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Conserved domains on  [gi|755534620|ref|XP_011241766|]
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17-beta-hydroxysteroid dehydrogenase type 6 isoform X1 [Mus musculus]

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 ...
30-306 2.37e-137

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 cd09805:

Pssm-ID: 451247 [Multi-domain]  Cd Length: 281  Bit Score: 390.10  E-value: 2.37e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE--KGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGDRGLW 107
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 108 GLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKARGRIVNVSSALGRVALF-GGFYSCSKYGVEAF 186
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 187 SDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERT-KKVWEAAPEHIKESYGQQFFDDFCSTTKRELMKCSRNLSLVT 265
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQaKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 755534620 266 DCMEHALTSTHPRTRYSAGWDAKFFFIPLSYLPASLVDYLL 306
Cdd:cd09805  241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
30-306 2.37e-137

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 390.10  E-value: 2.37e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE--KGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGDRGLW 107
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 108 GLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKARGRIVNVSSALGRVALF-GGFYSCSKYGVEAF 186
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 187 SDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERT-KKVWEAAPEHIKESYGQQFFDDFCSTTKRELMKCSRNLSLVT 265
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQaKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 755534620 266 DCMEHALTSTHPRTRYSAGWDAKFFFIPLSYLPASLVDYLL 306
Cdd:cd09805  241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
PRK05993 PRK05993
SDR family oxidoreductase;
30-307 2.97e-44

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 152.49  E-value: 2.97e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNktsDRLETVILDVTKTESIVAATQWVKERVGDRgLWGL 109
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEA---EGLEAFQLDYAEPESIAALVAQVLELSGGR-LDAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 110 VNNAGVLQPFAYiewyrpEDyMPI------FQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVAL-FGGFYSCSKY 181
Cdd:PRK05993  81 FNNGAYGQPGAV------ED-LPTealraqFEANFFGWHDLTRRVIpVMRKQGQGRIVQCSSILGLVPMkYRGAYNASKF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 182 GVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMT-DAELTIERTKKVwEAAPeHiKESYGQQffddfcsttKRELMKCSRN 260
Cdd:PRK05993 154 AIEGLSLTLRMELQGSGIHVSLIEPGPIETRFRaNALAAFKRWIDI-ENSV-H-RAAYQQQ---------MARLEGGGSK 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755534620 261 LSLV---TDCME---HALTSTHPRTRYSAGWDAKFFFIPLSYLPASLVDYLLA 307
Cdd:PRK05993 222 SRFKlgpEAVYAvllHALTAPRPRPHYRVTTPAKQGALLKRLLPARWLYRLLR 274
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
30-214 9.14e-43

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 145.83  E-value: 9.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLT----EKGAEELRNkTSDRLETVILDVTKTESIVAATQWVKERVGdrG 105
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSeeklEAVAKELGA-LGGKALFIQGDVTDRAQVKALVEQAVERLG--R 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  106 LWGLVNNAGVLQPFAYIEwYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVALFGG-FYSCSKYGV 183
Cdd:pfam00106  78 LDILVNNAGITGLGPFSE-LSDEDWERVIDVNLTGVFNLTRAVLpAMIKGSGGRIVNISSVAGLVPYPGGsAYSASKAAV 156
                         170       180       190
                  ....*....|....*....|....*....|.
gi 755534620  184 EAFSDVLRHEVQDFGVKVSIIEPGSFKTEMT 214
Cdd:pfam00106 157 IGFTRSLALELAPHGIRVNAVAPGGVDTDMT 187
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
26-225 2.14e-37

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 223959 [Multi-domain]  Cd Length: 251  Bit Score: 133.79  E-value: 2.14e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAC------LTEKGAEELRNKTSDRLETVILDVTKT-ESIVAATQWVK 98
Cdd:COG1028    2 DLSGKVALVTGASSGIGRAIARALAREGARVVVAArrseeeAAEALAAAIKEAGGGRAAAVAADVSDDeESVEALVAAAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  99 ERVGdrGLWGLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGLtqVTISMLFLVKKARGRIVNVSSALGRVALFGGF-YS 177
Cdd:COG1028   82 EEFG--RIDILVNNAGIAGPDAPLEELTEEDWDRVIDVNLLGA--FLLTRAALPLMKKQRIVNISSVAGLGGPPGQAaYA 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 755534620 178 CSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERTKK 225
Cdd:COG1028  158 ASKAALIGLTKALALELAPRGIRVNAVAPGYIDTPMTAALESAELEAL 205
dhbA_paeA TIGR04316
2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase; Members of this family are 2,3-dihydro-2, ...
32-213 2.03e-15

2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase; Members of this family are 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (EC 1.3.1.28), the third enzyme in the biosynthesis of 2,3-dihydroxybenzoic acid (DHB) from chorismate. The first two enzymes are isochorismate synthase (EC 5.4.4.2) and isochorismatase (EC 3.3.2.1). Synthesis is often followed by adenylation by the enzyme DHBA-AMP ligase (EC 2.7.7.58) to activate (DHB) for a non-ribosomal peptide synthetase.


Pssm-ID: 275120 [Multi-domain]  Cd Length: 250  Bit Score: 74.25  E-value: 2.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620   32 VFITGCDSGFGNLLARQLDRRGMRVLAaclTEKGAEELRNKTSD------RLETVILDVTKTESIVAATQWVKERVGdrG 105
Cdd:TIGR04316   1 VLVTGAAQGIGYAVARALAEAGARVAA---VDRNFEQLLELVADlrrygyPFATYKLDVADSAAVDEVVQRLEREYG--P 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  106 LWGLVNNAGVLQpFAYIEWYRPEDYMPIFQVNLIG----LTQVTISMlflVKKARGRIVNVSSALGRVALFG-GFYSCSK 180
Cdd:TIGR04316  76 IDVLVNVAGILR-LGAIDSLSDEDWQATFAVNTFGvfnvSQAVSPRM---KRRRSGAIVTVGSNAANVPRMGmAAYAASK 151
                         170       180       190
                  ....*....|....*....|....*....|...
gi 755534620  181 YGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:TIGR04316 152 AALTMLTKCLGLELAPYGIRCNVVSPGSTDTEM 184
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
30-306 2.37e-137

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 390.10  E-value: 2.37e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE--KGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGDRGLW 107
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 108 GLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKARGRIVNVSSALGRVALF-GGFYSCSKYGVEAF 186
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 187 SDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERT-KKVWEAAPEHIKESYGQQFFDDFCSTTKRELMKCSRNLSLVT 265
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQaKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 755534620 266 DCMEHALTSTHPRTRYSAGWDAKFFFIPLSYLPASLVDYLL 306
Cdd:cd09805  241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
30-288 7.66e-62

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


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 196.68  E-value: 7.66e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGdrGLWGL 109
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFG--RIDVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 110 VNNAGVLQPFAyIEWYRPEDYMPIFQVNLIGLTQVT-ISMLFLVKKARGRIVNVSSALGRVAL-FGGFYSCSKYGVEAFS 187
Cdd:cd05374   79 VNNAGYGLFGP-LEETSIEEVRELFEVNVFGPLRVTrAFLPLMRKQGSGRIVNVSSVAGLVPTpFLGPYCASKAALEALS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 188 DVLRHEVQDFGVKVSIIEPGSFKTEMTDAELtiertkkvwEAAPEHIKESYGQQFFDDFcSTTKRELMKCSRNLSLVTDC 267
Cdd:cd05374  158 ESLRLELAPFGIKVTIIEPGPVRTGFADNAA---------GSALEDPEISPYAPERKEI-KENAAGVGSNPGDPEKVADV 227
                        250       260
                 ....*....|....*....|.
gi 755534620 268 MEHALTSTHPRTRYSAGWDAK 288
Cdd:cd05374  228 IVKALTSESPPLRYFLGSDAL 248
PRK05993 PRK05993
SDR family oxidoreductase;
30-307 2.97e-44

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 152.49  E-value: 2.97e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNktsDRLETVILDVTKTESIVAATQWVKERVGDRgLWGL 109
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEA---EGLEAFQLDYAEPESIAALVAQVLELSGGR-LDAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 110 VNNAGVLQPFAYiewyrpEDyMPI------FQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVAL-FGGFYSCSKY 181
Cdd:PRK05993  81 FNNGAYGQPGAV------ED-LPTealraqFEANFFGWHDLTRRVIpVMRKQGQGRIVQCSSILGLVPMkYRGAYNASKF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 182 GVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMT-DAELTIERTKKVwEAAPeHiKESYGQQffddfcsttKRELMKCSRN 260
Cdd:PRK05993 154 AIEGLSLTLRMELQGSGIHVSLIEPGPIETRFRaNALAAFKRWIDI-ENSV-H-RAAYQQQ---------MARLEGGGSK 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755534620 261 LSLV---TDCME---HALTSTHPRTRYSAGWDAKFFFIPLSYLPASLVDYLLA 307
Cdd:PRK05993 222 SRFKlgpEAVYAvllHALTAPRPRPHYRVTTPAKQGALLKRLLPARWLYRLLR 274
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
30-214 9.14e-43

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 145.83  E-value: 9.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLT----EKGAEELRNkTSDRLETVILDVTKTESIVAATQWVKERVGdrG 105
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSeeklEAVAKELGA-LGGKALFIQGDVTDRAQVKALVEQAVERLG--R 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  106 LWGLVNNAGVLQPFAYIEwYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVALFGG-FYSCSKYGV 183
Cdd:pfam00106  78 LDILVNNAGITGLGPFSE-LSDEDWERVIDVNLTGVFNLTRAVLpAMIKGSGGRIVNISSVAGLVPYPGGsAYSASKAAV 156
                         170       180       190
                  ....*....|....*....|....*....|.
gi 755534620  184 EAFSDVLRHEVQDFGVKVSIIEPGSFKTEMT 214
Cdd:pfam00106 157 IGFTRSLALELAPHGIRVNAVAPGGVDTDMT 187
PRK06182 PRK06182
short chain dehydrogenase; Validated
28-306 1.55e-39

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 139.71  E-value: 1.55e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAAClteKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGdrGLW 107
Cdd:PRK06182   2 QKKVALVTGASSGIGKATARRLAAQGYTVYGAA---RRVDKMEDLASLGVHPLSLDVTDEASIKAAVDTIIAEEG--RID 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 108 GLVNNAGvlqpfaYIEWYRPEDyMPI------FQVNLIGLTQVTISMLFLVKKAR-GRIVNVSSALGRVA-LFGGFYSCS 179
Cdd:PRK06182  77 VLVNNAG------YGSYGAIED-VPIdearrqFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIYtPLGAWYHAT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 180 KYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTD--AELTIERT-----KKVWEAAPEHIKESYGQQFfddfcsttkr 252
Cdd:PRK06182 150 KFALEGFSDALRLEVAPFGIDVVVIEPGGIKTEWGDiaADHLLKTSgngayAEQAQAVAASMRSTYGSGR---------- 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755534620 253 elmkcSRNLSLVTDCMEHALTSTHPRTRYSAGWDAKFFFIPLSYLPASLVDYLL 306
Cdd:PRK06182 220 -----LSDPSVIADAISKAVTARRPKTRYAVGFGAKPLIFLRRILPDRAFDRLI 268
PRK06914 PRK06914
SDR family oxidoreductase;
30-307 4.87e-39

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 138.62  E-value: 4.87e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKT-----SDRLETVILDVTKTESIVAATQWVKErVGDR 104
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQAtqlnlQQNIKVQQLDVTDQNSIHNFQLVLKE-IGRI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 105 GLwgLVNNAGvlqpFAY---IEWYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVAlFGGF--YSC 178
Cdd:PRK06914  83 DL--LVNNAG----YANggfVEEIPVEEYRKQFETNVFGAISVTQAVLpYMRKQKSGKIINISSISGRVG-FPGLspYVS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 179 SKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTdaeltiERTKKVWEAAPEHIK--ESYGQQFFDDFCSTTKRelmk 256
Cdd:PRK06914 156 SKYALEGFSESLRLELKPFGIDVALIEPGSYNTNIW------EVGKQLAENQSETTSpyKEYMKKIQKHINSGSDT---- 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755534620 257 cSRNLSLVTDCMEHALTSTHPRTRYSAGWDAKFFFIPLSYLPASLVDYLLA 307
Cdd:PRK06914 226 -FGNPIDVANLIVEIAESKRPKLRYPIGKGVKLMILAKKILPWRLWEYLVL 275
PRK08017 PRK08017
SDR family oxidoreductase;
30-306 4.32e-38

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 135.60  E-value: 4.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAAClteKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGDRgLWGL 109
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAAC---RKPDDVARMNSLGFTGILLDLDDPESVERAADEVIALTDNR-LYGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 110 VNNAG--VLQPFAYIEWYRPEDYmpiFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVALFG-GFYSCSKYGVEA 185
Cdd:PRK08017  79 FNNAGfgVYGPLSTISRQQMEQQ---FSTNFFGTHQLTMLLLpAMLPHGEGRIVMTSSVMGLISTPGrGAYAASKYALEA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 186 FSDVLRHEVQDFGVKVSIIEPGSFKTEMTDaeltiertkKVWEAAPEHIKESYGqqffddfcsttkrelmkCSRNLSL-- 263
Cdd:PRK08017 156 WSDALRMELRHSGIKVSLIEPGPIRTRFTD---------NVNQTQSDKPVENPG-----------------IAARFTLgp 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 755534620 264 --VTDCMEHALTSTHPRTRYSAGWDAKFFFIPLSYLPASLVDYLL 306
Cdd:PRK08017 210 eaVVPKLRHALESPKPKLRYPVTLVTHAVMVLKRLLPGRMMDKIL 254
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
26-225 2.14e-37

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 223959 [Multi-domain]  Cd Length: 251  Bit Score: 133.79  E-value: 2.14e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAC------LTEKGAEELRNKTSDRLETVILDVTKT-ESIVAATQWVK 98
Cdd:COG1028    2 DLSGKVALVTGASSGIGRAIARALAREGARVVVAArrseeeAAEALAAAIKEAGGGRAAAVAADVSDDeESVEALVAAAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  99 ERVGdrGLWGLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGLtqVTISMLFLVKKARGRIVNVSSALGRVALFGGF-YS 177
Cdd:COG1028   82 EEFG--RIDILVNNAGIAGPDAPLEELTEEDWDRVIDVNLLGA--FLLTRAALPLMKKQRIVNISSVAGLGGPPGQAaYA 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 755534620 178 CSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERTKK 225
Cdd:COG1028  158 ASKAALIGLTKALALELAPRGIRVNAVAPGYIDTPMTAALESAELEAL 205
PRK06180 PRK06180
short chain dehydrogenase; Provisional
33-241 6.28e-37

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 133.12  E-value: 6.28e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  33 FITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGdrGLWGLVNN 112
Cdd:PRK06180   8 LITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFG--PIDVLVNN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 113 AGVLQpFAYIEWYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVALFG-GFYSCSKYGVEAFSDVL 190
Cdd:PRK06180  86 AGYGH-EGAIEESPLAEMRRQFEVNVFGAVAMTKAVLpGMRARRRGHIVNITSMGGLITMPGiGYYCGSKFALEGISESL 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755534620 191 RHEVQDFGVKVSIIEPGSFKTE-----MTDAELTIERTKKVWEAAPEHIKESYGQQ 241
Cdd:PRK06180 165 AKEVAPFGIHVTAVEPGSFRTDwagrsMVRTPRSIADYDALFGPIRQAREAKSGKQ 220
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
32-231 6.71e-36

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


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 129.33  E-value: 6.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD--RLETVILDVTKTESIVAATQWVKERVGdrGLWGL 109
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEALggNAVAVQADVSDEEDVEALVEEALEEFG--RLDIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 110 VNNAGVlQPFAYIEWYRPEDYMPIFQVNLIGLTQVT-ISMLFLVKKARGRIVNVSSALGRVALFG-GFYSCSKYGVEAFS 187
Cdd:cd05233   79 VNNAGI-ARPGPLEELTDEDWDRVLDVNLTGVFLLTrAALPHMKKQGGGRIVNISSVAGLRPLPGqAAYAASKAALEGLT 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 755534620 188 DVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERTKKVWEAAP 231
Cdd:cd05233  158 RSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAAIP 201
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
27-221 7.18e-34

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


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 124.62  E-value: 7.18e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacLT-------EKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKE 99
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLV---LSarreerlEEVKSECLELGAPSPHVVPLDMSDLEDAEQVVEEALK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 100 RVGdrGLWGLVNNAGVLQPfAYIEWYRPEDYMPIFQVNLIG---LTQVTISMLflVKKARGRIVNVSSALGRVAL-FGGF 175
Cdd:cd05332   78 LFG--GLDILINNAGISMR-SLFHDTSIDVDRKIMEVNYFGpvaLTKAALPHL--IERSQGSIVVVSSIAGKIGVpFRTA 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755534620 176 YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIE 221
Cdd:cd05332  153 YAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNALSGD 198
DltE COG0300
Short-chain dehydrogenase [General function prediction only];
26-226 1.73e-33

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 223377 [Multi-domain]  Cd Length: 265  Bit Score: 123.90  E-value: 1.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacLT-------EKGAEELRNKTSDRLETVILDVTKTESIVAATQWVK 98
Cdd:COG0300    3 PMKGKTALITGASSGIGAELAKQLARRGYNLI---LVarredklEALAKELEDKTGVEVEVIPADLSDPEALERLEDELK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  99 ERVGDRGLwgLVNNAGV--LQPFAYIEWYRPEDympIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVA-LFGG 174
Cdd:COG0300   80 ERGGPIDV--LVNNAGFgtFGPFLELSLDEEEE---MIQLNILALTRLTKAVLpGMVERGAGHIINIGSAAGLIPtPYMA 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755534620 175 FYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERTKKV 226
Cdd:COG0300  155 VYSATKAFVLSFSEALREELKGTGVKVTAVCPGPTRTEFFDAKGSDVYLLSP 206
PRK06179 PRK06179
short chain dehydrogenase; Provisional
28-303 1.25e-32

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 121.55  E-value: 1.25e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAAclTEKGAeelRNKTSDRLETVILDVTKTESIVAATQWVKERVGDRGLw 107
Cdd:PRK06179   3 NSKVALVTGASSGIGRATAEKLARAGYRVFGT--SRNPA---RAAPIPGVELLELDVTDDASVQAAVDEVIARAGRIDV- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 108 gLVNNAGVlQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKAR-GRIVNVSSALGRV-ALFGGFYSCSKYGVEA 185
Cdd:PRK06179  77 -LVNNAGV-GLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGsGRIINISSVLGFLpAPYMALYAASKHAVEG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 186 FSDVLRHEVQDFGVKVSIIEPGSFKTEMtDAELtiertkkvweAAPEHIKESYGQQFfdDFCSTTKRELMKCSRNLSLVT 265
Cdd:PRK06179 155 YSESLDHEVRQFGIRVSLVEPAYTKTNF-DANA----------PEPDSPLAEYDRER--AVVSKAVAKAVKKADAPEVVA 221
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 755534620 266 DCMEHALTSTHPRTRYSAGWDAKFFFIPLSYLPASLVD 303
Cdd:PRK06179 222 DTVVKAALGPWPKMRYTAGGQASLLSKLRRFMPAGAVD 259
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
27-228 1.19e-31

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


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 118.41  E-value: 1.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNK---TSDRLETVILDVTKTESIVAATQWVKERVGd 103
Cdd:cd08934    1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADEleaEGGKALVLELDVTDEQQVDAAVERTVEALG- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 rGLWGLVNNAGVLQpFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVK-KARGRIVNVSSALGRVALFG-GFYSCSKY 181
Cdd:cd08934   80 -RLDILVNNAGIML-LGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLlRNKGTIVNISSVAGRVAVRNsAVYNATKF 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 755534620 182 GVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDaELTIERTKKVWE 228
Cdd:cd08934  158 GVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRD-HITHTITKEAYE 203
PRK08263 PRK08263
short chain dehydrogenase; Provisional
33-256 5.70e-31

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 117.45  E-value: 5.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  33 FITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGDrgLWGLVNN 112
Cdd:PRK08263   7 FITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGR--LDIVVNN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 113 AGVLQpFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKAR-GRIVNVSSALGRVALFG-GFYSCSKYGVEAFSDVL 190
Cdd:PRK08263  85 AGYGL-FGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRsGHIIQISSIGGISAFPMsGIYHASKWALEGMSEAL 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755534620 191 RHEVQDFGVKVSIIEPGSFKTEMTDAELTIERTKKVWEAAPEHIKESYGQQFFDDFCSTTKRELMK 256
Cdd:PRK08263 164 AQEVAEFGIKVTLVEPGGYSTDWAGTSAKRATPLDAYDTLREELAEQWSERSVDGDPEAAAEALLK 229
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
27-236 4.15e-30

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 114.04  E-value: 4.15e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGM-RVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKErvgdrg 105
Cdd:cd05354    1 IKDKTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAAQAKD------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 106 LWGLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKA-RGRIVNVSSALGRVALFG-GFYSCSKYGV 183
Cdd:cd05354   75 VDVVINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANgGGAIVNLNSVASLKNFPAmGTYSASKSAA 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755534620 184 EAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAeltIERTKkvweAAPEHIKE 236
Cdd:cd05354  155 YSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAG---AGGPK----ESPETVAE 200
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
30-221 2.17e-29

