172 LDANDPKRNFLTMAiRPHGIFGPR----DPQLVPILI-EAARKGKMKfMIGNGENLVDFTFVENVVHG--HILAAEHL 242
Cdd:PLN02206 274 MDYHRGANVEVRIA-RIFNTYGPRmcidDGRVVSNFVaQALRKEPLT-VYGDGKQTRSFQFVSDLVEGlmRLMEGEHV 349
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
30-133 1.96e-10

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 60.71  E-value: 1.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARG-YTVNVFD------------MRQGFDNPRVQFFLGDLCSQQDLYPALK--GVSTVFHCAS 94
Cdd:cd05237    7 VTGGAGSIGSELVRQILKFGpKKLIVFDrdenklhelvreLRSRFPHDKLRFIIGDVRDKERLRRAFKerGPDIVFHAAA 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 928185501  95 ----PPPSSNNKELFyRVNYIGTKNVIETCKEAGVQKLILTSS 133
Cdd:cd05237   87 lkhvPSMEDNPEEAI-KTNVLGTKNVIDAAIENGVEKFVCIST 128
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
30-232 2.20e-10

dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4,6-dehydratase and related proteins, members of the extended-SDR family, with the characteristic Rossmann fold core region, active site tetrad and NAD(P)-binding motif. dTDP-D-glucose 4,6-dehydratase is closely related to other sugar epimerases of the SDR family. dTDP-D-dlucose 4,6,-dehydratase catalyzes the second of four steps in the dTDP-L-rhamnose pathway (the dehydration of dTDP-D-glucose to dTDP-4-keto-6-deoxy-D-glucose) in the synthesis of L-rhamnose, a cell wall component of some pathogenic bacteria. In many gram negative bacteria, L-rhamnose is an important constituent of lipopoylsaccharide O-antigen. The larger N-terminal portion of dTDP-D-Glucose 4,6-dehydratase forms a Rossmann fold NAD-binding domain, while the C-terminus binds the sugar substrate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187557 [Multi-domain]  Cd Length: 315  Bit Score: 61.03  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARG--YTVNVFD----------MRQGFDNPRVQFFLGDLCSQQDLYPALK--GVSTVFHCASP 95
Cdd:cd05246    5 VTGGAGFIGSNFVRYLLNKYpdYKIINLDkltyagnlenLEDVSSSPRYRFVKGDICDAELVDRLFEeeKIDAVIHFAAE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  96 ---PPSSNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKNGTEDLPYAmkPIDYYTETKILQERAVL 172
Cdd:cd05246   85 shvDRSISDPEPFIRTNVLGTYTLLEAARKYGVKRFVHISTDEVYGDLLDDGEFTETSPLA--PTSPYSASKAAADLLVR 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928185501 173 dandpkrnfltMAIRPHGI----------FGPR--DPQLVPILIEAARKGKMKFMIGNGENLVDFTFVENVV 232
Cdd:cd05246  163 -----------AYHRTYGLpvvitrcsnnYGPYqfPEKLIPLFILNALDGKPLPIYGDGLNVRDWLYVEDHA 223
FlaA1 COG1086
NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular ...
30-211 2.26e-10

NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular polysaccharide biosynthesis protein EpsC [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 224011 [Multi-domain]  Cd Length: 588  Bit Score: 61.90  E-value: 2.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTV---------NVFDM----RQGFDNPRVQFFLGDLCSQQDLYPALKG--VSTVFHCAS 94
Cdd:COG1086  255 VTGGGGSIGSELCRQILKFNPKEiilfsrdeyKLYLIdmelREKFPELKLRFYIGDVRDRDRVERAMEGhkVDIVFHAAA 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  95 ----PPPSSNNKELFyRVNYIGTKNVIETCKEAGVQKLILTSSASvifegvnikngtedlpyAMKPIDYYTETKILQERA 170
Cdd:COG1086  335 lkhvPLVEYNPEEAI-KTNVLGTENVAEAAIKNGVKKFVLISTDK-----------------AVNPTNVMGATKRLAEKL 396
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 928185501 171 VLDANDPKRNFLT--MAIRPHGIFGPRDpQLVPILIEAARKGK 211
Cdd:COG1086  397 FQAANRNVSGTGTrfCVVRFGNVLGSRG-SVIPLFKKQIAEGG 438
PLN02986 PLN02986
cinnamyl-alcohol dehydrogenase family protein
30-240 2.38e-10

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178567 [Multi-domain]  Cd Length: 322  Bit Score: 60.80  E-value: 2.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVfDMRQGFD-------------NPRVQFFLGDLCSQQDLYPALKGVSTVFHCASPP 96
Cdd:PLN02986  10 VTGASGYIASWIVKLLLLRGYTVKA-TVRDLTDrkktehllaldgaKERLKLFKADLLEESSFEQAIEGCDAVFHTASPV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  97 --PSSNNKELFYRVNYIGTKNVIETCKE-AGVQKLILTSS-ASVIFEGVNIK-NGTEDLPYAMKPI------DYYTETKI 165
Cdd:PLN02986  89 ffTVKDPQTELIDPALKGTINVLNTCKEtPSVKRVILTSStAAVLFRQPPIEaNDVVDETFFSDPSlcretkNWYPLSKI 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 166 LQERAVLDAndPKRNFLTMAI-RPHGIFGPrdpqlvpiLIEAARKGKMKFMIG--NGENLVD-----FTFVENVVHGHIL 237
Cdd:PLN02986 169 LAENAAWEF--AKDNGIDMVVlNPGFICGP--------LLQPTLNFSVELIVDfiNGKNLFNnrfyrFVDVRDVALAHIK 238