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


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 111.95  E-value: 2.17e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRG--MRVLAACLTEKG---AEELRNKTSDrLETVILDVTKTESIVAATQWVKERVGdr 104
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGpgTVILTARDVERGqaaVEKLRAEGLS-VRFHQLDVTDDASIEAAADFVEEKYG-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 105 GLWGLVNNAGVL-------QPFaYIEWyrpEDYMpifQVNLIGLTQVTISMLFLVKKAR-GRIVNVSSALGRVALFggfY 176
Cdd:cd05324   78 GLDILVNNAGIAfkgfddsTPT-REQA---RETM---KTNFFGTVDVTQALLPLLKKSPaGRIVNVSSGLGSLTSA---Y 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 755534620 177 SCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMT--DAELTIE 221
Cdd:cd05324  148 GVSKAALNALTRILAKELKETGIKVNACCPGWVKTDMGggKAPKTPE 194
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
32-215 8.49e-29

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 110.46  E-value: 8.49e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRG-MRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGDRGLWGLV 110
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSAATELAALGASHSRLHILELDVTDEIAESAEAVAERLGDAGLDVLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 111 NNAGVLQPFAYIEWYRPEDYMPIFQVNLIG---LTQVTISMlfLVKKARGRIVNVSSALGRVALFGGF----YSCSKYGV 183
Cdd:cd05325   81 NNAGILHSYGPASEVDSEDLLEVFQVNVLGpllLTQAFLPL--LLKGARAKIINISSRVGSIGDNTSGgwysYRASKAAL 158
                        170       180       190
                 ....*....|....*....|....*....|..
gi 755534620 184 EAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTD 215
Cdd:cd05325  159 NMLTKSLAVELKRDGITVVSLHPGWVRTDMGG 190
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion];
25-239 5.28e-28

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


Pssm-ID: 226674 [Multi-domain]  Cd Length: 246  Bit Score: 108.88  E-value: 5.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  25 SHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNK-TSDRLETVILDVTKTESIVAATQWVKERVGD 103
Cdd:COG4221    2 TTLKGKVALITGASSGIGEATARALAEAGAKVVLAARREERLEALADEiGAGAALALALDVTDRAAVEAAIEALPEEFGR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 RGLwgLVNNAGV--LQPFAYiewYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVALFGG-FYSCS 179
Cdd:COG4221   82 IDI--LVNNAGLalGDPLDE---ADLDDWDRMIDTNVKGLLNGTRAVLpGMVERKSGHIINLGSIAGRYPYPGGaVYGAT 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 180 KYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEmtdaELTIERTKKVWEAAPEHIKESYG 239
Cdd:COG4221  157 KAAVRAFSLGLRQELAGTGIRVTVISPGLVETT----EFSTVRFEGDDERADKVYKGGTA 212
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
27-216 3.06e-27

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 106.82  E-value: 3.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLT-EKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASsEAGAEALVAEIGAlggKALAVQGDVSDAESVERAVDEAKAEFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 drGLWGLVNNAGVLQPfAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKAR-GRIVNVSSALGRVALFG-GFYSCSK 180
Cdd:PRK05557  83 --GVDILVNNAGITRD-NLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRsGRIINISSVVGLMGNPGqANYAASK 159
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 755534620 181 YGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDA 216
Cdd:PRK05557 160 AGVIGFTKSLARELASRGITVNAVAPGFIETDMTDA 195
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
29-246 1.58e-26

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


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 104.64  E-value: 1.58e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE----KGAEELR---NKTSDRLETVILDVTKTESIVAATQWVKERV 101
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSEskleEAVEEIEaeaNASGQKVSYISADLSDYEEVEQAFAQAVEKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 102 GDRGLwgLVNNAGVLQPfAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKAR-GRIVNVSSALGRVALFG-GFYSCS 179
Cdd:cd08939   81 GPPDL--VVNCAGISIP-GLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRpGHIVFVSSQAALVGIYGySAYCPS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 180 KYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELT--------IERTKKVW---EAAPEHIK--ESYGQQFFDDF 246
Cdd:cd08939  158 KFALRGLAESLRQELKPYNIRVSVVYPPDTDTPGFEEENKtkpeetkaIEGSSGPItpeEAARIIVKglDRGYDDVFTDF 237
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
32-215 2.28e-26

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


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 104.25  E-value: 2.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRN---KTSDRLETVILDVTKTESIVAATQWVKERVGDRGLwg 108
Cdd:cd05339    2 VLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANnvrKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTI-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 109 LVNNAGVLQPFAYIEwYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVALFGGF-YSCSKYGVEAF 186
Cdd:cd05339   80 LINNAGVVSGKKLLE-LPDEEIEKTFEVNTLAHFWTTKAFLpDMLERNHGHIVTIASVAGLISPAGLAdYCASKAAAVGF 158
                        170       180       190
                 ....*....|....*....|....*....|..
gi 755534620 187 SDVLRHEV---QDFGVKVSIIEPGSFKTEMTD 215
Cdd:cd05339  159 HESLRLELkayGKPGIKTTLVCPYFINTGMFQ 190
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
30-236 3.81e-25

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


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 101.20  E-value: 3.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLaacLT-------EKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLI---LTgrraerlQELADELGAKFPVKVLPLQLDVSDRESIEAALENLPEEFR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 DrgLWGLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVALFGG-FYSCSK 180
Cdd:cd05346   78 D--IDILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILpIMIARNQGHIINLGSIAGRYPYAGGnVYCATK 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755534620 181 YGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMT------DAeltiERTKKVWEAA----PEHIKE 236
Cdd:cd05346  156 AAVRQFSLNLRKDLIGTGIRVTNIEPGLVETEFSlvrfhgDK----EKADKVYEGVepltPEDIAE 217
PRK12826 PRK12826
SDR family oxidoreductase;
27-219 1.39e-24

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 99.61  E-value: 1.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKERVGd 103
Cdd:PRK12826   4 LEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAaggKARARQVDVRDRAALKAAVAAGVEDFG- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 rGLWGLVNNAGV--LQPFAYIEwyrPEDYMPIFQVNLIG---LTQVTISMLflVKKARGRIVNVSSALGRVALFGGF--Y 176
Cdd:PRK12826  83 -RLDILVANAGIfpLTPFAEMD---DEQWERVIDVNLTGtflLTQAALPAL--IRAGGGRIVLTSSVAGPRVGYPGLahY 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 755534620 177 SCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELT 219
Cdd:PRK12826 157 AASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNLGD 199
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
27-225 1.66e-24

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 99.56  E-value: 1.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACL-TEKGAEELRNK---TSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK12825   4 LMGRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEAveaLGRRAQAVQADVTDKAALEAAVAAAVERFG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 drGLWGLVNNAGVLQPFAYIEwYRPEDYMPIFQVNLIG---LTQVTI-SMlflvKKAR-GRIVNVSSA------LGRVAl 171
Cdd:PRK12825  84 --RIDILVNNAGIFEDKPLAD-MSDDEWDEVIDVNLSGvfhLLRAVVpPM----RKQRgGRIVNISSVaglpgwPGRSN- 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755534620 172 fggfYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERTKK 225
Cdd:PRK12825 156 ----YAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAREAK 205
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
30-241 2.23e-24

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 99.07  E-value: 2.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGA----EELRNKTSDRLETVILDVTKTESIVAATQWVKERVGDRG 105
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCakdwFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGPVD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 106 LwgLVNNAGVLQPFAYIEwYRPEDYMPIFQVNLIGLTQVTiSMLF--LVKKARGRIVNVSSALGRVALFGGF-YSCSKYG 182
Cdd:PRK12824  83 I--LVNNAGITRDSVFKR-MSHQEWNDVINTNLNSVFNVT-QPLFaaMCEQGYGRIINISSVNGLKGQFGQTnYSAAKAG 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755534620 183 VEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTdaeltiertkkvwEAAPEHIKESYGQQ 241
Cdd:PRK12824 159 MIGFTKALASEGARYGITVNCIAPGYIATPMV-------------EQMGPEVLQSIVNQ 204
PRK09072 PRK09072
SDR family oxidoreductase;
26-219 2.24e-24

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 99.25  E-value: 2.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTS--DRLETVILDVTKTESIVAATQWVKERvgd 103
Cdd:PRK09072   2 DLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPypGRHRWVVADLTSEAGREAVLARAREM--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 RGLWGLVNNAGVLQpFAYIEWYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVAlFGGF--YSCSK 180
Cdd:PRK09072  79 GGINVLINNAGVNH-FALLEDQDPEAIERLLALNLTAPMQLTRALLpLLRAQPSAMVVNVGSTFGSIG-YPGYasYCASK 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 755534620 181 YGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELT 219
Cdd:PRK09072 157 FALRGFSEALRRELADTGVRVLYLAPRATRTAMNSEAVQ 195
PRK06482 PRK06482
SDR family oxidoreductase;
33-231 3.67e-24

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 99.03  E-value: 3.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  33 FITGCDSGFGNLLARQLDRRGMRVlAACLTEKGA-EELRNKTSDRLETVILDVTKTESIVAATQWVKERVGDRGLwgLVN 111
Cdd:PRK06482   6 FITGASSGFGRGMTERLLARGDRV-AATVRRPDAlDDLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAALGRIDV--VVS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 112 NAGvLQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVALFG-GFYSCSKYGVEAFSDV 189
Cdd:PRK06482  83 NAG-YGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALpHLRRQGGGRIVQVSSEGGQIAYPGfSLYHATKWGIEGFVEA 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 755534620 190 LRHEVQDFGVKVSIIEPGSFKTEMTdAELTIERTKKVWEAAP 231
Cdd:PRK06482 162 VAQEVAPFGIEFTIVEPGPARTNFG-AGLDRGAPLDAYDDTP 202
PRK05650 PRK05650
SDR family oxidoreductase;
32-215 6.06e-24

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 98.57  E-value: 6.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKERVGdrGLWG 108
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREaggDGFYQRCDVRDYSQLTALAQACEEKWG--GIDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 109 LVNNAGVLQPfAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKAR-GRIVNVSSALGRV-ALFGGFYSCSKYGVEAF 186
Cdd:PRK05650  81 IVNNAGVASG-GFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKsGRIVNIASMAGLMqGPAMSSYNVAKAGVVAL 159
                        170       180
                 ....*....|....*....|....*....
gi 755534620 187 SDVLRHEVQDFGVKVSIIEPGSFKTEMTD 215
Cdd:PRK05650 160 SETLLVELADDEIGVHVVCPSFFQTNLLD 188
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
30-281 2.19e-23

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 96.76  E-value: 2.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDR---RGMRVLAAC--LTEKG--AEELRNKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLASdpsKRFKVYATMrdLKKKGrlWEAAGALAGGTLETLQLDVCDSKSVAAAVERVTERHV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 DRglwgLVNNAGV--LQPFAYIEwyrpEDYMP-IFQVNLIGLTQVTISMLFLVKKAR-GRIVNVSSALGRVAL-FGGFYS 177
Cdd:cd09806   81 DV----LVCNAGVglLGPLEALS----EDAMAsVFDVNVFGTVRMLQAFLPDMKRRGsGRILVTSSVGGLQGLpFNDVYC 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 178 CSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDaeltiertkKVWEAAPE----HIKESYGQQFFDDFCSTTKRE 253
Cdd:cd09806  153 ASKFALEGLCESLAVQLLPFNVHLSLIECGPVHTAFME---------KVLGSPEEvldrTADDITTFHFFYQYLAHSKQV 223
                        250       260
                 ....*....|....*....|....*...
gi 755534620 254 LMKCSRNLSLVTDCMEHALTSTHPRTRY 281
Cdd:cd09806  224 FREAAQNPEEVAEVFLTAIRAPKPPLRY 251
PRK09291 PRK09291
SDR family oxidoreductase;
30-211 2.35e-23

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 96.61  E-value: 2.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDR---LETVILDVTKTESIVAATQWvkervgDRGL 106
Cdd:PRK09291   3 KTILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRglaLRVEKLDLTDAIDRAQAAEW------DVDV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 wgLVNNAGVLQPFAYIEwyrpedyMPI------FQVNLIG---LTQVTISMLflVKKARGRIVNVSSALG-RVALFGGFY 176
Cdd:PRK09291  77 --LLNNAGIGEAGAVVD-------IPVelvrelFETNVFGpleLTQGFVRKM--VARGKGKVVFTSSMAGlITGPFTGAY 145
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 755534620 177 SCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKT 211
Cdd:PRK09291 146 CASKHALEAIAEAMHAELKPFGIQVATVNPGPYLT 180
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
30-236 2.51e-23

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


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 95.65  E-value: 2.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGdrGLWGL 109
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFG--GLDAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 110 VNNAGV-----LQPFAYIEWYRPEDympifQVNLIGLTQVTISMLFLVKKARGRIVNVSSALGRVALFGGF-YSCSKYGV 183
Cdd:cd08929   79 VNNAGVgvmkpVEELTPEEWRLVLD-----TNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAaYNASKFGL 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755534620 184 EAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDaeltiERTKKVWEAAPEHIKE 236
Cdd:cd08929  154 LGLSEAAMLDLREANIRVVNVMPGSVDTGFAG-----SPEGQAWKLAPEDVAQ 201
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
27-216 2.68e-23

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 96.00  E-value: 2.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTS---DRLETVILDVTKTESIVAATQWVKERVGd 103
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRaagGEARVLVFDVSDEAAVRALIEAAVEAFG- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 rGLWGLVNNAGVLqPFAYIEWYRPEDYMPIFQVNLIG---LTQVTIsMLfLVKKARGRIVNVSSALGRVALFG-GFYSCS 179
Cdd:PRK05653  82 -ALDILVNNAGIT-RDALLPRMSEEDWDRVIDVNLTGtfnVVRAAL-PP-MIKARYGRIVNISSVSGVTGNPGqTNYSAA 157
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 755534620 180 KYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDA 216
Cdd:PRK05653 158 KAGVIGFTKALALELASRGITVNAVAPGFIDTDMTEG 194
PRK07326 PRK07326
SDR family oxidoreductase;
27-236 6.40e-23

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 94.69  E-value: 6.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVIL--DVTKTESIVAATQWVKERVGdr 104
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGNVLGLaaDVRDEADVQRAVDAIVAAFG-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 105 GLWGLVNNAGVLQpFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKARGRIVNVSSALGRVALFGGF-YSCSKYGV 183
Cdd:PRK07326  82 GLDVLIANAGVGH-FAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGTNFFAGGAaYNASKFGL 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755534620 184 EAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAEltiERTKKVWEAAPEHIKE 236
Cdd:PRK07326 161 VGFSEAAMLDLRQYGIKVSTIMPGSVATHFNGHT---PSEKDAWKIQPEDIAQ 210
PRK08264 PRK08264
SDR family oxidoreductase;
26-216 9.00e-23

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 94.57  E-value: 9.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  26 HLQDKYVFITGCDSGFGNLLARQLDRRG-MRVLAACltekgaeelRNKTS-----DRLETVILDVTKTESIVAATqwvkE 99
Cdd:PRK08264   3 DIKGKVVLVTGANRGIGRAFVEQLLARGaAKVYAAA---------RDPESvtdlgPRVVPLQLDVTDPASVAAAA----E 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 100 RVGDRGLwgLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISmlF---LVKKARGRIVNVSSALGRVAL-FGGF 175
Cdd:PRK08264  70 AASDVTI--LVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARA--FapvLAANGGGAIVNVLSVLSWVNFpNLGT 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 755534620 176 YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDA 216
Cdd:PRK08264 146 YSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAAG 186
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
30-216 9.59e-23

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


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 94.54  E-value: 9.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGA---EELRNKTSDRLETVILDVTKTESIVAATQWVKERVGdrGL 106
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAaetVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFG--PV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 WGLVNNAGVLQPfAYIEWYRPEDYMPIFQVNLIGL---TQ-VTISMlflVKKARGRIVNVSSALGRVALFGGF-YSCSKY 181
Cdd:cd05333   79 DILVNNAGITRD-NLLMRMSEEDWDAVINVNLTGVfnvTQaVIRAM---IKRRSGRIINISSVVGLIGNPGQAnYAASKA 154
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 755534620 182 GVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDA 216
Cdd:cd05333  155 GVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDA 189
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
27-216 9.60e-23

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


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 94.30  E-value: 9.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDrLETVILDVTKTESIVAATQWVKERvgDRGL 106
Cdd:cd05370    3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN-IHTIVLDVGDAESVEALAEALLSE--YPNL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 WGLVNNAGVLQPfayIEWYRPEDYMPIFQ----VNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVALFGG-FYSCSK 180
Cdd:cd05370   80 DILINNAGIQRP---IDLRDPASDLDKADteidTNLIGPIRLIKAFLpHLKKQPEATIVNVSSGLAFVPMAANpVYCATK 156
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 755534620 181 YGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDA 216
Cdd:cd05370  157 AALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEE 192
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
27-216 1.03e-22

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


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 94.37  E-value: 1.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGdrGL 106
Cdd:cd05341    3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFG--RL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 WGLVNNAGVLQPfAYIEWYRPEDYMPIFQVNL----IGLTQVTISMlflvKKA-RGRIVNVSSALGRV--ALFGGfYSCS 179
Cdd:cd05341   81 DVLVNNAGILTG-GTVETTTLEEWRRLLDINLtgvfLGTRAVIPPM----KEAgGGSIINMSSIEGLVgdPALAA-YNAS 154
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 755534620 180 KYGVEAFSDVLRHEV--QDFGVKVSIIEPGSFKTEMTDA 216
Cdd:cd05341  155 KGAVRGLTKSAALECatQGYGIRVNSVHPGYIYTPMTDE 193
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
30-217 3.41e-22

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


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 92.43  E-value: 3.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRnKTSDRLETVILDVTKTESIVAATQWVKERVGdrGLWGL 109
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALS-ASGGDVEAVPYDARDPEDARALVDALRDRFG--RIDVL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 110 VNNAGVLQPFAYIEwYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALG-RVALFGGFYSCSKYGVEAFS 187
Cdd:cd08932   78 VHNAGIGRPTTLRE-GSDAELEAHFSINVIAPAELTRALLpALREAGSGRVVFLNSLSGkRVLAGNAGYSASKFALRALA 156
                        170       180       190
                 ....*....|....*....|....*....|
gi 755534620 188 DVLRHEVQDFGVKVSIIEPGSFKTEMTDAE 217
Cdd:cd08932  157 HALRQEGWDHGVRVSAVCPGFVDTPMAQGL 186
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
32-211 3.66e-22

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


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 92.83  E-value: 3.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG----AEELRNKTSDRLeTVILDVTKTESIVAATQWVKERVGDRGLW 107
Cdd:cd05360    3 VVITGASSGIGRATALAFAERGAKVVLAARSAEAlhelAREVRELGGEAI-AVVADVADAAQVERAADTAVERFGRIDTW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 108 glVNNAGVlQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALG-RVALFGGFYSCSKYGVEA 185
Cdd:cd05360   82 --VNNAGV-AVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALpHLRRRGGGALINVGSLLGyRSAPLQAAYSASKHAVRG 158
                        170       180
                 ....*....|....*....|....*...
gi 755534620 186 FSDVLRHEVQDFG--VKVSIIEPGSFKT 211
Cdd:cd05360  159 FTESLRAELAHDGapISVTLVQPTAMNT 186
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
25-228 7.52e-22

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 92.54  E-value: 7.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  25 SHLQDKYVFITGCDSGFGNLLARQLDRRGMRVlaACL---TEKGAEELRNKTSdrlETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK06463   3 MRFKGKVALITGGTRGIGRAIAEAFLREGAKV--AVLynsAENEAKELREKGV---FTIKCDVGNRDQVKKSKEVVEKEF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 102 GDRGLwgLVNNAGV--LQPFayiEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKAR-GRIVNVSS--ALGRVALFGGFY 176
Cdd:PRK06463  78 GRVDV--LVNNAGImyLMPF---EEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKnGAIVNIASnaGIGTAAEGTTFY 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755534620 177 SCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERTKKVWE 228
Cdd:PRK06463 153 AITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLSGKSQEEAEKLRE 204
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
27-236 1.60e-21

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 91.29  E-value: 1.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG----AEELrNKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK07666   5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENlkavAEEV-EAYGVKVVIATADVSDYEEVTAAIEQLKNELG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 DRGLwgLVNNAGVLQPFAYIEwYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALG-RVALFGGFYSCSK 180
Cdd:PRK07666  84 SIDI--LINNAGISKFGKFLE-LDPAEWEKIIQVNLMGVYYATRAVLpSMIERQSGDIINISSTAGqKGAAVTSAYSASK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755534620 181 YGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM-TDAELTIERTKKVWEaaPEHIKE 236
Cdd:PRK07666 161 FGVLGLTESLMQEVRKHNIRVTALTPSTVATDMaVDLGLTDGNPDKVMQ--PEDLAE 215
PRK07825 PRK07825
short chain dehydrogenase; Provisional
27-214 2.84e-21

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 91.16  E-value: 2.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEElrnkTSDRLETVI---LDVTKTESIVAATQWVkervgd 103
Cdd:PRK07825   3 LRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKE----TAAELGLVVggpLDVTDPASFAAFLDAV------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 RGLWG----LVNNAGV--LQPFAYiewyRPEDYM-PIFQVNLIGLtqVTISMLFL---VKKARGRIVNVSSALGRVALFG 173
Cdd:PRK07825  73 EADLGpidvLVNNAGVmpVGPFLD----EPDAVTrRILDVNVYGV--ILGSKLAAprmVPRGRGHVVNVASLAGKIPVPG 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 755534620 174 G-FYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMT 214
Cdd:PRK07825 147 MaTYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELI 188
PRK05693 PRK05693
SDR family oxidoreductase;
32-235 2.88e-21