                 ...
gi 928185501 238 AAE 240
Cdd:PLN02986 239 ALE 241
PLN02583 PLN02583
cinnamoyl-CoA reductase
28-259 5.65e-10

cinnamoyl-CoA reductase


Pssm-ID: 178195 [Multi-domain]  Cd Length: 297  Bit Score: 59.73  E-value: 5.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  28 CTVIGGSGFLGQHMVEQLLARGYTVNVFDMRQG------------FDNPRVQFFLGDLCSQQDLYPALKGVSTVFHCASP 95
Cdd:PLN02583   9 VCVMDASGYVGFWLVKRLLSRGYTVHAAVQKNGeteiekeirglsCEEERLKVFDVDPLDYHSILDALKGCSGLFCCFDP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  96 PPSSNNK-ELFYRVNYIGTKNVIETCKEA-GVQKLILTSSAS-VIFEGVNIknGTE---------DLPYAMKPIDYYTET 163
Cdd:PLN02583  89 PSDYPSYdEKMVDVEVRAAHNVLEACAQTdTIEKVVFTSSLTaVIWRDDNI--STQkdvderswsDQNFCRKFKLWHALA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 164 KILQERAVLD-ANDPKRNFLtmAIRPHGIFGPRDPQLVPILIEAARkgkmkfMIGNGE-NLVDFTFVENVvhgHILAAEh 241
Cdd:PLN02583 167 KTLSEKTAWAlAMDRGVNMV--SINAGLLMGPSLTQHNPYLKGAAQ------MYENGVlVTVDVNFLVDA---HIRAFE- 234
                        250       260
                 ....*....|....*....|.
gi 928185501 242 lsqDTAVSGKAF---HITNDE 259
Cdd:PLN02583 235 ---DVSSYGRYLcfnHIVNTE 252
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
32-232 6.54e-10

Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.


Pssm-ID: 400380 [Multi-domain]  Cd Length: 257  Bit Score: 58.77  E-value: 6.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501   32 GGSGFLGQHMVEQLLARGYTVN--------------------------VFDMRQGFDNPRVQFFLGDLC------SQQDL 79
Cdd:pfam07993   3 GATGFLGKVLLEKLLRSTPDVKkiyllvrakdgesalerlrqelekypLFDALLKEALERIVPVAGDLSepnlglSEEDF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501   80 YPALKGVSTVFHCASP----PPSSNnkelFYRVNYIGTKNVIETCKEaGVQK--LILTSSA-------SVIFEGVNIKNG 146
Cdd:pfam07993  83 QRLAEEVDVIIHSAATvnfdEPYDD----ARAINVLGTREVLRLAKQ-GKQLkaFHHVSTAyvngereGLVEEKPYPEGE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  147 TEDLPYAMKPIDY------YTETKILQERAVLDANdpKRNFLTMAIRPhGI--------------FGPRdpqlvpILIEA 206
Cdd:pfam07993 158 DDMKLDEDEPALLgglpntYTQTKWLAEQLVREAA--RRGLPVVIYRP-SIitgepktgwinnfdFGPR------GLLGG 228
                         250       260
                  ....*....|....*....|....*.
gi 928185501  207 ARKGKMKFMIGNGENLVDFTFVENVV 232
Cdd:pfam07993 229 IGKGVLPSILGDPDAVLDLVPVDYVA 254
Polysacc_synt_2 pfam02719
Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide ...
30-133 2.17e-09

Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide biosynthesis proteins including the CapD protein, WalL protein, mannosyl-transferase, and several putative epimerases (e.g. WbiI).


Pssm-ID: 426938 [Multi-domain]  Cd Length: 284  Bit Score: 57.52  E-value: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501   30 VIGGSGFLGQHMVEQLLARG---------YTVNVFDMRQ----GFDNPRVQFF----LGDLCSQQDLYPALK--GVSTVF 90
Cdd:pfam02719   3 VTGGGGSIGSELCRQILKFNpkkiilfsrDELKLYEIRQelreKFNDPKLRFFivpvIGDVRDRERLERAMEqyGVDVVF 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 928185501   91 HCAS---PPPSSNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSS 133
Cdd:pfam02719  83 HAAAykhVPLVEYNPMEAIKTNVLGTENVADAAIEAGVKKFVLIST 128
PLN02214 PLN02214
cinnamoyl-CoA reductase
23-240 2.81e-09

cinnamoyl-CoA reductase


Pssm-ID: 177862 [Multi-domain]  Cd Length: 342  Bit Score: 57.84  E-value: 2.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  23 PNASKCTVIGGSGFLGQHMVEQLLARGYTVNvfDMRQGFDNP-------------RVQFFLGDLCSQQDLYPALKGVSTV 89
Cdd:PLN02214   8 PAGKTVCVTGAGGYIASWIVKILLERGYTVK--GTVRNPDDPknthlreleggkeRLILCKADLQDYEALKAAIDGCDGV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  90 FHCASPPPSSNNKELFYRVNyiGTKNVIETCKEAGVQKLILTSSASVIF-------EGVNIKNGTEDLPYAMKPIDYYTE 162
Cdd:PLN02214  86 FHTASPVTDDPEQMVEPAVN--GAKFVINAAAEAKVKRVVITSSIGAVYmdpnrdpEAVVDESCWSDLDFCKNTKNWYCY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 163 TKILQERAVLDANDPKRNFLTMaIRPHGIFGprdPQLVPIlIEAARKGKMKFMIGNGENLVDFTF----VENVVHGHILA 238
Cdd:PLN02214 164 GKMVAEQAAWETAKEKGVDLVV-LNPVLVLG---PPLQPT-INASLYHVLKYLTGSAKTYANLTQayvdVRDVALAHVLV 238

                 ..
gi 928185501 239 AE 240
Cdd:PLN02214 239 YE 240
PRK15181 PRK15181
Vi polysaccharide biosynthesis UDP-N-acetylglucosaminuronic acid C-4 epimerase TviC;
30-275 3.49e-09

Vi polysaccharide biosynthesis UDP-N-acetylglucosaminuronic acid C-4 epimerase TviC;