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 91.01  E-value: 2.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRGMRVLAaclTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGdrGLWGLVN 111
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWA---TARKAEDVEALAAAGFTAVQLDVNDGAALARLAEELEAEHG--GLDVLIN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 112 NAG--VLQPFAYIewyrPEDYM-PIFQVNLIGLTQVTISMLFLVKKARGRIVNVSSALG-RVALFGGFYSCSKYGVEAFS 187
Cdd:PRK05693  79 NAGygAMGPLLDG----GVEAMrRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGvLVTPFAGAYCASKAAVHALS 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755534620 188 DVLRHEVQDFGVKVSIIEPG----SF-KTEMTDAELTIERTKKVWEAApEHIK 235
Cdd:PRK05693 155 DALRLELAPFGVQVMEVQPGaiasQFaSNASREAEQLLAEQSPWWPLR-EHIQ 206
PRK05872 PRK05872
short chain dehydrogenase; Provisional
27-223 7.17e-21

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 90.41  E-value: 7.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNK--TSDRLETVILDVTKTESIVAATQWVKERVGdr 104
Cdd:PRK05872   7 LAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAElgGDDRVLTVVADVTDLAAMQAAAEEAVERFG-- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 105 GLWGLVNNAGVLQ--PFAYIEwyrPEDYMPIFQVNLIGLTQVTISMLFLVKKARGRIVNVSS--ALGrVALFGGFYSCSK 180
Cdd:PRK05872  85 GIDVVVANAGIASggSVAQVD---PDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSlaAFA-AAPGMAAYCASK 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755534620 181 YGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM---TDAELTIERT 223
Cdd:PRK05872 161 AGVEAFANALRLEVAHHGVTVGSAYLSWIDTDLvrdADADLPAFRE 206
PRK07832 PRK07832
SDR family oxidoreductase;
30-221 3.11e-20

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 88.18  E-value: 3.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEELRNKTSD---RLETVI----LDVTKTESIVAATQWVKERVG 102
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELF---LTDRDADGLAQTVADaraLGGTVPehraLDISDYDAVAAFAADIHAAHG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 DRGLwgLVNNAGVlQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGR-IVNVSSALGRVAL-FGGFYSCS 179
Cdd:PRK07832  78 SMDV--VMNIAGI-SAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVpPMVAAGRGGhLVNVSSAAGLVALpWHAAYSAS 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 755534620 180 KYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDaelTIE 221
Cdd:PRK07832 155 KFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVN---TVE 193
PRK12939 PRK12939
short chain dehydrogenase; Provisional
24-222 8.15e-20

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 86.56  E-value: 8.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  24 VSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKER 100
Cdd:PRK12939   2 ASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAaggRAHAIAADLADPASVQRFFDAAAAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 101 VGdrGLWGLVNNAGVLqPFAYIEWYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSAlgrVALFG----GF 175
Cdd:PRK12939  82 LG--GLDGLVNNAGIT-NSKSATELDIDTWDAVMNVNVRGTFLMLRAALpHLRDSGRGRIVNLASD---TALWGapklGA 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 755534620 176 YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIER 222
Cdd:PRK12939 156 YVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEATAYVPADER 202
PRK12829 PRK12829
short chain dehydrogenase; Provisional
20-241 8.91e-20

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 87.04  E-value: 8.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  20 ERQVVSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLET-VILDVTKTESIVAATQWVK 98
Cdd:PRK12829   2 AIDLLKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPGAKVTaTVADVADPAQVERVFDTAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  99 ERVGdrGLWGLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIG---LTQVTISMLflvkKARGR---IVNVSSALGRVAL- 171
Cdd:PRK12829  82 ERFG--GLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGqfyFARAAVPLL----KASGHggvIIALSSVAGRLGYp 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 172 FGGFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIeRTKKVWEAAPEHiKESYGQQ 241
Cdd:PRK12829 156 GRTPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEA-RAQQLGIGLDEM-EQEYLEK 223
PRK12828 PRK12828
short chain dehydrogenase; Provisional
26-222 1.33e-19

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 86.00  E-value: 1.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEELRNKTSDRLETVI----LDVTKTESIVAATQWVKERV 101
Cdd:PRK12828   4 SLQGKVVAITGGFGGLGRATAAWLAARGARVA---LIGRGAAPLSQTLPGVPADALriggIDLVDPQAARRAVDEVNRQF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 102 GdrGLWGLVNNAGVLqPFAYIEWYRPEDYMPIFQVNLIG-LTQVTISMLFLVKKARGRIVNVSSALGRVALFG-GFYSCS 179
Cdd:PRK12828  81 G--RLDALVNIAGAF-VWGTIADGDADTWDRMYGVNVKTtLNASKAALPALTASGGGRIVNIGAGAALKAGPGmGAYAAA 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 755534620 180 KYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIER 222
Cdd:PRK12828 158 KAGVARLTEALAAELLDRGITVNAVLPSIIDTPPNRADMPDAD 200
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
32-217 1.55e-19

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


Pssm-ID: 226476 [Multi-domain]  Cd Length: 245  Bit Score: 85.94  E-value: 1.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDrLETVILDVTKTESIVAATQWVKERVGDrgLWGLVN 111
Cdd:COG3967    8 ILITGGASGIGLALAKRFLELGNTVIICGRNEERLAEAKAENPE-IHTEVCDVADRDSRRELVEWLKKEYPN--LNVLIN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 112 NAGVLQPfayIEWYRPEDYMPI----FQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVALFGG-FYSCSKYGVEA 185
Cdd:COG3967   85 NAGIQRN---EDLTGAEDLLDDaeqeIATNLLAPIRLTALLLpHLLRQPEATIINVSSGLAFVPMASTpVYCATKAAIHS 161
                        170       180       190
                 ....*....|....*....|....*....|....
gi 755534620 186 FSDVLRHEVQDFGVKVSIIEPGSFKTE--MTDAE 217
Cdd:COG3967  162 YTLALREQLKDTSVEVIELAPPLVDTTegNTQAR 195
PRK06181 PRK06181
SDR family oxidoreductase;
29-212 2.62e-19

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 85.42  E-value: 2.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG----AEELRNKTSDRLeTVILDVTKTESIVAATQWVKERVGdr 104
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRlaslAQELADHGGEAL-VVPTDVSDAEACERLIEAAVARFG-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 105 GLWGLVNNAGV--LQPFAYIE---WYrpEDYMpifQVNLIGLTQVTISMLFLVKKARGRIVNVSSALGRVALFG-GFYSC 178
Cdd:PRK06181  78 GIDILVNNAGItmWSRFDELTdlsVF--ERVM---RVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTrSGYAA 152
                        170       180       190
                 ....*....|....*....|....*....|....
gi 755534620 179 SKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTE 212
Cdd:PRK06181 153 SKHALHGFFDSLRIELADDGVAVTVVCPGFVATD 186
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
31-216 3.42e-19

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 84.65  E-value: 3.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  31 YVFITGCDSGFGNLLARQLDRRGMRVLAACLTE------KGAEELRNktSDRLETVILDVTKT---ESIVAATQWV-KER 100
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARseeplqELKEELRP--GLRVTTVKADLSDAagvEQLLEAIRKLdGER 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 101 VGdrglwgLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKAR--GRIVNVSSALGRVALFG-GFYS 177
Cdd:cd05367   79 DL------LINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGlkKTVVNVSSGAAVNPFKGwGLYC 152
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 755534620 178 CSKYGVEAFSDVLRHEVQDfgVKVSIIEPGSFKTEMTDA 216
Cdd:cd05367  153 SSKAARDMFFRVLAAEEPD--VRVLSYAPGVVDTDMQRE 189
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase;
38-231 4.42e-19

Enoyl-(Acyl carrier protein) reductase;


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 84.40  E-value: 4.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620   38 DSGFGNLLARQLDRRGMRVLAACLTEKGAEELRnKTSDRLETVIL--DVTKTESIVAATQWVKERVGdrGLWGLVNNAGV 115
Cdd:pfam13561   5 ESGIGWAIARALAEEGAEVVLTDLNEALAKRVE-ELAEELGAAVLpcDVTDEEQVEALVAAAVEKFG--RLDILVNNAGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  116 LQPF--AYIEwYRPEDYMPIFQVNLIGLTQVT---ISMLflvkKARGRIVNVSSALGRVALFG-GFYSCSKYGVEAFSDV 189
Cdd:pfam13561  82 APKLkgPFLD-TSREDFDRALDVNLYSLFLLAkaaLPLM----KEGGSIVNLSSIGAERVVPNyNAYGAAKAALEALTRY 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 755534620  190 LRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERTKKVWEA-AP 231
Cdd:pfam13561 157 LAVELGPRGIRVNAISPGPIKTLAASGIPGFDELLAAAEArAP 199
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
32-215 6.87e-19

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


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 83.92  E-value: 6.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKERVGdrGLWG 108
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNpnpSVEVEILDVTDEERNQLVIAELEAELG--GLDL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 109 LVNNAGV--LQPFAYIEWyrpEDYMPIFQVNLIG-LTQVTISMLFLVKKARGRIVNVSSalgrVALFGGF-----YSCSK 180
Cdd:cd05350   79 VIINAGVgkGTSLGDLSF---KAFRETIDTNLLGaAAILEAALPQFRAKGRGHLVLISS----VAALRGLpgaaaYSASK 151
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 755534620 181 YGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTD 215
Cdd:cd05350  152 AALSSLAESLRYDVKKRGIRVTVINPGFIDTPLTA 186
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
30-230 1.09e-18

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


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 83.27  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKT-SDRLETVILDVTKTESIVAATQWVKERVGDRgLWG 108
Cdd:cd08931    1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELgAENVVAGALDVTDRAAWAAALADFAAATGGR-LDA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 109 LVNNAGVLQ--PFAYIEWyrpEDYMPIFQVNLIGLTQVTISMLFLVKKARG-RIVNVSSAlgrVALFG----GFYSCSKY 181
Cdd:cd08931   80 LFNNAGVGRggPFEDVPL---AAHDRMVDINVKGVLNGAYAALPYLKATPGaRVINTASS---SAIYGqpdlAVYSATKF 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755534620 182 GVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERTKK--------------VWEAA 230
Cdd:cd08931  154 AVRGLTEALDVEWARHGIRVADVWPWFVDTPILTKGETGAAPKKglgrvlpvsdvakvVWAAA 216
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
30-237 1.69e-18

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


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 82.73  E-value: 1.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEK--GAEEL-RNKTSDRLETVILDVTKTESIVAATQWVKERVGdrGL 106
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENpgAAAELqAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFG--RV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 WGLVNNAGVLQPFAYIEWYRPE-DYMPIFQVNLIGLTQ-VTISMLFLVKKAR---GRIVNVSSALGRVAL-FGGFYSCSK 180
Cdd:cd05323   79 DILINNAGILDEKSYLFAGKLPpPWEKTIDVNLTGVINtTYLALHYMDKNKGgkgGVIVNIGSVAGLYPApQFPVYSASK 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755534620 181 YGVEAFSDVLRHE-VQDFGVKVSIIEPGSFKTEMTDAEltierTKKVWEAAPEHIKES 237
Cdd:cd05323  159 HGVVGFTRSLADLlEYKTGVRVNAICPGFTNTPLLPDL-----VAKEAEMLPSAPTQS 211
PRK07109 PRK07109
short chain dehydrogenase; Provisional
27-211 1.98e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 84.20  E-value: 1.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG----AEELRNKTSDRLeTVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK07109   6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGlealAAEIRAAGGEAL-AVVADVADAEAVQAAADRAEEELG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 DRGLWglVNNAGV--LQPFAYIewyRPEDYMPIFQVNLIGltQVTISMLFL---VKKARGRIVNVSSALGRVAL-FGGFY 176
Cdd:PRK07109  85 PIDTW--VNNAMVtvFGPFEDV---TPEEFRRVTEVTYLG--VVHGTLAALrhmRPRDRGAIIQVGSALAYRSIpLQSAY 157
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 755534620 177 SCSKYGVEAFSDVLRHEVQDFG--VKVSIIEPGSFKT 211
Cdd:PRK07109 158 CAAKHAIRGFTDSLRCELLHDGspVSVTMVQPPAVNT 194
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
27-231 2.19e-18

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


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 82.71  E-value: 2.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEK-GAEELR---NKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:cd05362    1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNYASSKaAAEEVVaeiEAAGGKAIAVQADVSDPSQVARLFDAAEKAFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 drGLWGLVNNAGVLqPFAYIEWYRPEDYMPIFQVNLIGltqvtisMLFLVKKAR------GRIVNVSSALGRVAL-FGGF 175
Cdd:cd05362   81 --GVDILVNNAGVM-LKKPIAETSEEEFDRMFTVNTKG-------AFFVLQEAAkrlrdgGRIINISSSLTAAYTpNYGA 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755534620 176 YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERTKKVWEAAP 231
Cdd:cd05362  151 YAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYAGKTEEAVEGYAKMSP 206
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
29-214 4.24e-18

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


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 81.50  E-value: 4.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE----KGAEELRNKTSDRLETVILDVTKTESIVaatqwvkERVGDr 104
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQekldAVAKEIEEKYGVETKTIAADFSAGDDIY-------ERIEK- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 105 GLWG-----LVNNAGVLQPFA-YIEWYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRV-ALFGGFY 176
Cdd:cd05356   73 ELEGldigiLVNNVGISHSIPeYFLETPEDELQDIINVNVMATLKMTRLILpGMVKRKKGAIVNISSFAGLIpTPLLATY 152
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 755534620 177 SCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMT 214
Cdd:cd05356  153 SASKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMS 190
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
27-216 6.73e-18

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 81.34  E-value: 6.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKERVGd 103
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQegiKAHAAPFNVTHKQEVEAAIEHIEKDIG- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 rGLWGLVNNAGVLQPFAYIEWyrPE-DYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNV---SSALGRVALFGgfYSC 178
Cdd:PRK08085  86 -PIDVLINNAGIQRRHPFTEF--PEqEWNDVIAVNQTAVFLVSQAVArYMVKRQAGKIINIcsmQSELGRDTITP--YAA 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 755534620 179 SKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDA 216
Cdd:PRK08085 161 SKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKA 198
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
27-216 1.06e-17

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 80.83  E-value: 1.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAC-----LTEKGAEELRNKTSDRLETViLDVTKTESIVAATQWVKERV 101
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAGCgpnspRRVKWLEDQKALGFDFIASE-GNVGDWDSTKAAFDKVKAEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 102 GDRGLwgLVNNAGVLQPFAYIEWYRpEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVALFGGF-YSCS 179
Cdd:PRK12938  80 GEIDV--LVNNAGITRDVVFRKMTR-EDWTAVIDTNLTSLFNVTKQVIdGMVERGWGRIINISSVNGQKGQFGQTnYSTA 156
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 755534620 180 KYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDA 216
Cdd:PRK12938 157 KAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKA 193
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
27-215 1.12e-17

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 80.84  E-value: 1.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGdrGL 106
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFG--GI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 WGLVNNAGV--LQPFAYIEWyrpEDYMPIFQVNLIGltqvtisMLFLVKKA---------RGRIVNVSSALGR-----VA 170
Cdd:PRK07067  82 DILFNNAALfdMAPILDISR---DSYDRLFAVNVKG-------LFFLMQAVarhmveqgrGGKIINMASQAGRrgealVS 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 755534620 171 LfggfYSCSKYGV-----EAFSDVLRHevqdfGVKVSIIEPGSFKTEMTD 215
Cdd:PRK07067 152 H----YCATKAAVisytqSAALALIRH-----GINVNAIAPGVVDTPMWD 192
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
27-216 1.79e-17

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


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 80.09  E-value: 1.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKERVGD 103
Cdd:cd05347    3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKegvEATAFTCDVSDEEAIKAAVEAIEEDFGK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 RGLwgLVNNAGVLQPFAYIEWYRpEDYMPIFQVNLIG---LTQVTISMLflVKKARGRIVNVSSA---LGRVALFGgfYS 177
Cdd:cd05347   83 IDI--LVNNAGIIRRHPAEEFPE-AEWRDVIDVNLNGvffVSQAVARHM--IKQGHGKIINICSLlseLGGPPVPA--YA 155
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 755534620 178 CSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDA 216
Cdd:cd05347  156 ASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTEA 194
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
27-212 1.87e-17

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


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 80.25  E-value: 1.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAC----LTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:cd05343    4 WRGRVALVTGASVGIGAAVARALVQHGMKVVGCArrvdKIEALAAECQSAGYPTLFPYQCDLSNEEQILSMFSAIRTQHQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 drGLWGLVNNAGVLQPFAYIEWyRPEDYMPIFQVNLIGL---TQVTISMLFLVKKARGRIVNVSSALGRVALFG---GFY 176
Cdd:cd05343   84 --GVDVCINNAGLARPEPLLSG-KTEGWKEMFDVNVLALsicTREAYQSMKERNVDDGHIININSMSGHRVPPVsvfHFY 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 755534620 177 SCSKYGVEAFSDVLRHEVQDF--GVKVSIIEPGSFKTE 212
Cdd:cd05343  161 AATKHAVTALTEGLRQELREAktHIRATSISPGLVETE 198
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
27-213 2.25e-17

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 79.89  E-value: 2.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAC-LTEKGAEELRNKTSDRLETVIL---DVTKTESIVAATQWVKERVG 102
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYdINEEAAQELLEEIKEEGGDAIAvkaDVSSEEDVENLVEQIVEKFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 drGLWGLVNNAGVLQ--PFAYI---EWYRpedympIFQVNLIG---LTQ-VTISMLflvKKARGRIVNVSSALGRV-ALF 172
Cdd:PRK05565  83 --KIDILVNNAGISNfgLVTDMtdeEWDR------VIDVNLTGvmlLTRyALPYMI---KRKSGVIVNISSIWGLIgASC 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 755534620 173 GGFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:PRK05565 152 EVLYSASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEM 192
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
29-213 2.65e-17

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 79.96  E-value: 2.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNK-----TSDRLETVILDVTKTESIVAATQWVKERvGD 103
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEikketGNAKVEVIQLDLSSLASVRQFAEEFLAR-FP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 RgLWGLVNNAGVLQPfayieWYR--PEDYMPIFQVNLIG---LTqvtiSMLF--LVKKARGRIVNVSSALGRVALFGGFY 176
Cdd:cd05327   80 R-LDILINNAGIMAP-----PRRltKDGFELQFAVNYLGhflLT----NLLLpvLKASAPSRIVNVSSIAHRAGPIDFND 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755534620 177 SC-----SKYGVEAFSDV----------LRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:cd05327  150 LDlennkEYSPYKAYGQSklanilftreLARRLEGTGVTVNALHPGVVRTEL 201
FabG-like PRK07231
SDR family oxidoreductase;
27-231 3.07e-17

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 79.49  E-value: 3.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG----AEELRnkTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAaervAAEIL--AGGRAIAVAADVSDEADVEAAVAAALERFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 drGLWGLVNNAG---VLQPFAYIEwyrPEDYMPIFQVNLIGL---TQVTI-SMLflvKKARGRIVNVSSALG-RVALFGG 174
Cdd:PRK07231  81 --SVDILVNNAGtthRNGPLLDVD---EAEFDRIFAVNVKSPylwTQAAVpAMR---GEGGGAIVNVASTAGlRPRPGLG 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 175 FYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDA---ELTIERTKKVWEAAP 231
Cdd:PRK07231 153 WYNASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAfmgEPTPENRAKFLATIP 212
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
27-212 3.97e-17

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


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 79.35  E-value: 3.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEK-GAEEL-RNKTSDRLETVIL--DVTKTESIVAATQWVKERVG 102
Cdd:cd05358    1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEdAAEEVvEEIKAVGGKAIAVqaDVSKEEDVVALFQSAIKEFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 drGLWGLVNNAGVLQPFAYIEwYRPEDYMPIFQVNLIG--LTQVTISMLFLVKKARGRIVNVSSALGRVAlFGGF--YSC 178
Cdd:cd05358   81 --TLDILVNNAGLQGDASSHE-MTLEDWNKVIDVNLTGqfLCAREAIKRFRKSKIKGKIINMSSVHEKIP-WPGHvnYAA 156
                        170       180       190
                 ....*....|....*....|....*....|....
gi 755534620 179 SKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTE 212
Cdd:cd05358  157 SKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTP 190
PRK08219 PRK08219
SDR family oxidoreductase;
34-213 4.73e-17

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 78.44  E-value: 4.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  34 ITGCDSGFGNLLARQLDRRgMRVLAACLTEKGAEELRNkTSDRLETVILDVTKTESIVAATQWVKErvgdrgLWGLVNNA 113
Cdd:PRK08219   8 ITGASRGIGAAIARELAPT-HTLLLGGRPAERLDELAA-ELPGATPFPVDLTDPEAIAAAVEQLGR------LDVLVHNA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 114 GVLQPfAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKARGRIVNVSSALGRVALFG-GFYSCSKYGVEAFSDVLRH 192
Cdd:PRK08219  80 GVADL-GPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRANPGwGSYAASKFALRALADALRE 158
                        170       180
                 ....*....|....*....|.
gi 755534620 193 EvQDFGVKVSIIEPGSFKTEM 213
Cdd:PRK08219 159 E-EPGNVRVTSVHPGRTDTDM 178
PRK07454 PRK07454
SDR family oxidoreductase;
32-217 1.96e-16

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 76.92  E-value: 1.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRGMRVL----AACLTEKGAEELRNKTSdRLETVILDVTKTESIVAATQWVKERVGDRGLw 107
Cdd:PRK07454   9 ALITGASSGIGKATALAFAKAGWDLAlvarSQDALEALAAELRSTGV-KAAAYSIDLSNPEAIAPGIAELLEQFGCPDV- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 108 gLVNNAGVL-------QPFAYIEWyrpedympIFQVNLIGLTQVTISMLFLVKKAR-GRIVNVSSALGRVALFG-GFYSC 178
Cdd:PRK07454  87 -LINNAGMAytgplleMPLSDWQW--------VIQLNLTSVFQCCSAVLPGMRARGgGLIINVSSIAARNAFPQwGAYCV 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 755534620 179 SKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAE 217
Cdd:PRK07454 158 SKAALAAFTKCLAEEERSHGIRVCTITLGAVNTPLWDTE 196
PRK08267 PRK08267
SDR family oxidoreductase;
30-230 2.92e-16