Pssm-ID: 185103 [Multi-domain]  Cd Length: 348  Bit Score: 57.41  E-value: 3.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLL------------ARGYTVNVFDMRQGFDN---PRVQFFLGDLCSQQDLYPALKGVSTVFHCA- 93
Cdd:PRK15181  20 ITGVAGFIGSGLLEELLflnqtvigldnfSTGYQHNLDDVRTSVSEeqwSRFIFIQGDIRKFTDCQKACKNVDYVLHQAa 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  94 --SPPPSSNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKNGTEDLPyamKPIDYYTETKILQERAV 171
Cdd:PRK15181 100 lgSVPRSLKDPIATNSANIDGFLNMLTAARDAHVSSFTYAASSSTYGDHPDLPKIEERIG---RPLSPYAVTKYVNELYA 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 172 lDANDPKRNFLTMAIRPHGIFGPR-DPQ-----LVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHGHILAAEhlSQD 245
Cdd:PRK15181 177 -DVFARSYEFNAIGLRYFNVFGRRqNPNgaysaVIPRWILSLLKDEPIYINGDGSTSRDFCYIENVIQANLLSAT--TND 253
                        250       260       270
                 ....*....|....*....|....*....|
gi 928185501 246 TAVSGKAFHITNDEPIPFWTFLSRILTGLN 275
Cdd:PRK15181 254 LASKNKVYNVAVGDRTSLNELYYLIRDGLN 283
GDP_FS_SDR_e cd05239
GDP-fucose synthetase, extended (e) SDRs; GDP-fucose synthetase (aka 3, ...
30-249 5.75e-09

GDP-fucose synthetase, extended (e) SDRs; GDP-fucose synthetase (aka 3, 5-epimerase-4-reductase) acts in the NADP-dependent synthesis of GDP-fucose from GDP-mannose. Two activities have been proposed for the same active site: epimerization and reduction. Proteins in this subgroup are extended SDRs, which have a characteristic active site tetrad and an NADP-binding motif, [AT]GXXGXXG, that is a close match to the archetypical form. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187550 [Multi-domain]  Cd Length: 300  Bit Score: 56.44  E-value: 5.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFDMRQGFdnprvqfflgDLCSQQDLYPALKGVS--TVFHCAS----PPPSSNNKE 103
Cdd:cd05239    4 VTGHRGLVGSAIVRVLARRGYENVVFRTSKEL----------DLTDQEAVRAFFEKEKpdYVIHLAAkvggIVANMTYPA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 104 LFYRVNYIGTKNVIETCKEAGVQKLILTSSaSVIFEgvnikngtedlPYAMKPIDyytETKILQE-------------RA 170
Cdd:cd05239   74 DFLRDNLLINDNVIHAAHRFGVKKLVFLGS-SCIYP-----------DLAPQPID---ESDLLTGppeptnegyaiakRA 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 171 VLDAND-----PKRNFLTMAirPHGIFGPRD---PQ---LVPILI----EAARKGKMKFMI-GNGENLVDFTFVENVVHG 234
Cdd:cd05239  139 GLKLCEayrkqYGCDYISVM--PTNLYGPHDnfdPEnshVIPALIrkfhEAKLRGGKEVTVwGSGTPRREFLYSDDLARA 216
                        250
                 ....*....|....*
gi 928185501 235 HILAAEHLSQDTAVS 249
Cdd:cd05239  217 IVFLLENYDEPIIVN 231
SDR_a7 cd05262
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ...
30-263 9.28e-09

atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187572 [Multi-domain]  Cd Length: 291  Bit Score: 55.82  E-value: 9.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVnVFDMR-----QGFDNPRVQFFLGDLcsqQDLYPALKGVST---VFHCA---SPPPS 98
Cdd:cd05262    5 VTGATGFIGSAVVRELVAAGHEV-VGLARsdagaAKLEAAGAQVHRGDL---EDLDILRKAAAEadaVIHLAfthDFDNF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  99 SNNKELfyrvnyigTKNVIETCKEAGV---QKLILTSSASVIFEGVNIKNGTEDLPYAMKPIdyyteTKILQERAVLDAN 175
Cdd:cd05262   81 AQACEV--------DRRAIEALGEALRgtgKPLIYTSGIWLLGPTGGQEEDEEAPDDPPTPA-----ARAVSEAAALELA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 176 DPKRNFLTMaIRPHGIFGPRDPQLVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHGHILAAEHlsqdtAVSGKAFHI 255
Cdd:cd05262  148 ERGVRASVV-RLPPVVHGRGDHGFVPMLIAIAREKGVSAYVGDGKNRWPAVHRDDAARLYRLALEK-----GKAGSVYHA 221

                 ....*...
gi 928185501 256 TNDEPIPF 263
Cdd:cd05262  222 VAEEGIPV 229
PCBER_SDR_a cd05259
phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and ...
30-258 1.36e-08

phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and pinoresinol-lariciresinol reductases are NADPH-dependent aromatic alcohol reductases, and are atypical members of the SDR family. Other proteins in this subgroup are identified as eugenol synthase. These proteins contain an N-terminus characteristic of NAD(P)-binding proteins and a small C-terminal domain presumed to be involved in substrate binding, but they do not have the conserved active site Tyr residue typically found in SDRs. Numerous other members have unknown functions. The glycine rich NADP-binding motif in this subgroup is of 2 forms: GXGXXG and G[GA]XGXXG; it tends to be atypical compared with the forms generally seen in classical or extended SDRs. The usual SDR active site tetrad is not present, but a critical active site Lys at the usual SDR position has been identified in various members, though other charged and polar residues are found at this position in this subgroup. Atypical SDR-related proteins retain the Rossmann fold of the SDRs, but have limited sequence identity and generally lack the catalytic properties of the archetypical members. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187569 [Multi-domain]  Cd Length: 282  Bit Score: 55.39  E-value: 1.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLAR-GYTVNVFdMRQG------FDNPRVQFFLGDLCSQQDLYPALKGVSTVFHCASPPPssnnk 102
Cdd:cd05259    4 IAGATGTLGGPIVSALLASpGFTVTVL-TRPSstssneFQPSGVKVVPVDYASHESLVAALKGVDAVISALGGAA----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 103 elfyrvnyIGT-KNVIETCKEAGVQKLILtSSASVIFEGVNiKNGTEDLPYAMKPIDYYTETKILQERAVLDANDPkrnF 181
Cdd:cd05259   78 --------IGDqLKLIDAAIAAGVKRFIP-SEFGVDYDRIG-ALPLLDLFDEKRDVRRYLRAKNAGLPWTYVSTGM---F 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928185501 182 LTMAIRPHgiFGPRDPqlvpilieAARkgkmKFMI-GNGENLVDFTFVENVvhGHiLAAEHLSQDTAVSGKAFHITND 258
Cdd:cd05259  145 LDYLLEPL--FGVVDL--------ANR----TATIyGDGETKFAFTTLEDI--GR-AVARALTHPDRTLNRVVFVAGD 205
PLN02650 PLN02650
dihydroflavonol-4-reductase
30-134 1.49e-08