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 76.90  E-value: 2.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNK-TSDRLETVILDVTKtesivaATQWvKERVGDRGLWG 108
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAElGAGNAWTGALDVTD------RAAW-DAALADFAAAT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 109 ------LVNNAGVLQ--PFAYIEwyrPEDYMPIFQVNLIGLTQVTISMLFLVKKARG-RIVNVSSAlgrVALFG----GF 175
Cdd:PRK08267  75 ggrldvLFNNAGILRggPFEDIP---LEAHDRVIDINVKGVLNGAHAALPYLKATPGaRVINTSSA---SAIYGqpglAV 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755534620 176 YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERT----------------KKVWEAA 230
Cdd:PRK08267 149 YSATKFAVRGLTEALDLEWRRHGIRVADVMPLFVDTAMLDGTSNEVDAgstkrlgvrltpedvaEAVWAAV 219
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
24-240 3.55e-16

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 76.58  E-value: 3.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  24 VSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEK-GAEELRNKTSDRLETVIL---DVTKTESivaATQWVKE 99
Cdd:PRK12935   1 MVQLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKeAAENLVNELGKEGHDVYAvqaDVSKVED---ANRLVEE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 100 RVGDRG-LWGLVNNAGVLQPFAYIEWYRpEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVALFGGF-Y 176
Cdd:PRK12935  78 AVNHFGkVDILVNNAGITRDRTFKKLNR-EDWERVIDVNLSSVFNTTSAVLpYITEAEEGRIISISSIIGQAGGFGQTnY 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755534620 177 SCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTdAELTIERTKKVWEAAPehiKESYGQ 240
Cdd:PRK12935 157 SAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMV-AEVPEEVRQKIVAKIP---KKRFGQ 216
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
27-213 3.84e-16

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


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 76.34  E-value: 3.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVI-LDVTKTESIVAATQWVKERVGDrg 105
Cdd:cd05326    2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFVhCDVTVEADVRAAVDTAVARFGR-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 106 LWGLVNNAGVLQPFAY-IEWYRPEDYMPIFQVNLIGLTQVTI-SMLFLVKKARGRIVNVSSALGRVALFGGF-YSCSKYG 182
Cdd:cd05326   80 LDIMFNNAGVLGAPCYsILETSLEEFERVLDVNVYGAFLGTKhAARVMIPAKKGSIVSVASVAGVVGGLGPHaYTASKHA 159
                        170       180       190
                 ....*....|....*....|....*....|.
gi 755534620 183 VEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:cd05326  160 VLGLTRSAATELGEHGIRVNCVSPYGVATPL 190
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
32-207 5.58e-16

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 75.95  E-value: 5.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVgdRGLWGLVN 111
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEW--RNIDVLVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 112 NAGV---LQPfAYIEwyRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVALFGG-FYSCSKYGVEAF 186
Cdd:PRK10538  81 NAGLalgLEP-AHKA--SVEDWETMIDTNNKGLVYMTRAVLpGMVERNHGHIINIGSTAGSWPYAGGnVYGATKAFVRQF 157
                        170       180
                 ....*....|....*....|.
gi 755534620 187 SDVLRHEVQDFGVKVSIIEPG 207
Cdd:PRK10538 158 SLNLRTDLHGTAVRVTDIEPG 178
PRK08589 PRK08589
SDR family oxidoreductase;
27-215 5.62e-16

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 76.36  E-value: 5.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELR--NKTSDRLETVILDVTKTESIVAATQWVKERVGDR 104
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDkiKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 105 GLwgLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKARGRIVNVSSALGRVA-LFGGFYSCSKYGV 183
Cdd:PRK08589  84 DV--LFNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAAdLYRSGYNAAKGAV 161
                        170       180       190
                 ....*....|....*....|....*....|..
gi 755534620 184 EAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTD 215
Cdd:PRK08589 162 INFTKSIAIEYGRDGIRANAIAPGTIETPLVD 193
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
27-215 1.01e-15

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 75.31  E-value: 1.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGA---EELRNKTSDRLETVILDVTKTESIVAATQWVKERVGd 103
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAaaaAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFG- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 rGLWGLVNNAGvLQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKAR-GRIVNVSSALGRVALFG-GFYSCSKY 181
Cdd:PRK12429  81 -GVDILVNNAG-IQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGgGRIINMASVHGLVGSAGkAAYVSAKH 158
                        170       180       190
                 ....*....|....*....|....*....|....
gi 755534620 182 GVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTD 215
Cdd:PRK12429 159 GLIGLTKVVALEGATHGVTVNAICPGYVDTPLVR 192
PRK07060 PRK07060
short chain dehydrogenase; Provisional
30-216 1.57e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 74.75  E-value: 1.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDrlETVILDVTKTESIVAATQwvkervGDRGLWGL 109
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGC--EPLRLDVGDDAAIRAALA------AAGAFDGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 110 VNNAG--VLQPFAYIEwyrPEDYMPIFQVNLIGLtqvtismlFLVKK--ARGR--------IVNVSSALGRVAL-FGGFY 176
Cdd:PRK07060  82 VNCAGiaSLESALDMT---AEGFDRVMAVNARGA--------ALVARhvARAMiaagrggsIVNVSSQAALVGLpDHLAY 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755534620 177 SCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDA 216
Cdd:PRK07060 151 CASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPMAAE 190
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
27-213 1.88e-15

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 74.52  E-value: 1.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacltekgaeeLRNKTSDRLETV---------------ILD---VTKTE 88
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVI-----------LLGRTEEKLEAVydeieaaggpqpaiiPLDlltATPQN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  89 SI-VAATqwVKERVGDrgLWGLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIG---LTQvtiSMLFLVKKAR-GRIVNVS 163
Cdd:PRK08945  79 YQqLADT--IEEQFGR--LDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNAtfmLTQ---ALLPLLLKSPaASLVFTS 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755534620 164 SALGRVA-LFGGFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:PRK08945 152 SSVGRQGrANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAM 202
dhbA_paeA TIGR04316
2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase; Members of this family are 2,3-dihydro-2, ...
32-213 2.03e-15

2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase; Members of this family are 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (EC 1.3.1.28), the third enzyme in the biosynthesis of 2,3-dihydroxybenzoic acid (DHB) from chorismate. The first two enzymes are isochorismate synthase (EC 5.4.4.2) and isochorismatase (EC 3.3.2.1). Synthesis is often followed by adenylation by the enzyme DHBA-AMP ligase (EC 2.7.7.58) to activate (DHB) for a non-ribosomal peptide synthetase.


Pssm-ID: 275120 [Multi-domain]  Cd Length: 250  Bit Score: 74.25  E-value: 2.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620   32 VFITGCDSGFGNLLARQLDRRGMRVLAaclTEKGAEELRNKTSD------RLETVILDVTKTESIVAATQWVKERVGdrG 105
Cdd:TIGR04316   1 VLVTGAAQGIGYAVARALAEAGARVAA---VDRNFEQLLELVADlrrygyPFATYKLDVADSAAVDEVVQRLEREYG--P 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  106 LWGLVNNAGVLQpFAYIEWYRPEDYMPIFQVNLIG----LTQVTISMlflVKKARGRIVNVSSALGRVALFG-GFYSCSK 180
Cdd:TIGR04316  76 IDVLVNVAGILR-LGAIDSLSDEDWQATFAVNTFGvfnvSQAVSPRM---KRRRSGAIVTVGSNAANVPRMGmAAYAASK 151
                         170       180       190
                  ....*....|....*....|....*....|...
gi 755534620  181 YGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:TIGR04316 152 AALTMLTKCLGLELAPYGIRCNVVSPGSTDTEM 184
PRK07774 PRK07774
SDR family oxidoreductase;
27-214 2.04e-15

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 74.40  E-value: 2.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVI---LDVTKTESIVAATQWVKERVGd 103
Cdd:PRK07774   4 FDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIavqVDVSDPDSAKAMADATVSAFG- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 rGLWGLVNNAGV-----LQPFAYIEWyrpEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGrvALFGGFYS 177
Cdd:PRK07774  83 -GIDYLVNNAAIyggmkLDLLITVPW---DYYKKFMSVNLDGALVCTRAVYkHMAKRGGGAIVNQSSTAA--WLYSNFYG 156
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 755534620 178 CSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMT 214
Cdd:PRK07774 157 LAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEAT 193
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
30-244 3.47e-15

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


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 73.95  E-value: 3.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACL----TEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGDrg 105
Cdd:cd05366    3 KVAIITGAAQGIGRAIAERLAADGFNIVLADLnleeAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFGS-- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 106 LWGLVNNAGV--LQPFAYIEwyrPEDYMPIFQVNLIGLtqvtismLFLVKKA---------RGRIVNVSSALGRVALFG- 173
Cdd:cd05366   81 FDVMVNNAGIapITPLLTIT---EEDLKKVYAVNVFGV-------LFGIQAAarqfkklghGGKIINASSIAGVQGFPNl 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755534620 174 GFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDaelTIERtkKVWEAAPEhiKESYGQQFFD 244
Cdd:cd05366  151 GAYSASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMWD---YIDE--EVGEIAGK--PEGEGFAEFS 214
PRK05855 PRK05855
SDR family oxidoreductase;
29-215 4.29e-15

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 75.40  E-value: 4.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEElrnkTSDRLE-------TVILDVTKTESIVAATQWVKERV 101
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAER----TAELIRaagavahAYRVDVSDADAMEAFAEWVRAEH 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 102 G--DRglwgLVNNAGVLQ--PFAYIEwyrPEDYMPIFQVNLIGLtqVTISMLF---LVKKAR-GRIVNVSSAlgrvALFG 173
Cdd:PRK05855 391 GvpDI----VVNNAGIGMagGFLDTS---AEDWDRVLDVNLWGV--IHGCRLFgrqMVERGTgGHIVNVASA----AAYA 457
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 755534620 174 -----GFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTD 215
Cdd:PRK05855 458 psrslPAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVA 504
PRK06841 PRK06841
short chain dehydrogenase; Provisional
27-213 5.22e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 73.15  E-value: 5.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGdrGL 106
Cdd:PRK06841  13 LSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFG--RI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 WGLVNNAGVLqPFAYIEWYRPEDYMPIFQVNLIG---LTQ-VTISMLflvKKARGRIVNVSSALGRVALFGGF-YSCSKY 181
Cdd:PRK06841  91 DILVNSAGVA-LLAPAEDVSEEDWDKTIDINLKGsflMAQaVGRHMI---AAGGGKIVNLASQAGVVALERHVaYCASKA 166
                        170       180       190
                 ....*....|....*....|....*....|..
gi 755534620 182 GVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:PRK06841 167 GVVGMTKVLALEWGPYGITVNAISPTVVLTEL 198
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
27-231 8.88e-15

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 72.67  E-value: 8.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEELRNK----TSDRLETVIL--DVTKTESIVAATQWVKER 100
Cdd:PRK08213  10 LSGKTALVTGGSRGLGLQIAEALGEAGARVV---LSARKAEELEEAaahlEALGIDALWIaaDVADEADIERLAEETLER 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 101 VGDRGLwgLVNNAGVlqpfayiEWYRPEDYMP------IFQVNLIG---LTQVtISMLFLVKKARGRIVNVSSalgrVAL 171
Cdd:PRK08213  87 FGHVDI--LVNNAGA-------TWGAPAEDHPveawdkVMNLNVRGlflLSQA-VAKRSMIPRGYGRIINVAS----VAG 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 172 FGG---------FYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTdaELTIERT-KKVWEAAP 231
Cdd:PRK08213 153 LGGnppevmdtiAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMT--RGTLERLgEDLLAHTP 220
PRK06484 PRK06484
short chain dehydrogenase; Validated
32-211 9.05e-15

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 74.50  E-value: 9.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGDRGLwgLVN 111
Cdd:PRK06484 272 VAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRLDV--LVN 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 112 NAGVLQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKArGRIVNVSSALGRVALFG-GFYSCSKYGVEAFSDVL 190
Cdd:PRK06484 350 NAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG-GVIVNLGSIASLLALPPrNAYCASKAAVTMLSRSL 428
                        170       180
                 ....*....|....*....|.
gi 755534620 191 RHEVQDFGVKVSIIEPGSFKT 211
Cdd:PRK06484 429 ACEWAPAGIRVNTVAPGYIET 449
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
27-218 9.41e-15

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


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 72.52  E-value: 9.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGdrGL 106
Cdd:cd08944    1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFG--GL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 WGLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGlTQVTI--SMLFLVKKARGRIVNVSSALGRVALFG-GFYSCSKYGV 183
Cdd:cd08944   79 DLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRG-TFLCCrhAAPRMIARGGGSIVNLSSIAGQSGDPGyGAYGASKAAI 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 755534620 184 EAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAEL 218
Cdd:cd08944  158 RNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKL 192
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
23-218 1.10e-14

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 72.62  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  23 VVSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAE---ELRNKTSDRLETVILDVTKTESIVAATQWVKE 99
Cdd:PRK13394   1 MMSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANavaDEINKAGGKAIGVAMDVTNEDAVNAGIDKVAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 100 RVGDRGLwgLVNNAGVlQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKAR--GRIVNVSSALGRVALFG-GFY 176
Cdd:PRK13394  81 RFGSVDI--LVSNAGI-QIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHSHEASPLkSAY 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 755534620 177 SCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAEL 218
Cdd:PRK13394 158 VTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQI 199
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
30-252 1.10e-14

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 72.45  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLE---TVILDVTKTESIVAATQWVKERVGDrgL 106
Cdd:PRK08643   3 KVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGkaiAVKADVSDRDQVFAAVRQVVDTFGD--L 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 WGLVNNAGVlQPFAYIEWYRPEDYMPIFQVNLIGL---TQVTISmLFLVKKARGRIVNVSSALGRVALFG-GFYSCSKYG 182
Cdd:PRK08643  81 NVVVNNAGV-APTTPIETITEEQFDKVYNINVGGViwgIQAAQE-AFKKLGHGGKIINATSQAGVVGNPElAVYSSTKFA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755534620 183 VEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDaeltiERTKKVWEAAPEhiKESYG-QQFFDDFcsTTKR 252
Cdd:PRK08643 159 VRGLTQTAARDLASEGITVNAYAPGIVKTPMMF-----DIAHQVGENAGK--PDEWGmEQFAKDI--TLGR 220
PRK06484 PRK06484
short chain dehydrogenase; Validated
28-226 1.13e-14

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 74.12  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGDRGLw 107
Cdd:PRK06484   4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDV- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 108 gLVNNAGVLQPF--AYIEwYRPEDYMPIFQVNLIGLTQVTISMLFLVKKAR--GRIVNVSSALGRVALFG-GFYSCSKYG 182
Cdd:PRK06484  83 -LVNNAGVTDPTmtATLD-TTLEEFARLQAINLTGAYLVAREALRLMIEQGhgAAIVNVASGAGLVALPKrTAYSASKAA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 755534620 183 VEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTdAELtiERTKKV 226
Cdd:PRK06484 161 VISLTRSLACEWAAKGIRVNAVLPGYVRTQMV-AEL--ERAGKL 201
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
26-216 1.37e-14

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 71.92  E-value: 1.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRvLAacLTEKGAEELRNKTSD------RLETVILDVTKTESIVAATQWVKE 99
Cdd:PRK08217   2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAK-LA--LIDLNQEKLEEAVAEcgalgtEVRGYAANVTDEEDVEATFAQIAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 100 RVGdrGLWGLVNNAGVLQpfayiewyrpeDYMPI---------------FQ----VNLIG--LT--QVTISMLFLVKKar 156
Cdd:PRK08217  79 DFG--QLNGLINNAGILR-----------DGLLVkakdgkvtskmsleqFQsvidVNLTGvfLCgrEAAAKMIESGSK-- 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755534620 157 GRIVNVSSalgrVALFGGF----YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDA 216
Cdd:PRK08217 144 GVIINISS----IARAGNMgqtnYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAA 203
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
27-238 2.02e-14

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 71.97  E-value: 2.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEElrnktsDRLETVILDVTKTESIVAATQWVKERVGdrGL 106
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQH------ENYQFVPTDVSSAEEVNHTVAEIIEKFG--RI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 WGLVNNAGVLQPFAYIEWYRPE--------DYMPIFQVNLIGLTQVT-ISMLFLVKKARGRIVNVSSALGRVALFG-GFY 176
Cdd:PRK06171  79 DGLVNNAGINIPRLLVDEKDPAgkyelneaAFDKMFNINQKGVFLMSqAVARQMVKQHDGVIVNMSSEAGLEGSEGqSCY 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755534620 177 SCSKYGVEAFSDVLRHEVQDFGVKV-----SIIEPGSFKTEMTDAELTIERTKKVweaapEHIKESY 238
Cdd:PRK06171 159 AATKAALNSFTRSWAKELGKHNIRVvgvapGILEATGLRTPEYEEALAYTRGITV-----EQLRAGY 220
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
27-213 2.09e-14

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 71.45  E-value: 2.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRnktsdrLETVILDVTKTESIVAATQWVKERVGdrGL 106
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDYP------FATFVLDVSDAAAVAQVCQRLLAETG--PL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 WGLVNNAGVLQPFAyIEWYRPEDYMPIFQVNLIG----LTQVTISMlflVKKARGRIVNVSSALGRVALFG-GFYSCSKY 181
Cdd:PRK08220  78 DVLVNAAGILRMGA-TDSLSDEDWQQTFAVNAGGafnlFRAVMPQF---RRQRSGAIVTVGSNAAHVPRIGmAAYGASKA 153
                        170       180       190
                 ....*....|....*....|....*....|..
gi 755534620 182 GVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:PRK08220 154 ALTSLAKCVGLELAPYGVRCNVVSPGSTDTDM 185
PRK07023 PRK07023
SDR family oxidoreductase;
34-213 2.64e-14

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 71.20  E-value: 2.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  34 ITGCDSGFGNLLARQLDRRGMRVLaaCLTEKGAEELRNKTSDRLETVILDVTKTEsivAATQWVKERVGDRGLWG----- 108
Cdd:PRK07023   6 VTGHSRGLGAALAEQLLQPGIAVL--GVARSRHPSLAAAAGERLAEVELDLSDAA---AAAAWLAGDLLAAFVDGasrvl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 109 LVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKK-ARGRIVNVSSALGRVALFG-GFYSCSKYGVEAF 186
Cdd:PRK07023  81 LINNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDaAERRILHISSGAARNAYAGwSVYCATKAALDHH 160
                        170       180
                 ....*....|....*....|....*..
gi 755534620 187 SDVLRHEvQDFGVKVSIIEPGSFKTEM 213
Cdd:PRK07023 161 ARAVALD-ANRALRIVSLAPGVVDTGM 186
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
33-236 3.31e-14

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


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 71.03  E-value: 3.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  33 FITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEELRnKTSDRLETVIL-------DVTKTESIVAATQWVKERVGDRG 105
Cdd:cd08945    7 LVTGATSGIGLAIARRLGKEGLRVF---VCARGEEGLA-TTVKELREAGVeadgrtcDVRSVPEIEALVAAAVARYGPID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 106 LwgLVNNAGVLQPFAyIEWYRPEDYMPIFQVNLIGLTQVTISMLF---LVKKARGRIVNVSSALGRVA-LFGGFYSCSKY 181
Cdd:cd08945   83 V--LVNNAGRSGGGA-TAELADELWLDVVETNLTGVFRVTKEVLKaggMLERGTGRIINIASTGGKQGvVHAAPYSASKH 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755534620 182 GVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMtdAELTIERTKKVWEAAPEHIKE 236
Cdd:cd08945  160 GVVGFTKALGLELARTGITVNAVCPGFVETPM--AASVREHYADIWEVSTEEAFD 212
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
30-213 4.02e-14

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 70.87  E-value: 4.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE-KGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGDRGLWG 108
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTEnKELTKLAEQYNSNLTFHSLDLQDVHELETNFNEILSSIQEDNVSS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 109 --LVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIG---LTQVTISML--FLVKKargRIVNVSSALGRVALFG-GFYSCSK 180
Cdd:PRK06924  82 ihLINNAGMVAPIKPIEKAESEELITNVHLNLLApmiLTSTFMKHTkdWKVDK---RVINISSGAAKNPYFGwSAYCSSK 158
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 755534620 181 YGVEAFSDVLRHEVQD--FGVKVSIIEPGSFKTEM 213
Cdd:PRK06924 159 AGLDMFTQTVATEQEEeeYPVKIVAFSPGVMDTNM 193
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
32-213 5.36e-14

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


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 70.19  E-value: 5.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLtekgAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGdrGLWGLVN 111
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIALDL----PFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHG--PIDALVN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 112 NAGVLQPfAYIEWYRPEDYMPIFQVNLIG----LTQVTISMlflvkKAR--GRIVNVSSALGRVALFG-GFYSCSKYGVE 184
Cdd:cd05331   75 CAGVLRP-GATDPLSTEDWEQTFAVNVTGvfnlLQAVAPHM-----KDRrtGAIVTVASNAAHVPRISmAAYGASKAALA 148
                        170       180
                 ....*....|....*....|....*....
gi 755534620 185 AFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:cd05331  149 SLSKCLGLELAPYGVRCNVVSPGSTDTAM 177
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
27-216 5.66e-14

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


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 70.52  E-value: 5.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVlaaCLTEKGAEEL---------RNKTSDRLETVILDVTKTESIVAATQWV 97
Cdd:cd05364    1 LSGKVAIITGSSSGIGAGTAILFARLGARL---ALTGRDAERLeetrqsclqAGVSEKKILLVVADLTEEEGQDRIISTT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  98 KERVGDRGLwgLVNNAGVLQPFAyIEWYRPEDYMPIFQVNL---IGLTQVTISMLflvKKARGRIVNVSSALGRVAlFGG 174
Cdd:cd05364   78 LAKFGRLDI--LVNNAGILAKGG-GEDQDIEEYDKVMNLNLravIYLTKLAVPHL---IKTKGEIVNVSSVAGGRS-FPG 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 755534620 175 F--YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDA 216
Cdd:cd05364  151 VlyYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRR 194
PRK07024 PRK07024
SDR family oxidoreductase;
32-215 8.15e-14

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 69.96  E-value: 8.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRGMRV-LAACLTE---KGAEELRNktSDRLETVILDVTKTESIVAATQWVKERVGDRGLw 107
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLgLVARRTDalqAFAARLPK--AARVSVYAADVRDADALAAAAADFIAAHGLPDV- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 108 gLVNNAGV-----------LQPFAyiewyrpedymPIFQVNLIGLtqVTISMLFL---VKKARGRIVNVSSALGRVALFG 173
Cdd:PRK07024  82 -VIANAGIsvgtlteeredLAVFR-----------EVMDTNYFGM--VATFQPFIapmRAARRGTLVGIASVAGVRGLPG 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 755534620 174 -GFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTD 215
Cdd:PRK07024 148 aGAYSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPMTA 190
PRK06949 PRK06949
SDR family oxidoreductase;
27-233 8.78e-14

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 69.79  E-value: 8.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV-LAACLTEKgAEELRNKTSDR---LETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVvLASRRVER-LKELRAEIEAEggaAHVVSLDVTDYQSIKAAVAHAETEAG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 DRGLwgLVNNAGVLQPFAYIEwYRPEDYMPIFQVNLIG----LTQVTISMLFLVK-----KARGRIVNVSSALG-RVALF 172
Cdd:PRK06949  86 TIDI--LVNNSGVSTTQKLVD-VTPADFDFVFDTNTRGaffvAQEVAKRMIARAKgagntKPGGRIINIASVAGlRVLPQ 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755534620 173 GGFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERTKKVWEAAPEH 233
Cdd:PRK06949 163 IGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWETEQGQKLVSMLPRK 223
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
27-238 1.13e-13

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 69.14  E-value: 1.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEELRnKTSDRLET--------VILDVTK--TESIVAATQW 96
Cdd:cd05340    2 LNDRIILVTGASDGIGREAALTYARYGATVI---LLGRNEEKLR-QVADHINEeggrqpqwFILDLLTctSENCQQLAQR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  97 VKERVGDrgLWGLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKAR-GRIVNVSSALGRV-ALFGG 174
Cdd:cd05340   78 IAVNYPR--LDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQgRANWG 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755534620 175 FYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERTKKVweAAPEHIKESY 238
Cdd:cd05340  156 AYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRASAFPTEDPQKL--KTPADIMPLY 217
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
27-242 1.42e-13

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


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 69.47  E-value: 1.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD-----RLETVILDVTKTESIVAATQWVKERV 101
Cdd:cd05330    1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEiapdaEVLLIKADVSDEAQVEAYVDATVEQF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 102 GDrgLWGLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGltqVTISMLFLVKKAR----GRIVNVSSALG-RVALFGGFY 176
Cdd:cd05330   81 GR--IDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRG---VFYGLEKVLKVMReqgsGMIVNTASVGGiRGVGNQSGY 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755534620 177 SCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTiertkkvwEAAPEHIKESyGQQF 242
Cdd:cd05330  156 AAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSLK--------QLGPENPEEA-GEEF 212
PRK07775 PRK07775
SDR family oxidoreductase;
25-219 1.49e-13

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 69.40  E-value: 1.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  25 SHLQDKYVFITGCDSGFGNLLARQLDRRGMRV-LAACLTEKGAEELRNKTSDRLETVI--LDVTKTESIVAATQWVKERV 101
Cdd:PRK07775   6 PHPDRRPALVAGASSGIGAATAIELAAAGFPVaLGARRVEKCEELVDKIRADGGEAVAfpLDVTDPDSVKSFVAQAEEAL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 102 GDRGLwgLVNNAGVLQPFAYIEwYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSalgRVAL----FGGFY 176
Cdd:PRK07775  86 GEIEV--LVSGAGDTYFGKLHE-ISTEQFESQVQIHLVGANRLATAVLpGMIERRRGDLIFVGS---DVALrqrpHMGAY 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755534620 177 SCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM---TDAELT 219
Cdd:PRK07775 160 GAAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGMgwsLPAEVI 205
PRK06139 PRK06139
SDR family oxidoreductase;
27-197 2.59e-13

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 69.36  E-value: 2.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMR-VLAACLTE---KGAEELRNKTSDRLeTVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK06139   5 LHGAVVVITGASSGIGQATAEAFARRGARlVLAARDEEalqAVAEECRALGAEVL-VVPTDVTDADQVKALATQAASFGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 DRGLWglVNNAGVLQPFAYIEwyRP-EDYMPIFQVNLIG-LTQVTISMLFLVKKARGRIVNVSSALGRVAL-FGGFYSCS 179
Cdd:PRK06139  84 RIDVW--VNNVGVGAVGRFEE--TPiEAHEQVIQTNLIGyMRDAHAALPIFKKQGHGIFINMISLGGFAAQpYAAAYSAS 159
                        170
                 ....*....|....*...
gi 755534620 180 KYGVEAFSDVLRHEVQDF 197
Cdd:PRK06139 160 KFGLRGFSEALRGELADH 177
PRK08251 PRK08251
SDR family oxidoreductase;
30-215 3.47e-13

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 68.04  E-value: 3.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGmRVLAAC------LTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVG- 102
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKG-RDLALCarrtdrLEELKAELLARYPGIKVAVAALDVNDHDQVFEVFAEFRDELGg 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 -DRglwgLVNNAGvLQPFAYIEWYRPEDYMPIFQVNLIG-LTQVTISMLFLVKKARGRIVNVSSALGRVALFGGF--YSC 178
Cdd:PRK08251  82 lDR----VIVNAG-IGKGARLGTGKFWANKATAETNFVAaLAQCEAAMEIFREQGSGHLVLISSVSAVRGLPGVKaaYAA 156
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 755534620 179 SKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTD 215
Cdd:PRK08251 157 SKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNA 193
PRK07063 PRK07063
SDR family oxidoreductase;
27-232 3.78e-13

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 68.15  E-value: 3.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV----LAACLTEKGAEELRNKTSD-RLETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK07063   5 LAGKVALVTGAAQGIGAAIARAFAREGAAValadLDAALAERAAAAIARDVAGaRVLAVPADVTDAASVAAAVAAAEEAF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 102 GdrGLWGLVNNAGV---LQPFAYIEwyrpEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVALFGGF-Y 176
Cdd:PRK07063  85 G--PLDVLVNNAGInvfADPLAMTD----EDWRRCFAVDLDGAWNGCRAVLpGMVERGRGSIVNIASTHAFKIIPGCFpY 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755534620 177 SCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAeltiertkkVWEAAPE 232
Cdd:PRK07063 159 PVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTED---------WWNAQPD 205
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
29-235 4.18e-13

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


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 67.68  E-value: 4.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG----AEELRnKTSDRLETVILDVTKTESIVAATQWVKERVGdr 104
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENleraASELR-AGGAGVLAVVADLTDPEDIDRLVEKAGDAFG-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 105 GLWGLVNNAGVLQPFAYIEWyRPEDYMPIFQVNLIGLTQVTISMLFLVKKAR-GRIVNVSSALGRVALFGGFYS-CSKYG 182
Cdd:cd05344   78 RVDILVNNAGGPPPGPFAEL-TDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLTVKEPEPNLVLSnVARAG 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755534620 183 VEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTdAELTIERTKK----VWEAAPEHIK 235
Cdd:cd05344  157 LIGLVKTLSRELAPDGVTVNSVLPGYIDTERV-RRLLEARAEKegisVEEAEKEVAS 212
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
30-213 5.83e-13

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


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 67.47  E-value: 5.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVL------AACLtEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGd 103
Cdd:cd08940    3 KVALVTGSTSGIGLGIARALAAAGANIVlngfgdAAEI-EAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFG- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 rGLWGLVNNAGVlQPFAYIEWYRPEDYMPIFQVNligLTQV--TISMLFLVKKAR--GRIVNVSSALGRVA-LFGGFYSC 178
Cdd:cd08940   81 -GVDILVNNAGI-QHVAPIEDFPTEKWDAIIALN---LSAVfhTTRLALPHMKKQgwGRIINIASVHGLVAsANKSAYVA 155
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 755534620 179 SKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:cd08940  156 AKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPL 190
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
27-238 6.54e-13

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


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 67.36  E-value: 6.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV----LAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:cd05352    6 LKGKVAIVTGGSRGIGLAIARALAEAGADVaiiyNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 DrgLWGLVNNAGVLQPFAyIEWYRPEDYMPIFQVNLIGLTQVTISM-LFLVKKARGRIVNVSSALGRVALFG---GFYSC 178
Cdd:cd05352   86 K--IDILIANAGITVHKP-ALDYTYEQWNKVIDVNLNGVFNCAQAAaKIFKKQGKGSLIITASMSGTIVNRPqpqAAYNA 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755534620 179 SKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAelTIERTKKVWE--------AAPEHIKESY 238
Cdd:cd05352  163 SKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDF--VDKELRKKWEsyiplkriALPEELVGAY 228
PRK12743 PRK12743
SDR family oxidoreductase;
28-217 6.62e-13

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 67.37  E-value: 6.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  28 QDKYVFITGCDSGFGNLLARQLDRRGMRVlaaCLT----EKGA----EELRnKTSDRLETVILDVTKTESIVAATQWVKE 99
Cdd:PRK12743   1 MAQVAIVTASDSGIGKACALLLAQQGFDI---GITwhsdEEGAketaEEVR-SHGVRAEIRQLDLSDLPEGAQALDKLIQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 100 RVGdrGLWGLVNNAGVL--QPFAYIEWyrpEDYMPIFQVNLIGltqvtiSMLFLVKKAR--------GRIVNVSSALGRV 169
Cdd:PRK12743  77 RLG--RIDVLVNNAGAMtkAPFLDMDF---DEWRKIFTVDVDG------AFLCSQIAARhmvkqgqgGRIINITSVHEHT 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 755534620 170 ALFG-GFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAE 217
Cdd:PRK12743 146 PLPGaSAYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIATPMNGMD 194
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
30-213 6.79e-13

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 67.49  E-value: 6.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACL----TEKGAEELRNKTSDRLETVI-LDVTKTESIVA-ATQWVKERvgD 103
Cdd:cd09807    2 KTVIITGANTGIGKETARELARRGARVIMACRdmakCEEAAAEIRRDTLNHEVIVRhLDLASLKSIRAfAAEFLAEE--D 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 RgLWGLVNNAGVLQ-PFayieWYRPEDYMPIFQVNLIGLTQVTISMLFLVKK-ARGRIVNVSSAL---GRVAL------- 171
Cdd:cd09807   80 R-LDVLINNAGVMRcPY----SKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKsAPSRIVNVSSLAhkaGKINFddlnsek 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 755534620 172 ---FGGFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:cd09807  155 synTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTEL 199
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
27-243 8.02e-13

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


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 67.48  E-value: 8.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLT-EKG---AEELRNK--TSDRLETvilDVTKTESIVAATQWVKER 100
Cdd:cd08935    3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNqEKGdkvAKEITALggRAIALAA---DVLDRASLERAREEIVAQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 101 VGDRGLwgLVNNAGVLQPFAYI--EWYRP-----------EDYMPIFQVNLIGltQVTISMLF---LVKKARGRIVNVSS 164
Cdd:cd08935   80 FGTVDI--LINGAGGNHPDATTdpEHYEPeteqnffdldeEGWEFVFDLNLNG--SFLPSQVFgkdMLEQKGGSIINISS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 165 -----ALGRVALfggfYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTI------ERTKKVWEAAPE- 232
Cdd:cd08935  156 mnafsPLTKVPA----YSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLLINpdgsytDRSNKILGRTPMg 231
                        250
                 ....*....|....
gi 755534620 233 ---HIKESYGQQFF 243
Cdd:cd08935  232 rfgKPEELLGALLF 245
PRK09242 PRK09242
SDR family oxidoreductase;
27-234 8.35e-13

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 67.08  E-value: 8.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD-----RLETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK09242   7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEefperEVHGLAADVSDDEDRRAILDWVEDHW 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 102 GdrGLWGLVNNAGVLQPFAYIEwYRPEDYMPIFQVNLIGLTQvtISMLF---LVKKARGRIVNVSSALGRVAL-FGGFYS 177
Cdd:PRK09242  87 D--GLHILVNNAGGNIRKAAID-YTEDEWRGIFETNLFSAFE--LSRYAhplLKQHASSAIVNIGSVSGLTHVrSGAPYG 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755534620 178 CSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELT--------IERT--KKVWEaaPEHI 234
Cdd:PRK09242 162 MTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSdpdyyeqvIERTpmRRVGE--PEEV 226
PRK06114 PRK06114
SDR family oxidoreductase;
27-231 9.62e-13

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 66.73  E-value: 9.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVlaACLTEKGAEELRnKTSDRLET-------VILDVTKTESIVAATQWVKE 99
Cdd:PRK06114   6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADV--ALFDLRTDDGLA-ETAEHIEAagrraiqIAADVTSKADLRAAVARTEA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 100 RVGdrGLWGLVNNAGVLQPFAYIEwYRPEDYMPIFQVNLIGltqVTIS-------MLflvKKARGRIVNVSSALGRVA-- 170
Cdd:PRK06114  83 ELG--ALTLAVNAAGIANANPAEE-MEEEQWQTVMDINLTG---VFLScqaearaML---ENGGGSIVNIASMSGIIVnr 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755534620 171 -LFGGFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERTKKVWEAAP 231
Cdd:PRK06114 154 gLLQAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTRPEMVHQTKLFEEQTP 215
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
27-231 1.01e-12

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


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 66.70  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDR---LETVILDVTKTESIVAATQWVKERVGD 103
Cdd:cd05329    4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKgfkVEGSVCDVSSRSERQELMDTVASHFGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 RgLWGLVNNAGVLQPFAYIEwYRPEDYMPIFQVNLIG---LTQvtISMLFLVKKARGRIVNVSSALGRVAL-FGGFYSCS 179
Cdd:cd05329   84 K-LNILVNNAGTNIRKEAKD-YTEEDYSLIMSTNFEAayhLSR--LAHPLLKASGNGNIVFISSVAGVIAVpSGAPYGAT 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755534620 180 KYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELT-IERTKKVWEAAP 231
Cdd:cd05329  160 KGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQqKENLDKVIERTP 212
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
27-213 1.13e-12

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 66.34  E-value: 1.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDrLETVILDVtktesivAATQWVKERVGDRGL 106
Cdd:cd05351    5 FAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPG-IEPVCVDL-------SDWDATEEALGSVGP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 W-GLVNNAGV--LQPFAYIEwyrPEDYMPIFQVNLIGLTQVTISML--FLVKKARGRIVNVSSALGRVALFG-GFYSCSK 180
Cdd:cd05351   77 VdLLVNNAAVaiLQPFLEVT---KEAFDRSFDVNVRAVIHVSQIVArgMIARGVPGSIVNVSSQASQRALTNhTVYCSTK 153
                        170       180       190
                 ....*....|....*....|....*....|...
gi 755534620 181 YGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:cd05351  154 AALDMLTKVMALELGPHKIRVNSVNPTVVMTDM 186
PRK05866 PRK05866
SDR family oxidoreductase;
27-213 1.54e-12

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 66.69  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDR---LETVILDVTKTESIVAATQWVKERVGd 103
Cdd:PRK05866  38 LTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAggdAMAVPCDLSDLDAVDALVADVEKRIG- 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 rGLWGLVNNAG--VLQPFA--YIEWYRPEDYMpifQVNLIGLTQVTISML-FLVKKARGRIVNVSS---ALGRVALFgGF 175
Cdd:PRK05866 117 -GVDILINNAGrsIRRPLAesLDRWHDVERTM---VLNYYAPLRLIRGLApGMLERGDGHIINVATwgvLSEASPLF-SV 191
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 755534620 176 YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:PRK05866 192 YNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPM 229
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
27-233 1.73e-12

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 66.09  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV-LAACLTEKgAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGdrG 105
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVgLHGTRVEK-LEALAAELGERVKIFPANLSDRDEVKALGQKAEADLE--G 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 106 LWGLVNNAGVLQPFAYIEwYRPEDYMPIFQVNLIGLTQVTISMLF-LVKKARGRIVNVSSALGRVALFG-GFYSCSKYGV 183
Cdd:PRK12936  81 VDILVNNAGITKDGLFVR-MSDEDWDSVLEVNLTATFRLTRELTHpMMRRRYGRIINITSVVGVTGNPGqANYCASKAGM 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 755534620 184 EAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDaELTIERTKKVWEAAPEH 233
Cdd:PRK12936 160 IGFSKSLAQEIATRNVTVNCVAPGFIESAMTG-KLNDKQKEAIMGAIPMK 208
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
29-219 2.16e-12

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 65.37  E-value: 2.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGaeelrnKTSDRLETVILDVTKTESivAATQWVKErvgdrgLWG 108
Cdd:PRK06550   5 TKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDKP------DLSGNFHFLQLDLSDDLE--PLFDWVPS------VDI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 109 LVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRVALFGGF-YSCSKYGVEAF 186
Cdd:PRK06550  71 LCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLpQMLERKSGIIINMCSIASFVAGGGGAaYTASKHALAGF 150
                        170       180       190
                 ....*....|....*....|....*....|...
gi 755534620 187 SDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELT 219
Cdd:PRK06550 151 TKQLALDYAKDGIQVFGIAPGAVKTPMTAADFE 183
PRK07890 PRK07890
short chain dehydrogenase; Provisional
27-207 2.60e-12

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 65.75  E-value: 2.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKERVGd 103
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDlgrRALAVPTDITDEDQCANLVALALERFG- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 rGLWGLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKARGRIVNVSSALGR--VALFGGfYSCSKY 181
Cdd:PRK07890  82 -RVDALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMINSMVLRhsQPKYGA-YKMAKG 159
                        170       180
                 ....*....|....*....|....*.
gi 755534620 182 GVEAFSDVLRHEVQDFGVKVSIIEPG 207
Cdd:PRK07890 160 ALLAASQSLATELGPQGIRVNSVAPG 185
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
34-241 2.87e-12

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: 65.39  E-value: 2.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  34 ITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRnKTSDRLETVILDVTKTESIVAATQWVKERVGdrGLWGLVNNA 113
Cdd:cd05371    7 VTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVA-KLGDNCRFVPVDVTSEKDVKAALALAKAKFG--RLDIVVNCA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 114 GV-----------LQPFayiewyRPEDYMPIFQVNLIGltqvTISMLFLVKKA-----------RGRIVNVSSalgrVAL 171
Cdd:cd05371   84 GIavaaktynkkgQQPH------SLELFQRVINVNLIG----TFNVIRLAAGAmgknepdqggeRGVIINTAS----VAA 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755534620 172 FGG-----FYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTdaeltiertkkvwEAAPEHIKESYGQQ 241
Cdd:cd05371  150 FEGqigqaAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLL-------------AGLPEKVRDFLAKQ 211
PRK12937 PRK12937
short chain dehydrogenase; Provisional
27-213 4.63e-12

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 64.76  E-value: 4.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVL-----AACLTEKGAEELRnKTSDRLETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK12937   3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAvnyagSAAAADELVAEIE-AAGGRAIAVQADVADAAAVTRLFDAAETAF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 102 GdrGLWGLVNNAGVLQPfAYIEWYRPEDYMPIFQVNLIGLtqvtismlFLVKKAR-------GRIVNVS-SALGRVALFG 173
Cdd:PRK12937  82 G--RIDVLVNNAGVMPL-GTIADFDLEDFDRTIATNLRGA--------FVVLREAarhlgqgGRIINLStSVIALPLPGY 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755534620 174 GFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:PRK12937 151 GPYAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL 190
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
27-215 5.12e-12

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 64.95  E-value: 5.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGdrGL 106
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWG--SI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 WGLVNNAGV--LQPFAYIEWyrpEDYMPIFQVNLIGltqvtisMLFLVKKAR---------GRIVNVSSALGR--VALFg 173
Cdd:cd05363   79 DILVNNAALfdLAPIVDITR---ESYDRLFAINVSG-------TLFMMQAVAramiaqgrgGKIINMASQAGRrgEALV- 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 755534620 174 GFYSCSKYGVEAFS-----DVLRHevqdfGVKVSIIEPGSFKTEMTD 215
Cdd:cd05363  148 GVYCATKAAVISLTqsaglNLIRH-----GINVNAIAPGVVDGEHWD 189
PRK07074 PRK07074
SDR family oxidoreductase;
29-230 5.26e-12

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 64.79  E-value: 5.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD-RLETVILDVTKTESIVAAtqwVKERVGDRGLW 107
Cdd:PRK07074   2 KRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDaRFVPVACDLTDAASLAAA---LANAAAERGPV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 108 G-LVNNAGV-----LQPFAYIEWYRPEDympifqVNLIG----LTQVTISMLflvKKARGRIVNVSSALGrVALFGG-FY 176
Cdd:PRK07074  79 DvLVANAGAaraasLHDTTPASWRADNA------LNLEAaylcVEAVLEGML---KRSRGAVVNIGSVNG-MAALGHpAY 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755534620 177 SCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAEltIERTKKVWEAA 230
Cdd:PRK07074 149 SAAKAGLIHYTKLLAVEYGRFGIRANAVAPGTVKTQAWEAR--VAANPQVFEEL 200
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
29-213 7.91e-12