dihydroflavonol-4-reductase


Pssm-ID: 178256 [Multi-domain]  Cd Length: 351  Bit Score: 55.60  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTV--------NVFDMRQGFDNP----RVQFFLGDLCSQQDLYPALKGVSTVFHCASP-- 95
Cdd:PLN02650  10 VTGASGFIGSWLVMRLLERGYTVratvrdpaNVKKVKHLLDLPgattRLTLWKADLAVEGSFDDAIRGCTGVFHVATPmd 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 928185501  96 --PPSSNNKELFYRVNyiGTKNVIETCKEAG-VQKLILTSSA 134
Cdd:PLN02650  90 feSKDPENEVIKPTVN--GMLSIMKACAKAKtVRRIVFTSSA 129
SDR_e1 cd05235
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ...
32-261 2.01e-08

extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins identified as putative polyketide sythases fatty acid synthases (FAS), and nonribosomal peptide synthases, among others. However, unlike the usual ketoreductase modules of FAS and polyketide synthase, these domains are related to the extended SDRs, and have canonical NAD(P)-binding motifs and an active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187546 [Multi-domain]  Cd Length: 290  Bit Score: 54.96  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  32 GGSGFLGQHMVEQLLARGYTVNVF------------------------DMRQGFDNPRVQFFLGDLcSQ------QDLYP 81
Cdd:cd05235    6 GATGFLGAYLLRELLKRKNVSKIYclvrakdeeaalerlidnlkeyglNLWDELELSRIKVVVGDL-SKpnlglsDDDYQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  82 AL-KGVSTVFHCASpppssnNKELFY------RVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVNIKNGTEDLPYAM 154
Cdd:cd05235   85 ELaEEVDVIIHNGA------NVNWVYpyeelkPANVLGTKELLKLAATGKLKPLHFVSTLSVFSAEEYNALDDEESDDML 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 155 KPIDY----YTETKILQERAVLDANDpkRNFLTMAIRPHGIFGprDPQLVPI-----LIEAARKGKMKFMIGNGENLVDF 225
Cdd:cd05235  159 ESQNGlpngYIQSKWVAEKLLREAAN--RGLPVAIIRPGNIFG--DSETGIGntddfFWRLLKGCLQLGIYPISGAPLDL 234
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 928185501 226 TFVENVVHGHILAAEHLSQDTAVsgkaFHITNDEPI 261
Cdd:cd05235  235 SPVDWVARAIVKLALNESNEFSI----YHLLNPPLI 266
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
30-211 2.69e-08

dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224016 [Multi-domain]  Cd Length: 281  Bit Score: 54.22  E-value: 2.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQL--------LARGyTVNVFDmrqgFDNPRvQFFLGDLCSqqdlypalkgvsTVFHCA---SPPPS 98
Cdd:COG1091    5 ITGANGQLGTELRRALpgefeviaTDRA-ELDITD----PDAVL-EVIRETRPD------------VVINAAaytAVDKA 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  99 SNNKELFYRVNYIGTKNVIETCKEAGVqKLILTSSASViFEGVNIKNGTEDLPYAmkPIDYYTETKILQERAVLDANDpk 178
Cdd:COG1091   67 ESEPELAFAVNATGAENLARAAAEVGA-RLVHISTDYV-FDGEKGGPYKETDTPN--PLNVYGRSKLAGEEAVRAAGP-- 140
                        170       180       190
                 ....*....|....*....|....*....|...
gi 928185501 179 rNFLTmaIRPHGIFGPRDPQLVPILIEAARKGK 211
Cdd:COG1091  141 -RHLI--LRTSWVYGEYGNNFVKTMLRLAKEGK 170
PLN02896 PLN02896
cinnamyl-alcohol dehydrogenase
30-137 3.01e-08

cinnamyl-alcohol dehydrogenase


Pssm-ID: 178484 [Multi-domain]  Cd Length: 353  Bit Score: 54.83  E-value: 3.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVN--VFDMRQGFD-------NPRVQFFLGDLCSQQDLYPALKGVSTVFHCASP----- 95
Cdd:PLN02896  15 VTGATGYIGSWLVKLLLQRGYTVHatLRDPAKSLHllskwkeGDRLRLFRADLQEEGSFDEAVKGCDGVFHVAASmefdv 94
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 928185501  96 PPSSNNKELFYRVNYI-----GTKNVIETCKEAG-VQKLILTSSASVI 137
Cdd:PLN02896  95 SSDHNNIEEYVQSKVIdpaikGTLNVLKSCLKSKtVKRVVFTSSISTL 142
PLN00141 PLN00141
Tic62-NAD(P)-related group II protein; Provisional
30-136 3.23e-08

Tic62-NAD(P)-related group II protein; Provisional


Pssm-ID: 215072 [Multi-domain]  Cd Length: 251  Bit Score: 53.71  E-value: 3.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTV-----NVFDMRQGF-DNPRVQFFLGDLCSQQD-LYPALKGVSTVFHCASPPPSSNNK 102
Cdd:PLN00141  22 VAGATGRTGKRIVEQLLAKGFAVkagvrDVDKAKTSLpQDPSLQIVRADVTEGSDkLVEAIGDDSDAVICATGFRRSFDP 101
                         90       100       110
                 ....*....|....*....|....*....|....
gi 928185501 103 ELFYRVNYIGTKNVIETCKEAGVQKLILTSSASV 136
Cdd:PLN00141 102 FAPWKVDNFGTVNLVEACRKAGVTRFILVSSILV 135
UGD_SDR_e cd05230
UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the ...
30-136 3.52e-08

UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the formation of UDP-xylose from UDP-glucuronate; it is an extended-SDR, and has the characteristic glycine-rich NAD-binding pattern, TGXXGXXG, and active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187541 [Multi-domain]  Cd Length: 305  Bit Score: 54.18  E-value: 3.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFD---------MRQGFDNPRVQFFLGDLcsqqdLYPALKGVSTVFHCASP--PPs 98
Cdd:cd05230    5 ITGGAGFLGSHLCDRLLEDGHEVICVDnfftgrkrnIEHLIGHPNFEFIRHDV-----TEPLYLEVDQIYHLACPasPV- 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 928185501  99 snnkelFY--------RVNYIGTKNVIETCKEAGVqKLILTSSASV 136
Cdd:cd05230   79 ------HYqynpiktlKTNVLGTLNMLGLAKRVGA-RVLLASTSEV 117
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
30-198 3.71e-08

Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; Nucleoside-diphosphate-sugar 4-epimerase has the characteristic active site tetrad and NAD-binding motif of the extended SDR, and is related to more specifically defined epimerases such as UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), which catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup includes Escherichia coli 055:H7 Gne, a UDP-GlcNAc 4-epimerase, essential for O55 antigen synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187549 [Multi-domain]  Cd Length: 305  Bit Score: 54.31  E-value: 3.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARG--YTVNVFDMRQGFD---NPRVQFFLGDLCSQQDLYPALKGVS-TVFHCA---SPPPSSN 100
Cdd:cd05238    5 ITGASGFVGQRLAERLLSDVpnERLILIDVVSPKApsgAPRVTQIAGDLAVPALIEALANGRPdVVFHLAaivSGGAEAD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 101 NkELFYRVNYIGTKNVIETCKEAG-VQKLILTSSASVIfeGVNIKNGTEDLPyAMKPIDYYTETKILQEraVLDANDPKR 179
Cdd:cd05238   85 F-DLGYRVNVDGTRNLLEALRKNGpKPRFVFTSSLAVY--GLPLPNPVTDHT-ALDPASSYGAQKAMCE--LLLNDYSRR 158
                        170       180
                 ....*....|....*....|
gi 928185501 180 NFL-TMAIRPHGIFgPRDPQ 198
Cdd:cd05238  159 GFVdGRTLRLPTVC-VRPGR 177
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
30-175 4.47e-08

RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesized by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide.


Pssm-ID: 427865 [Multi-domain]  Cd Length: 284  Bit Score: 53.82  E-value: 4.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501   30 VIGGSGFLGQHMVEQLLARGYTVnvfdmrQGFDNPRVQffLGDLCSQQDLYPALKGvSTVFHCAS---PPPSSNNKELFY 106
Cdd:pfam04321   3 ITGANGQLGTELRRLLAERGIEV------VALTRAELD--LTDPEAVARLLREIKP-DVVVNAAAytaVDKAESEPDLAY 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928185501  107 RVNYIGTKNVIETCKEAGVqKLILTSSASViFEgvniknGTEDLPYAMK----PIDYYTETKILQERAVLDAN 175
Cdd:pfam04321  74 AINALAPANLAEACAAVGA-PLIHISTDYV-FD------GTKPRPYEEDdetnPLNVYGRTKLAGEQAVRAAG 138
NmrA_like_SDR_a cd05251
NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) ...
29-136 5.97e-08

NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) SDRs; NmrA and HSCARG like proteins. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187561 [Multi-domain]  Cd Length: 242  Bit Score: 53.05  E-value: 5.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  29 TVIGGSGFLGQHMVEQLLAR-GYTVNVF------DMRQGFDNPRVQFFLGDLCSQQDLYPALKGVSTVFHCASPPPSSNN 101
Cdd:cd05251    2 LVFGATGKQGGSVVRALLKDpGFKVRALtrdpssPAAKALAAPGVEVVQGDLDDPESLEAALKGVYGVFLVTDFWEAGGE 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 928185501 102 KELFyrvnyIGtKNVIETCKEAGVQKLILTSSASV 136
Cdd:cd05251   82 DEIA-----QG-KNVVDAAKRAGVQHFVFSSVPDV 110
TMR_SDR_a cd05269
triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an ...
30-134 1.70e-07

triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187578 [Multi-domain]  Cd Length: 272  Bit Score: 51.89  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARG----YTVNVFDMRQGFDNPRVQFFLGDLCSQQDLYPALKGVSTVFhCASPPPSSNNKELF 105
Cdd:cd05269    3 VTGATGKLGTAVVELLLAKVasvvALVRNPEKAKAFAADGVEVRQGDYDDPETLERAFEGVDRLL-LISPSDLEDRIQQH 81
                         90       100
                 ....*....|....*....|....*....
gi 928185501 106 yrvnyigtKNVIETCKEAGVQKLILTSSA 134
Cdd:cd05269   82 --------KNFIDAAKQAGVKHIVYLSAS 102
PLN02989 PLN02989
cinnamyl-alcohol dehydrogenase family protein
30-138 2.91e-07

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178569 [Multi-domain]  Cd Length: 325  Bit Score: 51.57  E-value: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVF----DMRQGFDN--------PRVQFFLGDLCSQQDLYPALKGVSTVFHCASP-- 95
Cdd:PLN02989  10 VTGASGYIASWIVKLLLFRGYTINATvrdpKDRKKTDHllaldgakERLKLFKADLLDEGSFELAIDGCETVFHTASPva 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 928185501  96 -PPSSNNKELFYRVNYIGTKNVIETC-KEAGVQKLILTSSASVIF 138
Cdd:PLN02989  90 iTVKTDPQVELINPAVNGTINVLRTCtKVSSVKRVILTSSMAAVL 134
PLN02725 PLN02725
GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase
30-249 8.60e-07

GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase


Pssm-ID: 178326 [Multi-domain]  Cd Length: 306  Bit Score: 50.08  E-value: 8.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFDMRQGfdnprvqfflGDLCSQQDlypalkgVSTVFHCASPP------------- 96
Cdd:PLN02725   2 VAGHRGLVGSAIVRKLEALGFTNLVLRTHKE----------LDLTRQAD-------VEAFFAKEKPTyvilaaakvggih 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  97 PSSNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSaSVIFEgvniKNGTEDLPYAM---KPIDYYTETKILQERAVLD 173
Cdd:PLN02725  65 ANMTYPADFIRENLQIQTNVIDAAYRHGVKKLLFLGS-SCIYP----KFAPQPIPETAlltGPPEPTNEWYAIAKIAGIK 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 174 ANDPKR---NFLTMAIRPHGIFGPRDP------QLVPILI----EAARKGKmKFMI--GNGENLVDFTFVENVVHGHILA 238
Cdd:PLN02725 140 MCQAYRiqyGWDAISGMPTNLYGPHDNfhpensHVIPALIrrfhEAKANGA-PEVVvwGSGSPLREFLHVDDLADAVVFL 218
                        250
                 ....*....|.
gi 928185501 239 AEHLSQDTAVS 249
Cdd:PLN02725 219 MRRYSGAEHVN 229
PLN02695 PLN02695
GDP-D-mannose-3',5'-epimerase
27-284 1.92e-06