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 64.29  E-value: 7.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTS-----DRLETVILDVTKTESIVAATQWVKERVGD 103
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINaeygeGMAYGFGADATSEQSVLALSRGVDEIFGR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 RGLwgLVNNAGVLQPfAYIEWYRPEDYMPIFQVNLIG--LTQVTISMLFLVKKARGRIVNVSSALGRV-ALFGGFYSCSK 180
Cdd:PRK12384  82 VDL--LVYNAGIAKA-AFITDFQLGDFDRSLQVNLVGyfLCAREFSRLMIRDGIQGRIIQINSKSGKVgSKHNSGYSAAK 158
                        170       180       190
                 ....*....|....*....|....*....|....
gi 755534620 181 YGVEAFSDVLRHEVQDFGVKVSIIEPGSF-KTEM 213
Cdd:PRK12384 159 FGGVGLTQSLALDLAEYGITVHSLMLGNLlKSPM 192
PRK06138 PRK06138
SDR family oxidoreductase;
26-213 1.05e-11

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 63.63  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD--RLETVILDVTKTESIVAATQWVKERVGd 103
Cdd:PRK06138   2 RLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAggRAFARQGDVGSAEAVEALVDFVAARWG- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 rGLWGLVNNAGVLQPfAYIEWYRPEDYMPIFQVNLIGL---TQVTISMlfLVKKARGRIVNVSSALGRVALFG-GFYSCS 179
Cdd:PRK06138  81 -RLDVLVNNAGFGCG-GTVVTTDEADWDAVMRVNVGGVflwAKYAIPI--MQRQGGGSIVNTASQLALAGGRGrAAYVAS 156
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 755534620 180 KYGVEAFSdvlRHEVQDF---GVKVSIIEPGSFKTEM 213
Cdd:PRK06138 157 KGAIASLT---RAMALDHatdGIRVNAVAPGTIDTPY 190
PRK06124 PRK06124
SDR family oxidoreductase;
27-219 1.48e-11

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 63.58  E-value: 1.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEELRNKTSD------RLETVILDVTKTESIVAATQWVKER 100
Cdd:PRK06124   9 LAGQVALVTGSARGLGFEIARALAGAGAHVL---VNGRNAATLEAAVAAlraaggAAEALAFDIADEEAVAAAFARIDAE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 101 VGdrGLWGLVNNAGVL--QPFAYIEwyrPEDYMPIFQVNL---IGLTQ-VTISMlflVKKARGRIVNVSSALGRVALFG- 173
Cdd:PRK06124  86 HG--RLDILVNNVGARdrRPLAELD---DAAIRALLETDLvapILLSRlAAQRM---KRQGYGRIIAITSIAGQVARAGd 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755534620 174 GFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEmTDAELT 219
Cdd:PRK06124 158 AVYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATE-TNAAMA 202
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-214 1.56e-11

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 63.22  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAE--ELRNKTSDRLETVILDVTKTESIVAATQWVKERVGDR 104
Cdd:PRK06935  13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWDEtrRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 105 GLwgLVNNAGVLQPFAYIEwYRPEDYMPIFQVNLIG---LTQVTISMLflVKKARGRIVNVSSALgrvALFGGF----YS 177
Cdd:PRK06935  93 DI--LVNNAGTIRRAPLLE-YKDEDWNAVMDINLNSvyhLSQAVAKVM--AKQGSGKIINIASML---SFQGGKfvpaYT 164
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 755534620 178 CSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMT 214
Cdd:PRK06935 165 ASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANT 201
PRK06947 PRK06947
SDR family oxidoreductase;
30-213 5.74e-11

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 61.74  E-value: 5.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRV-------LAAclTEKGAEELRnKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVginyardAAA--AEETADAVR-AAGGRACVVAGDVANEADVIAMFDAVQSAFG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 drGLWGLVNNAGVL---QPFAYIEWYRPEDympIFQVNLIGLTQVTISMLFLVKKARG----RIVNVSSALGRVALFGGF 175
Cdd:PRK06947  80 --RLDALVNNAGIVapsMPLADMDAARLRR---MFDTNVLGAYLCAREAARRLSTDRGgrggAIVNVSSIASRLGSPNEY 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755534620 176 --YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:PRK06947 155 vdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEI 194
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
27-214 5.90e-11

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


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 61.57  E-value: 5.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLteKGAEELRNKTSDRLETVILDVTK--------TESIVAATQWVK 98
Cdd:cd05353    3 FDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDL--GGDRKGSGKSSSAADKVVDEIKAaggkavanYDSVEDGEKIVK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  99 ERVGDRG-LWGLVNNAGVL--QPFAYIEwyrPEDYMPIFQVNLIGLTQVT-ISMLFLVKKARGRIVNVSSALGrvaLFGG 174
Cdd:cd05353   81 TAIDAFGrVDILVNNAGILrdRSFAKMS---EEDWDLVMRVHLKGSFKVTrAAWPYMRKQKFGRIINTSSAAG---LYGN 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 755534620 175 F----YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSfKTEMT 214
Cdd:cd05353  155 FgqanYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPAA-GSRMT 197
PRK12827 PRK12827
short chain dehydrogenase; Provisional
27-215 6.64e-11

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 61.27  E-value: 6.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLET-------VILDVTKTESIVAATQWVKE 99
Cdd:PRK12827   4 LDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAVAAGIEAaggkalgLAFDVRDFAATRAALDAGVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 100 RVGdrGLWGLVNNAGVLQPFAYIEWYRpEDYMPIFQVNLIGLTQVTISMLFLVKKAR--GRIVNVSS-ALGRVALFGGFY 176
Cdd:PRK12827  84 EFG--RLDILVNNAGIATDAAFAELSI-EEWDDVIDVNLDGFFNVTQAALPPMIRARrgGRIVNIASvAGVRGNRGQVNY 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 755534620 177 SCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTD 215
Cdd:PRK12827 161 AASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMAD 199
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
27-211 1.44e-10

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 60.51  E-value: 1.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLT-EKGAEELRN---KTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK08936   5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSdEEEANDVAEeikKAGGEAIAVKGDVTVESDVVNLIQTAVKEFG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 DRGLWglVNNAGVLQPFAYIEwYRPEDYMPIFQVNLIGLTQVTISML--FLVKKARGRIVNVSSALGRV--ALFgGFYSC 178
Cdd:PRK08936  85 TLDVM--INNAGIENAVPSHE-MSLEDWNKVINTNLTGAFLGSREAIkyFVEHDIKGNIINMSSVHEQIpwPLF-VHYAA 160
                        170       180       190
                 ....*....|....*....|....*....|...
gi 755534620 179 SKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKT 211
Cdd:PRK08936 161 SKGGVKLMTETLAMEYAPKGIRVNNIGPGAINT 193
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
32-225 1.63e-10

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


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 60.06  E-value: 1.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRGMRVL-----AACLTEKGAEELRNKTSdRLETVILDVTKTESIVAATQWVKERVGdrGL 106
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVVinyrkSKDAAAEVAAEIEELGG-KAVVVRADVSQPQDVEEMFAAVKERFG--RL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 WGLVNNA--GVLQPFAYIEWYRPEDYMPIfqvNLIGL----TQVTISMlflVKKARGRIVNVSSAL-GRVALFGGFYSCS 179
Cdd:cd05359   78 DVLVSNAaaGAFRPLSELTPAHWDAKMNT---NLKALvhcaQQAAKLM---RERGGGRIVAISSLGsIRALPNYLAVGTA 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755534620 180 KYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERTKK 225
Cdd:cd05359  152 KAALEALVRYLAVELGPRGIRVNAVSPGVIDTDALAHFPNREDLLE 197
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
28-215 1.73e-10

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


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 60.24  E-value: 1.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNK--TSDRLETVIL--DVTKTESIVAATQWVKERVGD 103
Cdd:cd08933    8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESElnRAGPGSCKFVpcDVTKEEDIKTLISVTVERFGR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 rgLWGLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKARGRIVNVSSALGRVALFGGF-YSCSKYG 182
Cdd:cd08933   88 --IDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIGQKQAApYVATKGA 165
                        170       180       190
                 ....*....|....*....|....*....|...
gi 755534620 183 VEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTD 215
Cdd:cd08933  166 ITAMTKALAVDESRYGVRVNCISPGNIWTPLWE 198
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
27-213 1.77e-10

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


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 60.10  E-value: 1.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGdrGL 106
Cdd:cd05345    3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFG--RL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 WGLVNNAGVL---QPFAYIEwyrPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALG---RVALfgGFYSCS 179
Cdd:cd05345   81 DILVNNAGIThrnKPMLEVD---EEEFDRVFAVNVKSIYLSAQALVpHMEEQGGGVIINIASTAGlrpRPGL--TWYNAS 155
                        170       180       190
                 ....*....|....*....|....*....|....
gi 755534620 180 KYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:cd05345  156 KGWVVTATKAMAVELAPRNIRVNCLCPVAGETPL 189
PRK07201 PRK07201
SDR family oxidoreductase;
13-213 2.20e-10

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 61.51  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  13 HLLRW-YRERQVVSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVIL---DVTKTE 88
Cdd:PRK07201 354 HLDPDrARRRDLRGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAytcDLTDSA 433
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  89 SIVAATQWVKERVGdrGLWGLVNNAG------VLQPFAyiewyRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVN 161
Cdd:PRK07201 434 AVDHTVKDILAEHG--HVDYLVNNAGrsirrsVENSTD-----RFHDYERTMAVNYFGAVRLILGLLpHMRERRFGHVVN 506
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755534620 162 VSSA--LGRVALFGGfYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:PRK07201 507 VSSIgvQTNAPRFSA-YVASKAALDAFSDVAASETLSDGITFTTIHMPLVRTPM 559
PRK06194 PRK06194
hypothetical protein; Provisional
27-217 2.53e-10

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 60.03  E-value: 2.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMR-VLAACLT---EKGAEELRNKTSDRLeTVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK06194   4 FAGKVAVITGAASGFGLAFARIGAALGMKlVLADVQQdalDRAVAELRAQGAEVL-GVRTDVSDAAQVEALADAALERFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 DRGLwgLVNNAGVlQPFAYIEWYRPEDYMPIFQVNLIGLTQ----VTISMLFLVKKA---RGRIVNVSSALGRVALFG-G 174
Cdd:PRK06194  83 AVHL--LFNNAGV-GAGGLVWENSLADWEWVLGVNLWGVIHgvraFTPLMLAAAEKDpayEGHIVNTASMAGLLAPPAmG 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 755534620 175 FYSCSKYGVEAFSDVLRHEVQDFG--VKVSIIEPGSFKTEMTDAE 217
Cdd:PRK06194 160 IYNVSKHAVVSLTETLYQDLSLVTdqVGASVLCPYFVPTGIWQSE 204
PRK06172 PRK06172
SDR family oxidoreductase;
27-213 4.35e-10

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 58.99  E-value: 4.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEE----LRNKTSDRLeTVILDVTK---TESIVAATQWVKE 99
Cdd:PRK06172   5 FSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEEtvalIREAGGEAL-FVACDVTRdaeVKALVEQTIAAYG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 100 RVgDRGLwglvNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGltqVTISMLF----LVKKARGRIVNVSSALGRVALFG-G 174
Cdd:PRK06172  84 RL-DYAF----NNAGIEIEQGRLAEGSEAEFDAIMGVNVKG---VWLCMKYqiplMLAQGGGAIVNTASVAGLGAAPKmS 155
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 755534620 175 FYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:PRK06172 156 IYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDM 194
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
27-214 6.65e-10

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


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 58.65  E-value: 6.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVL------AACltEKGAEELrnKTSDRLETVILDVTKTESIVAATQWVKER 100
Cdd:cd08942    4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIisarkaEAC--ADAAEEL--SAYGECIAIPADLSSEEGIEALVARVAER 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 101 vGDRgLWGLVNNAGVlqpfayiEWYRPEDYMP------IFQVNLIGLTQVTISMLFLVKKAR-----GRIVNVSSALGRV 169
Cdd:cd08942   80 -SDR-LDVLVNNAGA-------TWGAPLEAFPesgwdkVMDINVKSVFFLTQALLPLLRAAAtaenpARVINIGSIAGIV 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 755534620 170 A--LFGGFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMT 214
Cdd:cd08942  151 VsgLENYSYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMT 197
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
27-212 7.56e-10

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


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 58.37  E-value: 7.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAC----LTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:cd05369    1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGrkpeVLEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLKEFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 DrgLWGLVNNAG--VLQPFAYIewyRPEDYMPIFQVNLIG---LTQVTISMLFLVKKArGRIVNVSSALGRVAL-FGGFY 176
Cdd:cd05369   81 K--IDILINNAAgnFLAPAESL---SPNGFKTVIDIDLNGtfnTTKAVGKRLIEAKHG-GSILNISATYAYTGSpFQVHS 154
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 755534620 177 SCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTE 212
Cdd:cd05369  155 AAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTT 190
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
27-231 9.27e-10

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 58.37  E-value: 9.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLT-EKG---AEELRNKTSDRLeTVILDVTKTESIVAATQWVKERvg 102
Cdd:PRK08277   8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNqEKAeavVAEIKAAGGEAL-AVKADVLDKESLEQARQQILED-- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 drglWG----LVNNAGVLQPFA---YIEWYRPEDYMPIF-----------QVNLIGltqvTI--SMLF---LVKKARGRI 159
Cdd:PRK08277  85 ----FGpcdiLINGAGGNHPKAttdNEFHELIEPTKTFFdldeegfefvfDLNLLG----TLlpTQVFakdMVGRKGGNI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 160 VNVSS-----ALGRVALfggfYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM-------TDAELTiERTKKVW 227
Cdd:PRK08277 157 INISSmnaftPLTKVPA----YSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQnrallfnEDGSLT-ERANKIL 231

                 ....
gi 755534620 228 EAAP 231
Cdd:PRK08277 232 AHTP 235
PRK08628 PRK08628
SDR family oxidoreductase;
26-206 1.14e-09

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 58.05  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  26 HLQDKYVFITGCDSGFGNLLARQLDRRG-MRVLAACLTEKG--AEELRNKTSdRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK08628   4 NLKDKVVIVTGGASGIGAAISLRLAEEGaIPVIFGRSAPDDefAEELRALQP-RAEFVQVDLTDDAQCRDAVEQTVAKFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 drGLWGLVNNAGVlQPFAYIEWYRpEDYMPIFQVNLIGLTQVTISMLFLVKKARGRIVNVSSalgRVALFG----GFYSC 178
Cdd:PRK08628  83 --RIDGLVNNAGV-NDGVGLEAGR-EAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISS---KTALTGqggtSGYAA 155
                        170       180
                 ....*....|....*....|....*...
gi 755534620 179 SKYGVEAFSDVLRHEVQDFGVKVSIIEP 206
Cdd:PRK08628 156 AKGAQLALTREWAVALAKDGVRVNAVIP 183
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-216 1.22e-09

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 57.61  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAacLTEKGAEELRNK---TSDRLETVILDVTKTESIVAATQWVKERVGD 103
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVG--VGVAEAPETQAQveaLGRKFHFITADLIQQKDIDSIVSQAVEVMGH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 RGLwgLVNNAGVLQ-----PFAYIEWyrpEDYMPIFQVNLIGLTQvTISMLFLVKKARGRIVNVSSALgrvALFGGF--- 175
Cdd:PRK12481  84 IDI--LINNAGIIRrqdllEFGNKDW---DDVININQKTVFFLSQ-AVAKQFVKQGNGGKIINIASML---SFQGGIrvp 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 755534620 176 -YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDA 216
Cdd:PRK12481 155 sYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAA 196
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
30-213 1.60e-09

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


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 57.09  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELrnKTSDRLETVILDVTKTESIVAATQWVkERVGDrglwgL 109
Cdd:cd05368    3 KVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKEL--ERGPGITTRVLDVTDKEQVAALAKEE-GRIDV-----L 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 110 VNNAGVLQPFAYIEwYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALGRV-ALFGGF-YSCSKYGVEAF 186
Cdd:cd05368   75 FNCAGFVHHGSILD-CEDDDWDFAMNLNVRSMYLMIKAVLpKMLARKDGSIINMSSVASSIkGVPNRFvYSTTKAAVIGL 153
                        170       180
                 ....*....|....*....|....*..
gi 755534620 187 SDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:cd05368  154 TKSVAADFAQQGIRCNAICPGTVDTPS 180
PRK08177 PRK08177
SDR family oxidoreductase;
30-221 2.01e-09

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 56.58  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETviLDVTKTESIVAATQWVKERVGDRglwgL 109
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIEK--LDMNDPASLDQLLQRLQGQRFDL----L 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 110 VNNAGVLQPFAY-IEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKARGRIVNVSSALGRVALFGG----FYSCSKYGVE 184
Cdd:PRK08177  76 FVNAGISGPAHQsAADATAAEIGQLFLTNAIAPIRLARRLLGQVRPGQGVLAFMSSQLGSVELPDGgempLYKASKAALN 155
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 755534620 185 AFSDVLRHEVQDFGVKVSIIEPGSFKTEM--TDAELTIE 221
Cdd:PRK08177 156 SMTRSFVAELGEPTLTVLSMHPGWVKTDMggDNAPLDVE 194
PRK07577 PRK07577
SDR family oxidoreductase;
27-213 2.01e-09

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 57.04  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACltekgaeelRNKTSD---RLETVIL-DVTKTESIVAATqwvkerVG 102
Cdd:PRK07577   1 MSSRTVLVTGATKGIGLALSLRLANLGHQVIGIA---------RSAIDDfpgELFACDLaDIEQTAATLAQI------NE 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 DRGLWGLVNNAGVL--QPFAYIEWyrpEDYMPIFQVNLIGLTQVTISMLFLVKKAR-GRIVNVSSalgrVALFGGF---- 175
Cdd:PRK07577  66 IHPVDAIVNNVGIAlpQPLGKIDL---AALQDVYDLNVRAAVQVTQAFLEGMKLREqGRIVNICS----RAIFGALdrts 138
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 755534620 176 YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:PRK07577 139 YSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETEL 176
PRK06953 PRK06953
SDR family oxidoreductase;
30-226 2.30e-09

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 56.62  E-value: 2.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSdrlETVILDVTKTESiVAATQWvkeRVGDRGLWGL 109
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQALGA---EALALDVADPAS-VAGLAW---KLDGEALDAA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 110 VNNAGVLQP-FAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKARGRIVNVSSALGRVA----LFGGFYSCSKYGVE 184
Cdd:PRK06953  75 VYVAGVYGPrTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSRMGSIGdatgTTGWLYRASKAALN 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 755534620 185 AFSDVLRHEVQdfGVKVSIIEPGSFKTEMTDAELTIERTKKV 226
Cdd:PRK06953 155 DALRAASLQAR--HATCIALHPGWVRTDMGGAQAALDPAQSV 194
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
28-245 2.98e-09

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


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 56.70  E-value: 2.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAACL----TEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGD 103
Cdd:cd05322    1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADInsenAEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 RGLwgLVNNAGVLQPfAYIEWYRPEDYMPIFQVNLIG--LTQVTISMLFLVKKARGRIVNVSSALGRV-ALFGGFYSCSK 180
Cdd:cd05322   81 VDL--LVYSAGIAKS-AKITDFELGDFDRSLQVNLVGyfLCAREFSKLMIRDGIQGRIIQINSKSGKVgSKHNSGYSAAK 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755534620 181 YGVEAFSDVLRHEVQDFGVKVSIIEPGSF-KTEMTDAeLTIERTKKVweaapeHIKESYGQQFFDD 245
Cdd:cd05322  158 FGGVGLTQSLALDLAEHGITVNSLMLGNLlKSPMFQS-LLPQYAKKL------GIKESEVEQYYID 216
PRK06123 PRK06123
SDR family oxidoreductase;
29-213 3.04e-09

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 56.71  E-value: 3.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEK-GAEELRNKTSDRLETVIL---DVTKTESIVAATQWVKERVGDr 104
Cdd:PRK06123   2 RKVMIITGASRGIGAATALLAAERGYAVCLNYLRNRdAAEAVVQAIRRQGGEALAvaaDVADEADVLRLFEAVDRELGR- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 105 gLWGLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIG----LTQVTISMLFLVKKARGRIVNVSSALGRVALFGGF--YSC 178
Cdd:PRK06123  81 -LDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGsflcAREAVKRMSTRHGGRGGAIVNVSSMAARLGSPGEYidYAA 159
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 755534620 179 SKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:PRK06123 160 SKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEI 194
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-231 3.76e-09

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 56.42  E-value: 3.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE-KGAEELRNKTSDRLETVILDVTKTESIVAAtqwVKERVGDRG 105
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEpTETIEQVTALGRRFLSLTADLRKIDGIPAL---LERAVAEFG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 106 -LWGLVNNAGVLQ-----PFAYIEWyrpEDYMPIFQVNLIGLTQvTISMLFLVKKARGRIVNVSSALgrvALFGGF---- 175
Cdd:PRK08993  85 hIDILVNNAGLIRredaiEFSEKDW---DDVMNLNIKSVFFMSQ-AAAKHFIAQGNGGKIINIASML---SFQGGIrvps 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755534620 176 YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIE-RTKKVWEAAP 231
Cdd:PRK08993 158 YTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEqRSAEILDRIP 214
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
28-210 4.22e-09

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


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 56.19  E-value: 4.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAE----ELRNKTSDRLETVILDVTKTESIVAATQWVKERVG- 102
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEqlkeELTNLYKNRVIALELDITSKESIKELIESYLEKFGr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 -DrglwGLVNNAGVlQPFAYIEWY---RPEDYMPIFQVNLIG---LTQVTISmlFLVKKARGRIVNVSSALGRVA----L 171
Cdd:cd08930   81 iD----ILINNAYP-SPKVWGSRFeefPYEQWNEVLNVNLGGaflCSQAFIK--LFKKQGKGSIINIASIYGVIApdfrI 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755534620 172 FGG-------FYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFK 210
Cdd:cd08930  154 YENtqmyspvEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGIL 199
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
27-245 4.80e-09

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


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 55.86  E-value: 4.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEELRNKTSDRLETVI------------------LDVTKTE 88
Cdd:cd05338    1 LSGKVAFVTGASRGIGRAIALRLAKAGATVV---VAAKTASEGDNGSAKSLPGTIeetaeeieaaggqalpivVDVRDED 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  89 SIVAATQWVKERVGdrGLWGLVNNAGVLQpFAYIEWYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVSSALG 167
Cdd:cd05338   78 QVRALVEATVDQFG--RLDILVNNAGAIW-LSLVEDTPAKRFDLMQRVNLRGTYLLSQAALpHMVKAGQGHILNISPPLS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 168 RVALFGGF-YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTierTKKVWEAA--PEHIKES------- 237
Cdd:cd05338  155 LRPARGDVaYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIETPAATELS---GGSDPARArsPEILSDAvlailsr 231
                        250
                 ....*....|...
gi 755534620 238 -----YGQQFFDD 245
Cdd:cd05338  232 paaerTGLVVIDE 244
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
32-211 1.21e-08

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 54.07  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEELRNKTSDRLE-TVILDVTKTESIVAATQwvkeRVGDRGLWglV 110
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLL---LSGRDAGALAGLAAEVGAlARPADVAAELEVWALAQ----ELGPLDLL--V 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 111 NNAGVLQPFAYIEwYRPEDYMPIFQVNLIGLTQVTISMLF-LVKKARGRIVNVSSALGRVALFGGfYSCSKYGVEAFSDV 189
Cdd:cd11730   72 YAAGAILGKPLAR-TKPAAWRRILDANLTGAALVLKHALAlLAAGARLVFLGAYPELVMLPGLSA-YAAAKAALEAYVEV 149
                        170       180
                 ....*....|....*....|..
gi 755534620 190 LRHEVQdfGVKVSIIEPGSFKT 211
Cdd:cd11730  150 ARKEVR--GLRLTLVRPPAVDT 169
PRK06125 PRK06125
short chain dehydrogenase; Provisional
26-212 1.27e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 54.66  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRV-LAACLTEK---GAEELRNKTSDRLETVILDVTKTESIVAatqwVKERV 101
Cdd:PRK06125   4 HLAGKRVLITGASKGIGAAAAEAFAAEGCHLhLVARDADAleaLAADLRAAHGVDVAVHALDLSSPEAREQ----LAAEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 102 GDRGLwgLVNNAGVLqPFAYIEWYRPEDYMPIFQVNLIGLtqVTISMLFLVK-KARGR--IVNVSSALGRVALFGgfYSC 178
Cdd:PRK06125  80 GDIDI--LVNNAGAI-PGGGLDDVDDAAWRAGWELKVFGY--IDLTRLAYPRmKARGSgvIVNVIGAAGENPDAD--YIC 152
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 755534620 179 SKYG---VEAFSDVLRHEVQDFGVKVSIIEPGSFKTE 212
Cdd:PRK06125 153 GSAGnaaLMAFTRALGGKSLDDGVRVVGVNPGPVATD 189
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
27-216 1.59e-08

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 54.33  E-value: 1.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACL-TEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGdRG 105
Cdd:PRK08642   3 ISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHqSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEHFG-KP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 106 LWGLVNNA-------GVLQP-FAYIEWyrpEDYMPIFQVNLIGLTQVTISMLFLVKKAR-GRIVNVSSALgrvalfggF- 175
Cdd:PRK08642  82 ITTVVNNAladfsfdGDARKkADDITW---EDFQQQLEGSVKGALNTIQAALPGMREQGfGRIINIGTNL--------Fq 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 755534620 176 --------YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTemTDA 216
Cdd:PRK08642 151 npvvpyhdYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRT--TDA 197
PRK09730 PRK09730
SDR family oxidoreductase;
34-213 2.12e-08

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 54.09  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  34 ITGCDSGFGNLLARQLDRRGMRVLAACL-TEKGAEELRNK---TSDRLETVILDVTKTESIVAATQWVKERVGDrgLWGL 109
Cdd:PRK09730   6 VTGGSRGIGRATALLLAQEGYTVAVNYQqNLHAAQEVVNLitqAGGKAFVLQADISDENQVVAMFTAIDQHDEP--LAAL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 110 VNNAGVLQPFAYIEWYRPEdympifQVNLIGLTQVTISMLFL---VKKAR-------GRIVNVSSALGRVALFGGF--YS 177
Cdd:PRK09730  84 VNNAGILFTQCTVENLTAE------RINRVLSTNVTGYFLCCreaVKRMAlkhggsgGAIVNVSSAASRLGAPGEYvdYA 157
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 755534620 178 CSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:PRK09730 158 ASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEM 193
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
30-214 5.86e-08

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 53.16  E-value: 5.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFG-----NLLARQLDRRGMRVLAACLTEKGAEELRNKTSD-------RLETVILDVTKTESIVAATQWV 97
Cdd:cd08941    2 KVVLVTGANSGLGlaiceRLLAEDDENPELTLILACRNLQRAEAACRALLAshpdarvVFDYVLVDLSNMVSVFAAAKEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  98 KERVgdRGLWGLVNNAGvLQPFAYIEWYR---------------------------------PEDYMPIFQVNLIG---L 141
Cdd:cd08941   82 KKRY--PRLDYLYLNAG-IMPNPGIDWIGaikevltnplfavtnptykiqaegllsqgdkatEDGLGEVFQTNVFGhyyL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 142 TQVTISMLFLvKKARGRIVNVSSALGRVALFG----------GFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKT 211
Cdd:cd08941  159 IRELEPLLCR-SDGGSQIIWTSSLNASPKYFSlediqhlkgpAPYSSSKYLVDLLSLALNRKFNKLGVYSYVVHPGICTT 237

                 ...
gi 755534620 212 EMT 214
Cdd:cd08941  238 NLT 240
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
27-256 5.87e-08

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


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 52.92  E-value: 5.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEEL--RNKTSDRLETVILDVTKTESIVAATQWVKERVGDR 104
Cdd:cd08937    2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLaeILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 105 GLwgLVNNAG--VLQPFayIEWYRPEDYMPIFQVNLigLTQVTISMLFL---VKKARGRIVNVSSalgrVALFGGF---Y 176
Cdd:cd08937   82 DV--LINNVGgtIWAKP--YEHYEEEQIEAEIRRSL--FPTLWCCRAVLphmLERQQGVIVNVSS----IATRGIYripY 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 177 SCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMtdaeltieRTKKVWEAAPEHIKESYGQQFFDdfcSTTKRELMK 256
Cdd:cd08937  152 SAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAPP--------RKIPRNAAPMSEQEKVWYQRIVD---QTLDSSLMG 220
PRK06198 PRK06198
short chain dehydrogenase; Provisional
25-164 8.44e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 52.31  E-value: 8.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  25 SHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAC--LTEKG---AEELRnKTSDRLETVILDVTKTESIVAATQWVKE 99
Cdd:PRK06198   2 GRLDGKVALVTGGTQGLGAAIARAFAERGAAGLVICgrNAEKGeaqAAELE-ALGAKAVFVQADLSDVEDCRRVVAAADE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755534620 100 RVGdrGLWGLVNNAGVLQPFAYIEwYRPEDYMPIFQVNLIG---LTQVTISMLfLVKKARGRIVNVSS 164
Cdd:PRK06198  81 AFG--RLDALVNAAGLTDRGTILD-TSPELFDRHFAVNVRApffLMQEAIKLM-RRRKAEGTIVNIGS 144
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
26-223 9.71e-08

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 52.16  E-value: 9.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVI---LDVTKTESIVAATQWVKERVG 102
Cdd:PRK06113   8 RLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFacrCDITSEQELSALADFALSKLG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 drGLWGLVNNAGVLQPfayiewyRPEDyMPI------FQVNLIGLTQVT-ISMLFLVKKARGRIVNVSSALG-----RVA 170
Cdd:PRK06113  88 --KVDILVNNAGGGGP-------KPFD-MPMadfrraYELNVFSFFHLSqLVAPEMEKNGGGVILTITSMAAenkniNMT 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755534620 171 LFGGfyscSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELT--IERT 223
Cdd:PRK06113 158 SYAS----SKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITpeIEQK 208
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
27-207 2.84e-07

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


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 50.75  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKgaEELRNKTSDRLET-----VIL--DVTKTESIVAATQWVKE 99
Cdd:cd05355   24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEE--EDDAEETKKLIEEegrkcLLIpgDLGDESFCRDLVKEVVK 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 100 RVGdrGLWGLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLigltqvtISMLFLVKKA------RGRIVNVSSAL---GRVA 170
Cdd:cd05355  102 EFG--KLDILVNNAAYQHPQESIEDITTEQLEKTFRTNI-------FSMFYLTKAAlphlkkGSSIINTTSVTaykGSPH 172
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 755534620 171 LFGgfYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPG 207
Cdd:cd05355  173 LLD--YAATKGAIVAFTRGLSLQLAEKGIRVNAVAPG 207
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
30-216 3.00e-07

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


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 50.53  E-value: 3.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACL-TEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGDRGLwg 108
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYrSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDT-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 109 LVNNAGVLQPF--------AYIEWyrpEDYMPIFQVNLIGLTQVTISMLFLVKKAR-GRIVNVSSALGR--VALFGGfYS 177
Cdd:cd05349   79 IVNNALIDFPFdpdqrktfDTIDW---EDYQQQLEGAVKGALNLLQAVLPDFKERGsGRVINIGTNLFQnpVVPYHD-YT 154
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 755534620 178 CSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTemTDA 216
Cdd:cd05349  155 TAKAALLGFTRNMAKELGPYGITVNMVSGGLLKV--TDA 191
PLN02780 PLN02780
ketoreductase/ oxidoreductase
31-214 3.08e-07

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 51.02  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  31 YVFITGCDSGFGNLLARQLDRRGMR-VLAACLTEK---GAEELRNKTSD-RLETVILDVTKteSIVAATQWVKERVGDRG 105
Cdd:PLN02780  55 WALVTGPTDGIGKGFAFQLARKGLNlVLVARNPDKlkdVSDSIQSKYSKtQIKTVVVDFSG--DIDEGVKRIKETIEGLD 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 106 LWGLVNNAGVLQPFA-YIEWYRPEDYMPIFQVNLIGLTQVTISMLF-LVKKARGRIVNVSSALGRVA---LFGGFYSCSK 180
Cdd:PLN02780 133 VGVLINNVGVSYPYArFFHEVDEELLKNLIKVNVEGTTKVTQAVLPgMLKRKKGAIINIGSGAAIVIpsdPLYAVYAATK 212
                        170       180       190
                 ....*....|....*....|....*....|....
gi 755534620 181 YGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMT 214
Cdd:PLN02780 213 AYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMA 246
PRK12746 PRK12746
SDR family oxidoreductase;
24-213 3.15e-07

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 50.80  E-value: 3.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  24 VSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGA--EELRNKTSDRLETVIL--DVTKTESIVAATQWVKE 99
Cdd:PRK12746   1 MKNLDGKVALVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAadETIREIESNGGKAFLIeaDLNSIDGVKKLVEQLKN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 100 ----RVGDRGLWGLVNNAGVLQPfAYIEWYRPEDYMPIFQVNLIG---LTQVTISMLflvkKARGRIVNVSSALGRVALF 172
Cdd:PRK12746  81 elqiRVGTSEIDILVNNAGIGTQ-GTIENTTEEIFDEIMAVNIKApffLIQQTLPLL----RAEGRVINISSAEVRLGFT 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 755534620 173 GGF-YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:PRK12746 156 GSIaYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDI 197
PRK06701 PRK06701
short chain dehydrogenase; Provisional
27-207 3.17e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 50.80  E-value: 3.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG-AEElrnkTSDRLE-------TVILDVTKT---ESIVAATq 95
Cdd:PRK06701  44 LKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEdANE----TKQRVEkegvkclLIPGDVSDEafcKDAVEET- 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  96 wVKErVGdrGLWGLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIG---LTQVTISMLflvkKARGRIVNVSSA---LGRV 169
Cdd:PRK06701 119 -VRE-LG--RLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSyfhMTKAALPHL----KQGSAIINTGSItgyEGNE 190
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 755534620 170 ALFGgfYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPG 207
Cdd:PRK06701 191 TLID--YSATKGAIHAFTRSLAQSLVQKGIRVNAVAPG 226
PRK07814 PRK07814
SDR family oxidoreductase;
27-212 3.95e-07

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 50.55  E-value: 3.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKERVGD 103
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAagrRAHVVAADLAHPEATAGLAGQAVEAFGR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 104 RGLwgLVNNAGVLQPFAYIEwYRPEDYMPIFQVNLI---GLTQVTISmLFLVKKARGRIVNVSSALGRVAlfG-GFYScs 179
Cdd:PRK07814  88 LDI--VVNNVGGTMPNPLLS-TSTKDLADAFTFNVAtahALTVAAVP-LMLEHSGGGSVINISSTMGRLA--GrGFAA-- 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 755534620 180 kYGVE--AFSDVLRHEVQDFG--VKVSIIEPGSFKTE 212
Cdd:PRK07814 160 -YGTAkaALAHYTRLAALDLCprIRVNAIAPGSILTS 195
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
27-213 5.69e-07

2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 49.95  E-value: 5.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGdrGL 106
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAFG--KL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 WGLVNNAGVLQPFAYIEWYRPEDYMP----IFQVNLIGLTQVTISMLFLVKKARGRIVNVSSALGRVALFGG-FYSCSKY 181
Cdd:PRK06200  82 DCFVGNAGIWDYNTSLVDIPAETLDTafdeIFNVNVKGYLLGAKAALPALKASGGSMIFTLSNSSFYPGGGGpLYTASKH 161
                        170       180       190
                 ....*....|....*....|....*....|..
gi 755534620 182 GVEAFSDVLRHEVQDfGVKVSIIEPGSFKTEM 213
Cdd:PRK06200 162 AVVGLVRQLAYELAP-KIRVNGVAPGGTVTDL 192
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
34-214 5.76e-07

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 49.77  E-value: 5.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  34 ITGCDSGFGNLLARQLDRRGMRVL------AACLTEKGAEELR-NKTSDRLETVILDVTKTESIVAATQwvkERVGdrGL 106
Cdd:cd05337    6 VTGASRGIGRAIATELAARGFDIAindlpdDDQATEVVAEVLAaGRRAIYFQADIGELSDHEALLDQAW---EDFG--RL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 WGLVNNAGV-LQPFAYIEWYRPEDYMPIFQVNLIG---LTQ-VTISMLFLVKKARG---RIVNVSS-ALGRVALFGGFYS 177
Cdd:cd05337   81 DCLVNNAGIaVRPRGDLLDLTEDSFDRLIAINLRGpffLTQaVARRMVEQPDRFDGphrSIIFVTSiNAYLVSPNRGEYC 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 755534620 178 CSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMT 214
Cdd:cd05337  161 ISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMT 197
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
32-231 5.76e-07

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 49.88  E-value: 5.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAeelrNKTSDRLET-------VILDVTKTESIVAATQWVKERVGdr 104
Cdd:cd05365    2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGA----EAVAAAIQQaggqaigLECNVTSEQDLEAVVKATVSQFG-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 105 GLWGLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGLTQvtISML---FLVKKARGRIVNVSSALGRVALFG-GFYSCSK 180
Cdd:cd05365   76 GITILVNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFR--LSQLcapHMQKAGGGAILNISSMSSENKNVRiAAYGSSK 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755534620 181 YGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERTKKVWEAAP 231
Cdd:cd05365  154 AAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDALASVLTPEIERAMLKHTP 204
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
32-224 6.09e-07

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 49.80  E-value: 6.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEkgAEelrnktsdrletVILDVTKTESIVAATQWVKERVgDRGLWGLVN 111
Cdd:cd05328    2 IVITGAASGIGAATAELLEDAGHTVIGIDLRE--AD------------VIADLSTPEGRAAAIADVLARC-SGVLDGLVN 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 112 NAGVLQPFAYIEwyrpedympIFQVNLIGLTQVTISMLFLVKKARG-RIVNVSSALG----------RVALFGGF----- 175
Cdd:cd05328   67 CAGVGGTTVAGL---------VLKVNYFGLRALMEALLPRLRKGHGpAAVVVSSIAGagwaqdklelAKALAAGTearav 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755534620 176 -------------YSCSKYGVEAFsdVLRHEVQDF---GVKVSIIEPGSFKTEMTDAELTIERTK 224
Cdd:cd05328  138 alaehagqpgylaYAGSKEALTVW--TRRRAATWLygaGVRVNTVAPGPVETPILQAFLQDPRGG 200
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
27-216 6.33e-07

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 49.77  E-value: 6.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVL-----AACLtEKGAEELRNKTSDrLETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVIlngrdPAKL-AAAAESLKGQGLS-AHALAFDVTDHDAVRAAIDAFEAEI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 102 GDRGLwgLVNNAGvLQPFAYIEWYRPEDYMPIFQVNligltqvtISMLF---------LVKKARGRIVN---VSSALGRV 169
Cdd:PRK07523  86 GPIDI--LVNNAG-MQFRTPLEDFPADAFERLLRTN--------ISSVFyvgqavarhMIARGAGKIINiasVQSALARP 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 755534620 170 ALfgGFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDA 216
Cdd:PRK07523 155 GI--APYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAA 199
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
30-213 6.65e-07

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


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 49.70  E-value: 6.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACL----TEKGAEELRNKtsDRLETVILDVTKTESIVAATQWVKERVGdrG 105
Cdd:cd08943    2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIdpeiAEKVAEAAQGG--PRALGVQCDVTSEAQVQSAFEQAVLEFG--G 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 106 LWGLVNNAGVLQPfAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKAR--GRIVNVSSalgRVALFGG----FYSCS 179
Cdd:cd08943   78 LDIVVSNAGIATS-SPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGigGNIVFNAS---KNAVAPGpnaaAYSAA 153
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 755534620 180 KYGVEAFSDVLRHEVQDFGVKVSIIEP-----GSFKTEM 213
Cdd:cd08943  154 KAAEAHLARCLALEGGEDGIRVNTVNPdavfrGSKIWEG 192
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
27-213 7.73e-07

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


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 49.37  E-value: 7.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVL----AACLTEKG-AEELRnKTSDRLETVILDVTKTESIVAATQWVKERV 101
Cdd:cd09763    1 LSGKIALVTGASRGIGRGIALQLGEAGATVYitgrTILPQLPGtAEEIE-ARGGKCIPVRCDHSDDDEVEALFERVAREQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 102 GDRgLWGLVNNA---------GVLQPFayieWYRPE---DYMpifqvNLIGLTQVTISMLF----LVKKARGRIVNVSSA 165
Cdd:cd09763   80 QGR-LDILVNNAyaavqlilvGVAKPF----WEEPPtiwDDI-----NNVGLRAHYACSVYaaplMVKAGKGLIVIISST 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 755534620 166 LGRVALFGGFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:cd09763  150 GGLEYLFNVAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTEL 197
PRK05876 PRK05876
short chain dehydrogenase; Provisional
34-213 1.02e-06

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 49.18  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  34 ITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEE----LRNKTSDrLETVILDVTKTESIVAATQWVKERVGdrGLWGL 109
Cdd:PRK05876  11 ITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQavnhLRAEGFD-VHGVMCDVRHREEVTHLADEAFRLLG--HVDVV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 110 VNNAGVL--QPFAYIEwyrPEDYMPIFQVNLIGLTQVTISML--FLVKKARGRIVNVSSALGRVALFG-GFYSCSKYGVE 184
Cdd:PRK05876  88 FSNAGIVvgGPIVEMT---HDDWRWVIDVDLWGSIHTVEAFLprLLEQGTGGHVVFTASFAGLVPNAGlGAYGVAKYGVV 164
                        170       180
                 ....*....|....*....|....*....
gi 755534620 185 AFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:PRK05876 165 GLAETLAREVTADGIGVSVLCPMVVETNL 193
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
28-207 1.46e-06

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 48.79  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLA---ACLTEKGAEELRNKTSDRLeTVILDVTKTESIVAATQWVKERVGdr 104
Cdd:PRK12823   7 AGKVVVVTGAAQGIGRGVALRAAAEGARVVLvdrSELVHEVAAELRAAGGEAL-ALTADLETYAGAQAAMAAAVEAFG-- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 105 GLWGLVNNAG---VLQPFAYiewYRPED--------YMPifqvNLIGLTQVTISMLflvKKARGRIVNVSS----ALGRV 169
Cdd:PRK12823  84 RIDVLINNVGgtiWAKPFEE---YEEEQieaeirrsLFP----TLWCCRAVLPHML---AQGGGAIVNVSSiatrGINRV 153
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 755534620 170 AlfggfYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPG 207
Cdd:PRK12823 154 P-----YSAAKGGVNALTASLAFEYAEHGIRVNAVAPG 186
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
32-240 1.48e-06