GDP-D-mannose-3',5'-epimerase


Pssm-ID: 178298 [Multi-domain]  Cd Length: 370  Bit Score: 49.04  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  27 KCTVIGGSGFLGQHMVEQLLARGYTVNVFDMRQGFDNPRV----QFFLGDLCSQQDLYPALKGVSTVFHCASPPP----- 97
Cdd:PLN02695  23 RICITGAGGFIASHIARRLKAEGHYIIASDWKKNEHMSEDmfchEFHLVDLRVMENCLKVTKGVDHVFNLAADMGgmgfi 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  98 SSNNKELFYRvNYIGTKNVIETCKEAGVQKLILTSSASVIFEG------VNIKngtEDLPYAMKPIDYYTETKILQERAV 171
Cdd:PLN02695 103 QSNHSVIMYN-NTMISFNMLEAARINGVKRFFYASSACIYPEFkqletnVSLK---ESDAWPAEPQDAYGLEKLATEELC 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 172 LDANdpkRNF-LTMAI-RPHGIFGP-------RDPQLVPILIEAARKGKMKFMIGNGENLVDFTFVENVVHGhILAAEHL 242
Cdd:PLN02695 179 KHYT---KDFgIECRIgRFHNIYGPfgtwkggREKAPAAFCRKALTSTDEFEMWGDGKQTRSFTFIDECVEG-VLRLTKS 254
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 928185501 243 SQDTAVSgkafhITNDEPIPFWTFLSRILTGLNYEAPKYHIP 284
Cdd:PLN02695 255 DFREPVN-----IGSDEMVSMNEMAEIALSFENKKLPIKHIP 291
ADP_GME_SDR_e cd05248
ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ...
30-241 2.01e-06

ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ADP-L-glycero-D-mannoheptose 6-epimerase, an extended SDR, which catalyzes the NAD-dependent interconversion of ADP-D-glycero-D-mannoheptose and ADP-L-glycero-D-mannoheptose. This subgroup has the canonical active site tetrad and NAD(P)-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187559 [Multi-domain]  Cd Length: 317  Bit Score: 48.84  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYT--VNVFDMRQG--FDNPRVQFFlGDLCSQQDLYPALKG------VSTVFH---CASpp 96
Cdd:cd05248    4 VTGGAGFIGSNLVKALNERGITdiLVVDNLSNGekFKNLVGLKI-ADYIDKDDFKDWVRKgdenfkIEAIFHqgaCSD-- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  97 PSSNNKELFYRVNYIGTKNVIETCKEAGVqKLILTSSASVIFEGVNIKNgTEDLPYAMKPIDYYTETKILQERAVLDaND 176
Cdd:cd05248   81 TTETDGKYMMDNNYQYTKELLHYCLEKKI-RFIYASSAAVYGNGSLGFA-EDIETPNLRPLNVYGYSKLLFDQWARR-HG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 177 PKRNFLTMAIRPHGIFGPRDpqlvpilieaARKGKMKFMI----------------------GNGENLVDFTFVENVVHG 234
Cdd:cd05248  158 KEVLSQVVGLRYFNVYGPRE----------YHKGRMASVVfhlfnqikagekvklfkssdgyADGEQLRDFVYVKDVVKV 227

                 ....*..
gi 928185501 235 HILAAEH 241
Cdd:cd05248  228 NLFFLEN 234
ycf39 CHL00194
Ycf39; Provisional
30-132 9.33e-06

Ycf39; Provisional


Pssm-ID: 177093  Cd Length: 317  Bit Score: 46.92  E-value: 9.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFdMRqgfdNPRVQFFL---------GDLCSQQDLYPALKGVSTVFHCASPPPSSN 100
Cdd:CHL00194   5 VIGATGTLGRQIVRQALDEGYQVRCL-VR----NLRKASFLkewgaelvyGDLSLPETLPPSFKGVTAIIDASTSRPSDL 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 928185501 101 NKelFYRVNYIGTKNVIETCKEAGVQKLILTS 132
Cdd:CHL00194  80 YN--AKQIDWDGKLALIEAAKAAKIKRFIFFS 109
NmrA pfam05368
NmrA-like family; NmrA is a negative transcriptional regulator involved in the ...
29-132 3.00e-05

NmrA-like family; NmrA is a negative transcriptional regulator involved in the post-translational modification of the transcription factor AreA. NmrA is part of a system controlling nitrogen metabolite repression in fungi. This family only contains a few sequences as iteration results in significant matches to other Rossmann fold families.


Pssm-ID: 398829 [Multi-domain]  Cd Length: 236  Bit Score: 44.64  E-value: 3.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501   29 TVIGGSGFLGQHMVEQLLARGYTVNVF------DMRQGFDNPRVQFFLGDLCSQQDLYPALKGVSTVFhCASPPPSSNNK 102
Cdd:pfam05368   2 LVFGATGQQGGSVVRASLKAGHKVRALvrdpksELAKSLKEAGVELVKGDLDDKESLVEALKGVDVVF-SVTGFWAGKEI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 928185501  103 ElfyrvnyIGtKNVIETCKEAGVQKLILTS 132
Cdd:pfam05368  81 E-------DG-KKLADAAKEAGVKHFIPSS 102
WbmH_like_SDR_e cd08957
Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella ...
27-129 3.22e-05

Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella bronchiseptica enzymes WbmH and WbmG, and related proteins. This subgroup exhibits the active site tetrad and NAD-binding motif of the extended SDR family. It has been proposed that the active site in Bordetella WbmG and WbmH cannot function as an epimerase, and that it plays a role in O-antigen synthesis pathway from UDP-2,3-diacetamido-2,3-dideoxy-l-galacturonic acid. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187660 [Multi-domain]  Cd Length: 307  Bit Score: 45.19  E-value: 3.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  27 KCTVIGGSGFLGQHMVEQLLARGYTVNVFD-----MRQGF-DNPRVQFFLGDLCSQ-------QDLYPalkgvSTVFHCA 93
Cdd:cd08957    2 KVLITGGAGQIGSHLIEHLLERGHQVVVIDnfatgRREHLpDHPNLTVVEGSIADKalvdklfGDFKP-----DAVVHTA 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 928185501  94 SPPPSSNNKELFYRVNYIGTKNVIETCKEAGVQKLI 129
Cdd:cd08957   77 AAYKDPDDWYEDTLTNVVGGANVVQAAKKAGVKRLI 112
SDR_a2 cd05245
atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified ...
28-133 3.64e-05

atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified as Escherichia coli protein ybjT, function unknown. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that generally matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187556 [Multi-domain]  Cd Length: 293  Bit Score: 45.03  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  28 CTVIGGSGFLGQHMVEQLLARGYTV-----NVFDMRQGFDNPRVQFFLGDLCSQQDLYPALKGVSTVFHCASpppSSNNK 102
Cdd:cd05245    1 VLVTGATGYVGGRLVPRLLQEGHQVralvrSPEKLADRPWSERVTVVRGDLEDPESLRAALEGIDTAYYLVH---SMGSG 77
                         90       100       110
                 ....*....|....*....|....*....|.
gi 928185501 103 ELFYRVNYIGTKNVIETCKEAGVQKLILTSS 133
Cdd:cd05245   78 GDFEEADRRAARNFARAARAAGVKRIIYLGG 108
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
32-263 7.00e-05

Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 225857 [Multi-domain]  Cd Length: 382  Bit Score: 44.31  E-value: 7.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  32 GGSGFLGQHMVEQLLARGY---------------------TVNVFDMRQGFDNPRVQFFLGDLcSQQDL------YPALK 84
Cdd:COG3320    7 GATGFLGAYLLLELLDRSDakviclvraqsdeaalarlekTFDLYRHWDELSADRVEVVAGDL-AEPDLglsertWQELA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  85 G-VSTVFHCAS-----PPPSsnnkELFyRVNYIGTKNVIETCKEAGVQKLILTSSASViFEGVNIKNGTEDL-------- 150
Cdd:COG3320   86 EnVDLIIHNAAlvnhvFPYS----ELR-GANVLGTAEVLRLAATGKPKPLHYVSSISV-GETEYYSNFTVDFdeisptrn 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501 151 ---PYAMKpidyYTETKILQERAVLDANDpkRNFLTMAIRPHGIFGP-RDPQLvpilieAARKGKMKFMIG--------N 218
Cdd:COG3320  160 vgqGLAGG----YGRSKWVAEKLVREAGD--RGLPVTIFRPGYITGDsRTGAL------NTRDFLTRLVLGllqlgiapD 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 928185501 219 GENLVDFTFVENVVHGHILAAEHLSQDTAV----SGKAFHITNDEPIPF 263
Cdd:COG3320  228 SEYSLDMLPVDHVARAVVAPSVQVAEAIAAlgahSDIRFNQLHMLTHPD 276
PLN02657 PLN02657
3,8-divinyl protochlorophyllide a 8-vinyl reductase
30-220 1.34e-04

3,8-divinyl protochlorophyllide a 8-vinyl reductase


Pssm-ID: 178263 [Multi-domain]  Cd Length: 390  Bit Score: 43.60  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVF--------------DMRQGFDNPRVQFflGDLCS----QQDLYPALKGVSTVFH 91
Cdd:PLN02657  65 VVGATGYIGKFVVRELVRRGYNVVAVareksgirgkngkeDTKKELPGAEVVF--GDVTDadslRKVLFSEGDPVDVVVS 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  92 C-ASPppsSNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVifegvnikngtedlpyaMKPIDYYTETKiLQERA 170
Cdd:PLN02657 143 ClASR---TGGVKDSWKIDYQATKNSLDAGREVGAKHFVLLSAICV-----------------QKPLLEFQRAK-LKFEA 201
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 928185501 171 VLDANDPkrNFLTMAIRPHGIFGPRDPQlvpilIEAARKGKMKFMIGNGE 220
Cdd:PLN02657 202 ELQALDS--DFTYSIVRPTAFFKSLGGQ-----VEIVKDGGPYVMFGDGK 244
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
30-140 1.60e-04

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: 42.66  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFDMR--QGFDN----PRVQFFLGDLCSQQDLYPALK-------GVSTVFHCASPP 96
Cdd:cd05371    7 VTGGASGLGLATVERLLAQGAKVVILDLPnsPGETVaklgDNCRFVPVDVTSEKDVKAALAlakakfgRLDIVVNCAGIA 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 928185501  97 PSS---NNK-------ELFYR---VNYIGTKNVI--------ETCKEAGVQKLILTSSASVI-FEG 140
Cdd:cd05371   87 VAAktyNKKgqqphslELFQRvinVNLIGTFNVIrlaagamgKNEPDQGGERGVIINTASVAaFEG 152
PRK05865 PRK05865
sugar epimerase family protein;
27-133 1.89e-04

sugar epimerase family protein;


Pssm-ID: 235630 [Multi-domain]  Cd Length: 854  Bit Score: 43.49  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  27 KCTVIGGSGFLGQHMVEQLLARGYTVNVFDMRQGFDNP-RVQFFLGDLCSQQDLYPALKGVSTVFHCA-SPPPSSnnkel 104
Cdd:PRK05865   2 RIAVTGASGVLGRGLTARLLSQGHEVVGIARHRPDSWPsSADFIAADIRDATAVESAMTGADVVAHCAwVRGRND----- 76
                         90       100
                 ....*....|....*....|....*....
gi 928185501 105 fyRVNYIGTKNVIETCKEAGVQKLILTSS 133
Cdd:PRK05865  77 --HINIDGTANVLKAMAETGTGRIVFTSS 103
CC3_like_SDR_a cd05250
CC3(TIP30)-like, atypical (a) SDRs; Atypical SDRs in this subgroup include CC3 (also known as ...
27-134 3.55e-04