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


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 48.53  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVIL----DVTKTESIVAATQWVKERVGDRGLw 107
Cdd:cd05373    2 AAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKavptDARDEDEVIALFDLIEEEIGPLEV- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 108 gLVNNAGVLQPFAYIEwYRPEDYMPIFQVNLIG--LT--QVTISMLflvKKARGRIV--NVSSALGRVALFGGFySCSKY 181
Cdd:cd05373   81 -LVYNAGANVWFPILE-TTPRVFEKVWEMAAFGgfLAarEAAKRML---ARGRGTIIftGATASLRGRAGFAAF-AGAKF 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755534620 182 GVEAFSDVLRHEVQDFGVKVS--IIEPGsfktemTDAELTIERTKKVWEAA-------PEHIKESYGQ 240
Cdd:cd05373  155 ALRALAQSMARELGPKGIHVAhvIIDGG------IDTDFIRERFPKRDERKeedgildPDAIAEAYWQ 216
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
27-215 2.34e-06

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 48.13  E-value: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV----LAACLTEKGAEELRNKTSDrLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIvfndINQELVDKGLAAYRELGIE-AHGYVCDVTDEDGVQAMVSQIEKEVG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 103 DRGLwgLVNNAGVLQPFAYIEwYRPEDYMPIFQVNLIGLTQVTISML-FLVKKARGRIVNVS---SALGRVALfgGFYSC 178
Cdd:PRK07097  87 VIDI--LVNNAGIIKRIPMLE-MSAEDFRQVIDIDLNAPFIVSKAVIpSMIKKGHGKIINICsmmSELGRETV--SAYAA 161
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 755534620 179 SKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTD 215
Cdd:PRK07097 162 AKGGLKMLTKNIASEYGEANIQCNGIGPGYIATPQTA 198
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
30-213 3.93e-06

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 47.49  E-value: 3.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKtesiVAATQWVKERVGDRGLW-G 108
Cdd:cd08951    8 KRIFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSS----LAETRKLADQVNAIGRFdA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 109 LVNNAGVLQ-PFAYIEwyrPEDYMPIFQVNLIGLTQVTIsmlfLVKKARgRIVNVSSAL--------------GRVALFG 173
Cdd:cd08951   84 VIHNAGILSgPNRKTP---DTGIPAMVAVNVLAPYVLTA----LIRRPK-RLIYLSSGMhrggnaslddidwfNRGENDS 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755534620 174 GFYSCSKYGVEAFSDVLRHEVQDfgVKVSIIEPGSFKTEM 213
Cdd:cd08951  156 PAYSDSKLHVLTLAAAVARRWKD--VSSNAVHPGWVPTKM 193
PRK06500 PRK06500
SDR family oxidoreductase;
25-211 4.01e-06

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 47.26  E-value: 4.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  25 SHLQDKYVFITGCDSGFGNLLARQLDRRGMRV---------LAACLTEKGAEEL--RNKTSDrletvildvtktesiVAA 93
Cdd:PRK06500   2 SRLQGKTALITGGTSGIGLETARQFLAEGARVaitgrdpasLEAARAELGESALviRADAGD---------------VAA 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  94 TQWVKERVGDRG--LWGLVNNAGVLQpFAYIEWYRPEDYMPIFQVNLIG---LTQvtiSMLFLVKKARGRIVN--VSSAL 166
Cdd:PRK06500  67 QKALAQALAEAFgrLDAVFINAGVAK-FAPLEDWDEAMFDRSFNTNVKGpyfLIQ---ALLPLLANPASIVLNgsINAHI 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 755534620 167 GRVAlfGGFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKT 211
Cdd:PRK06500 143 GMPN--SSVYAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQT 185
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
27-207 4.03e-06

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 47.35  E-value: 4.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGDrgL 106
Cdd:cd05348    2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGK--L 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 WGLVNNAGVLQPFAYIEwYRPED-----YMPIFQVNLIGLTQVTISMLFLVKKARGRIV-NVSSALGRVALFGGFYSCSK 180
Cdd:cd05348   80 DCFIGNAGIWDYSTSLV-DIPEEkldeaFDELFHINVKGYILGAKAALPALYATEGSVIfTVSNAGFYPGGGGPLYTASK 158
                        170       180
                 ....*....|....*....|....*..
gi 755534620 181 YGVEAFSDVLRHEVQDFgVKVSIIEPG 207
Cdd:cd05348  159 HAVVGLVKQLAYELAPH-IRVNGVAPG 184
PRK09186 PRK09186
flagellin modification protein A; Provisional
27-207 4.69e-06

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 46.91  E-value: 4.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEEL-----RNKTSDRLETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELleslgKEFKSKKLSLVELDITDQESLEEFLSKSAEKY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 102 GDrgLWGLVNNAgvlqpfayiewY-RPEDYMPIF----------QVNLigltQVTISMLF-------LVKKARGRIVNVS 163
Cdd:PRK09186  82 GK--IDGAVNCA-----------YpRNKDYGKKFfdvslddfneNLSL----HLGSSFLFsqqfakyFKKQGGGNLVNIS 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755534620 164 SALGRVA----LFGGF-------YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPG 207
Cdd:PRK09186 145 SIYGVVApkfeIYEGTsmtspveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPG 199
PRK07069 PRK07069
short chain dehydrogenase; Validated
33-170 8.04e-06

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 46.24  E-value: 8.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  33 FITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEELRNKTSDRLET---------VILDVTKTESIVAATQWVKERVGd 103
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVF---LTDINDAAGLDAFAAEINAahgegvafaAVQDVTDEAQWQALLAQAADAMG- 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755534620 104 rGLWGLVNNAGV-----LQPFAYIEWYRpedympIFQVN----LIGLTQvtiSMLFLVKKARGRIVNVSSALGRVA 170
Cdd:PRK07069  79 -GLSVLVNNAGVgsfgaIEQIELDEWRR------VMAINvesiFLGCKH---ALPYLRASQPASIVNISSVAAFKA 144
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
46-223 8.23e-06

decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 46.24  E-value: 8.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  46 ARQLDRRGMRVLAACLT-----EKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERvGDRGL----WGLVNNAGVL 116
Cdd:PRK07904  26 ERYLKNAPARVVLAALPddprrDAAVAQMKAAGASSVEVIDFDALDTDSHPKVIDAAFAG-GDVDVaivaFGLLGDAEEL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 117 qpfayieWYRPEDYMPIFQVNLIGltQVTISMLfLVKKAR----GRIVNVSSALG-RVALFGGFYSCSKYGVEAFSDVLR 191
Cdd:PRK07904 105 -------WQNQRKAVQIAEINYTA--AVSVGVL-LGEKMRaqgfGQIIAMSSVAGeRVRRSNFVYGSTKAGLDGFYLGLG 174
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 755534620 192 HEVQDFGVKVSIIEPGSFKTEMT----DAELTIERT 223
Cdd:PRK07904 175 EALREYGVRVLVVRPGQVRTRMSahakEAPLTVDKE 210
PRK12747 PRK12747
short chain dehydrogenase; Provisional
27-218 1.27e-05

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 45.84  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG-AEELRNKTSDRLETVILDVTKTESI-------VAATQWVK 98
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEeAEETVYEIQSNGGSAFSIGANLESLhgvealySSLDNELQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  99 ERVGDRGLWGLVNNAGVlQPFAYIEWYRPEDYMPIFQVNLIG---LTQVTISMLflvkKARGRIVNVSSALGRVALFGGF 175
Cdd:PRK12747  82 NRTGSTKFDILINNAGI-GPGAFIEETTEQFFDRMVSVNAKApffIIQQALSRL----RDNSRIINISSAATRISLPDFI 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 755534620 176 -YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMtDAEL 218
Cdd:PRK12747 157 aYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDM-NAEL 199
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
33-214 1.37e-05

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 45.72  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  33 FITGCDSGFGNLLARQLDRRGMRVLAACLTEkgAEELRnKTSDRLET-------VILDVTKTESIVAATQWVKERVGdrG 105
Cdd:PRK12745   6 LVTGGRRGIGLGIARALAAAGFDLAINDRPD--DEELA-ATQQELRAlgvevifFPADVADLSAHEAMLDAAQAAWG--R 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 106 LWGLVNNAGVlqpfAYIEwyR-------PEDYMPIFQVNLIG---LTQVTISMLFLVKKARGR----IVNVSSALGRVAL 171
Cdd:PRK12745  81 IDCLVNNAGV----GVKV--RgdlldltPESFDRVLAINLRGpffLTQAVAKRMLAQPEPEELphrsIVFVSSVNAIMVS 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 755534620 172 FG-GFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMT 214
Cdd:PRK12745 155 PNrGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMT 198
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
32-174 3.42e-05

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 44.82  E-value: 3.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCDSGFGNLLARQLDRRGM-RVLAACLTEKGAEELRNKT---SDRLETVILDVTKTESIvaaTQWVKE-RVGDRGL 106
Cdd:cd09810    4 VVITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQEVgmpKDSYSVLHCDLASLDSV---RQFVDNfRRTGRPL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755534620 107 WGLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIG---LTQVTISMLFLVKKARGRIVNVSSALGRVALFGG 174
Cdd:cd09810   81 DALVCNAAVYLPTAKEPRFTADGFELTVGVNHLGhflLTNLLLEDLQRSENASPRIVIVGSITHNPNTLAG 151
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
27-212 7.82e-05

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 43.17  E-value: 7.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGA-----EELRnKTSDRLETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK08063   2 FSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAaeetaEEIE-ALGRKALAVKANVGDVEKIKEMFAQIDEEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 102 GdrGLWGLVNNA--GVLQPFAYIE---WyrpeDY-MPIFQVNLIGLTQVTISMlfLVKKARGRIVNVSSaLG--RVALFG 173
Cdd:PRK08063  81 G--RLDVFVNNAasGVLRPAMELEeshW----DWtMNINAKALLFCAQEAAKL--MEKVGGGKIISLSS-LGsiRYLENY 151
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 755534620 174 GFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTE 212
Cdd:PRK08063 152 TTVGVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTD 190
PRK05875 PRK05875
short chain dehydrogenase; Provisional
27-213 1.06e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 43.25  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV---------LAACLTEKGAeeLRNKTSDRLETVilDVTKTESIVAATQWV 97
Cdd:PRK05875   5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVmivgrnpdkLAAAAEEIEA--LKGAGAVRYEPA--DVTDEDQVARAVDAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  98 KERVGdrGLWGLVNNAG---VLQPFAYIE---WYRPEDYmpifqvnligltQVTISMLFLVKKAR-------GRIVNVSS 164
Cdd:PRK05875  81 TAWHG--RLHGVVHCAGgseTIGPITQIDsdaWRRTVDL------------NVNGTMYVLKHAARelvrgggGSFVGISS 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 755534620 165 -ALGRVALFGGFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEM 213
Cdd:PRK05875 147 iAASNTHRWFGAYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDL 196
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
29-170 1.09e-04

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 42.97  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEE-----LRNKTSDRLETVILDVTKTESIVAATQWVKERVGD 103
Cdd:cd09809    1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAavsriLEEWHKARVEAMTLDLASLRSVQRFAEAFKAKNSP 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755534620 104 rgLWGLVNNAGVlqpFAyIEWYRPEDYM-PIFQVNLIG---LTQVTISMLFLVKKArgRIVNVSSALGRVA 170
Cdd:cd09809   81 --LHVLVCNAAV---FA-LPWTLTEDGLeTTFQVNHLGhfyLVQLLEDVLRRSAPA--RVIVVSSESHRFT 143
PRK07062 PRK07062
SDR family oxidoreductase;
27-204 1.43e-04

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 42.72  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVlAACLTE----KGAE-ELRNKTSD-RLETVILDVTKTESIVAATQWVKER 100
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASV-AICGRDeerlASAEaRLREKFPGaRLLAARCDVLDEADVAAFAAAVEAR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 101 VGdrGLWGLVNNAG--VLQPFAYI--EWYRPEDYMPIFQVnlIGLTQVTISMlfLVKKARGRIVNVSSALGR------VA 170
Cdd:PRK07062  85 FG--GVDMLVNNAGqgRVSTFADTtdDAWRDELELKYFSV--INPTRAFLPL--LRASAAASIVCVNSLLALqpephmVA 158
                        170       180       190
                 ....*....|....*....|....*....|....
gi 755534620 171 LfggfySCSKYGVEAFSDVLRHEVQDFGVKVSII 204
Cdd:PRK07062 159 T-----SAARAGLLNLVKSLATELAPKGVRVNSI 187
PRK07856 PRK07856
SDR family oxidoreductase;
27-212 1.98e-04

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 42.23  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNktsdrLETVILDVTKTESIVAATQWVKERVGdrGL 106
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETVDGRP-----AEFHAADVRDPDQVAALVDAIVERHG--RL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 WGLVNNAGVlQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKK--ARGRIVNVSSALGRVALFG-GFYSCSKYGV 183
Cdd:PRK07856  77 DVLVNNAGG-SPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQqpGGGSIVNIGSVSGRRPSPGtAAYGAAKAGL 155
                        170       180       190
                 ....*....|....*....|....*....|.
gi 755534620 184 EAFSDVLRHEvqdFG--VKVSIIEPGSFKTE 212
Cdd:PRK07856 156 LNLTRSLAVE---WApkVRVNAVVVGLVRTE 183
PRK07102 PRK07102
SDR family oxidoreductase;
30-216 2.07e-04

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 41.83  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRV-LAACLTEK---GAEELRNKTSDRLETVILDVTKTESIVAATQWVKERvgdrg 105
Cdd:PRK07102   2 KKILIIGATSDIARACARRYAAAGARLyLAARDVERlerLADDLRARGAVAVSTHELDILDTASHAAFLDSLPAL----- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 106 LWGLVNNAGVL--QPFAYIEWyrpEDYMPIFQVNLIGltqvTISMLFLV-----KKARGRIVNVSSAL---GRVALFggF 175
Cdd:PRK07102  77 PDIVLIAVGTLgdQAACEADP---ALALREFRTNFEG----PIALLTLLanrfeARGSGTIVGISSVAgdrGRASNY--V 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 755534620 176 YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDA 216
Cdd:PRK07102 148 YGSAKAALTAFLSGLRNRLFKSGVHVLTVKPGFVRTPMTAG 188
PRK12744 PRK12744
SDR family oxidoreductase;
27-211 4.03e-04

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 41.26  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLE-----TVIL--DVTKTESIVAATQWVKE 99
Cdd:PRK12744   6 LKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSAASKADAEETVAAVKaagakAVAFqaDLTTAAAVEKLFDDAKA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 100 RVGDRGLwgLVNNAG-VL-QPFAYIEwyrPEDYMPIFQVNligltqvTISMLFLVKKA------RGRIVNVSSALgrVAL 171
Cdd:PRK12744  86 AFGRPDI--AINTVGkVLkKPIVEIS---EAEYDEMFAVN-------SKSAFFFIKEAgrhlndNGKIVTLVTSL--LGA 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 755534620 172 FGGFYSC---SKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKT 211
Cdd:PRK12744 152 FTPFYSAyagSKAPVEHFTRAASKEFGARGISVTAVGPGPMDT 194
PRK06197 PRK06197
short chain dehydrogenase; Provisional
34-164 5.23e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 41.16  E-value: 5.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  34 ITGCDSGFGNLLARQLDRRGMRV-LAACLTEKG---AEELRNKTSDRLETVI-LDVTKTESIVAATQWVKERVGDRGLwg 108
Cdd:PRK06197  21 VTGANTGLGYETAAALAAKGAHVvLAVRNLDKGkaaAARITAATPGADVTLQeLDLTSLASVRAAADALRAAYPRIDL-- 98
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755534620 109 LVNNAGVLqpfayiewYRP----EDYMPI-FQVNLIGLTQVTISMLFLVKKARG-RIVNVSS 164
Cdd:PRK06197  99 LINNAGVM--------YTPkqttADGFELqFGTNHLGHFALTGLLLDRLLPVPGsRVVTVSS 152
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
66-219 6.81e-04

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 40.54  E-value: 6.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  66 AEELRnKTSDRLETVILDVTKTESIVAATQWVKERVGDRGLwgLVNNA--GVLQPF-AYIEWYRPEDYMpifqVNLIGLT 142
Cdd:PRK12859  60 QEELL-KNGVKVSSMELDLTQNDAPKELLNKVTEQLGYPHI--LVNNAaySTNNDFsNLTAEELDKHYM----VNVRATT 132
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755534620 143 QVTISMLFLVKKARG-RIVNVSSALGRVALFGGF-YSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELT 219
Cdd:PRK12859 133 LLSSQFARGFDKKSGgRIINMTSGQFQGPMVGELaYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGWMTEEIK 211
PRK08703 PRK08703
SDR family oxidoreductase;
27-207 9.83e-04

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 39.91  E-value: 9.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---------RLEtvILDVTKTESIVAATQWV 97
Cdd:PRK08703   4 LSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEaghpepfaiRFD--LMSAEEKEFEQFAATIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  98 KERVGDrgLWGLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLI---GLTQVTISMLFLVKKARGRIVNVSSALGRVALFGG 174
Cdd:PRK08703  82 EATQGK--LDGIVHCAGYFYALSPLDFQTVAEWVNQYRINTVapmGLTRALFPLLKQSPDASVIFVGESHGETPKAYWGG 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 755534620 175 FySCSKYGVEAFSDVLRHEVQDFG-VKVSIIEPG 207
Cdd:PRK08703 160 F-GASKAALNYLCKVAADEWERFGnLRANVLVPG 192
PRK08278 PRK08278
SDR family oxidoreductase;
27-117 1.33e-03

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 39.50  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMR-VLAACLTEK----------GAEELRNKTSDRLeTVILDVTKTESIVAATQ 95
Cdd:PRK08278   4 LSGKTLFITGASRGIGLAIALRAARDGANiVIAAKTAEPhpklpgtihtAAEEIEAAGGQAL-PLVGDVRDEDQVAAAVA 82
                         90       100
                 ....*....|....*....|..
gi 755534620  96 WVKERVGdrGLWGLVNNAGVLQ 117
Cdd:PRK08278  83 KAVERFG--GIDICVNNASAIN 102
PRK07677 PRK07677
short chain dehydrogenase; Provisional
30-237 1.34e-03

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 39.66  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRN--KTSD-RLETVILDVTKTESIVAATQWVKERVGDrgL 106
Cdd:PRK07677   2 KVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLeiEQFPgQVLTVQMDVRNPEDVQKMVEQIDEKFGR--I 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 107 WGLVNNAG--VLQPfayIEWYRPEDYMPIFQVNLIGLTQVT--ISMLFLVKKARGRIVNVSSALGRVALFGGFYS-CSKY 181
Cdd:PRK07677  80 DALINNAAgnFICP---AEDLSVNGWNSVIDIVLNGTFYCSqaVGKYWIEKGIKGNIINMVATYAWDAGPGVIHSaAAKA 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755534620 182 GVEAFSDVLRHEV-QDFGVKVSIIEPGSfktemtdaeltIERT---KKVW--EAAPEHIKES 237
Cdd:PRK07677 157 GVLAMTRTLAVEWgRKYGIRVNAIAPGP-----------IERTggaDKLWesEEAAKRTIQS 207
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
27-216 2.83e-03

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 38.55  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAclTEKGAEE-------LRNKTSDRLeTVILDVTKTE---SIVAATQw 96
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVN--AKKRAEEmnetlkmVKENGGEGI-GVLADVSTREgceTLAKATI- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  97 vkERVGdrGLWGLVNNAGV--LQPF-----AYIEWYRPEDYMPIfqvnlIGLTQvtisMLFLVKKARGRIVNVSSALGRV 169
Cdd:PRK06077  80 --DRYG--VADILVNNAGLglFSPFlnvddKLIDKHISTDFKSV-----IYCSQ----ELAKEMREGGAIVNIASVAGIR 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 755534620 170 ALFG-GFYSCSKYGVEAFSDVLRHEVQDfGVKVSIIEPGSFKTEMTDA 216
Cdd:PRK06077 147 PAYGlSIYGAMKAAVINLTKYLALELAP-KIRVNAIAPGFVKTKLGES 193
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
32-207 4.39e-03

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


Pssm-ID: 223528 [Multi-domain]  Cd Length: 314  Bit Score: 38.38  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  32 VFITGCdSGF-GNLLARQLDRRGMRVLAACLTEKGAEELRnktsDRLETVILDVTKTESIVAATQWVKERVgdrglwglV 110
Cdd:COG0451    3 ILVTGG-AGFiGSHLVERLLAAGHDVRGLDRLRDGLDPLL----SGVEFVVLDLTDRDLVDELAKGVPDAV--------I 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 111 NNAGVlqpfAYIEWYRPEDYMPIFQVNLIGLTQVtisMLFLVKKARGRIVNVSSA--------------LGRVALFGGFY 176
Cdd:COG0451   70 HLAAQ----SSVPDSNASDPAEFLDVNVDGTLNL---LEAARAAGVKRFVFASSVsvvygdppplpideDLGPPRPLNPY 142
                        170       180       190
                 ....*....|....*....|....*....|.
gi 755534620 177 SCSKYGVEAfsdVLRHEVQDFGVKVSIIEPG 207
Cdd:COG0451  143 GVSKLAAEQ---LLRAYARLYGLPVVILRPF 170
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
30-164 6.04e-03

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


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 37.56  E-value: 6.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGdrGLWGL 109
Cdd:cd09761    2 KVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLG--RIDVL 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534620 110 VNNA-----GVLQPFAYIEWYRpedympIFQVNLIGLTQVTISMLFLVKKARGRIVNVSS 164
Cdd:cd09761   80 VNNAargskGILSSLLLEEWDR------ILSVNLTGPYELSRYCRDELIKNKGRIINIAS 133
 
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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