CC3(TIP30)-like, atypical (a) SDRs; Atypical SDRs in this subgroup include CC3 (also known as TIP30) which is implicated in tumor suppression. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine rich NAD(P)-binding motif that resembles the extended SDRs, and have an active site triad of the SDRs (YXXXK and upstream Ser), although the upstream Asn of the usual SDR active site is substituted with Asp. For CC3, the Tyr of the triad is displaced compared to the usual SDRs and the protein is monomeric, both these observations suggest that the usual SDR catalytic activity is not present. NADP appears to serve an important role as a ligand, and may be important in the interaction with other macromolecules. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187560 [Multi-domain]  Cd Length: 214  Bit Score: 41.13  E-value: 3.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  27 KCTVIGGSGFLGQHMVEQLLARGY--TVNVFDMRQG---FDNPRVQFFLGDLCSQQDLYPALKGVSTVFHC-ASPPPSSN 100
Cdd:cd05250    2 TALVLGATGLVGKHLLRELLKSPYysKVTAIVRRKLtfpEAKEKLVQIVVDFERLDEYLEAFQNPDVGFCClGTTRKKAG 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 928185501 101 NKELFYRVNYIGTKNVIETCKEAGVQKLILTSSA 134
Cdd:cd05250   82 SQENFRKVDHDYVLKLAKLAKAAGVQHFLLVSSL 115
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
30-86 5.88e-04

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 41.15  E-value: 5.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVFDMRQG-FDNPRVQFFLGDLCSQQDLYPALKGV 86
Cdd:PRK06171  14 VTGGSSGIGLAIVKELLANGANVVNADIHGGdGQHENYQFVPTDVSSAEEVNHTVAEI 71
PLN02686 PLN02686
cinnamoyl-CoA reductase
30-133 1.49e-03

cinnamoyl-CoA reductase


Pssm-ID: 215370  Cd Length: 367  Bit Score: 40.15  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVF-----------------DMRQGFDNprVQFFLGDLCSQQDLYPALKGVSTVFHC 92
Cdd:PLN02686  58 VTGGVSFLGLAIVDRLLRHGYSVRIAvdtqedkeklrememfgEMGRSNDG--IWTVMANLTEPESLHEAFDGCAGVFHT 135
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 928185501  93 AS---PPPSSNNKELFYRVNYIGTKNVIETC-KEAGVQKLILTSS 133
Cdd:PLN02686 136 SAfvdPAGLSGYTKSMAELEAKASENVIEACvRTESVRKCVFTSS 180
PLN02260 PLN02260
probable rhamnose biosynthetic enzyme
30-231 2.17e-03

probable rhamnose biosynthetic enzyme


Pssm-ID: 215146 [Multi-domain]  Cd Length: 668  Bit Score: 40.11  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLAR--GYTVNVFD----------MRQGFDNPRVQFFLGDLCSQqDLYPAL---KGVSTVFHCAS 94
Cdd:PLN02260  11 ITGAAGFIASHVANRLIRNypDYKIVVLDkldycsnlknLNPSKSSPNFKFVKGDIASA-DLVNYLlitEGIDTIMHFAA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  95 PPPSSN---NKELFYRVNYIGTKNVIETCKEAG-VQKLILTSSASVIFEGvnikngTEDLPYA------MKPIDYYTETK 164
Cdd:PLN02260  90 QTHVDNsfgNSFEFTKNNIYGTHVLLEACKVTGqIRRFIHVSTDEVYGET------DEDADVGnheasqLLPTNPYSATK 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928185501 165 ILQERAVLdANDPKRNFLTMAIRPHGIFGPRD-PQ-LVPILIEAARKGKMKFMIGNGENLVDFTFVENV 231
Cdd:PLN02260 164 AGAEMLVM-AYGRSYGLPVITTRGNNVYGPNQfPEkLIPKFILLAMQGKPLPIHGDGSNVRSYLYCEDV 231
RfbB COG1088
dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];
30-229 4.64e-03

dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224013 [Multi-domain]  Cd Length: 340  Bit Score: 38.36  E-value: 4.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARG------------YTVNVFDMRQGFDNPRVQFFLGDLCSQQDLYPALKG--VSTVFHCASP 95
Cdd:COG1088    5 VTGGAGFIGSNFVRYILNKHpddhvvnldkltYAGNLENLADVEDSPRYRFVQGDICDRELVDRLFKEyqPDAVVHFAAE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  96 P---PSSNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIF--EGVNIKNGTEDLPYAmkPIDYYTETKilqerA 170
Cdd:COG1088   85 ShvdRSIDGPAPFIQTNVVGTYTLLEAARKYWGKFRFHHISTDEVYgdLGLDDDAFTETTPYN--PSSPYSASK-----A 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928185501 171 VLDandpkrnFLTMA-IRPHGI----------FGPR-DPQ-LVPILIEAARKGKMKFMIGNGENLVDFTFVE 229
Cdd:COG1088  158 ASD-------LLVRAyVRTYGLpatitrcsnnYGPYqFPEkLIPLMIINALLGKPLPVYGDGLQIRDWLYVE 222
NmrA_TMR_like_1_SDR_a cd05231
NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, ...
30-140 5.03e-03

NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, subgroup 1, atypical (a) SDRs; Atypical SDRs related to NMRa, TMR, and HSCARG (an NADPH sensor). This subgroup resembles the SDRs and has a partially conserved characteristic [ST]GXXGXXG NAD-binding motif, but lacks the conserved active site residues. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187542 [Multi-domain]  Cd Length: 259  Bit Score: 38.08  E-value: 5.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928185501  30 VIGGSGFLGQHMVEQLLARGYTVNVF---DMRQGFDNPR-VQFFLGDLCSQQDLYPALKGVSTVFHCasPPPSSNNKELF 105
Cdd:cd05231    3 VTGATGRIGSKVATTLLEAGRPVRALvrsDERAAALAARgAEVVVGDLDDPAVLAAALAGVDAVFFL--APPAPTADARP 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 928185501 106 YRVNYIgtKNVIETCKEAGVQKLILTSSASVIFEG 140
Cdd:cd05231   81 GYVQAA--EAFASALREAGVKRVVNLSSVGADPES 113
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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