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Conserved domains on  [gi|74750135|sp|Q7Z5J1|]
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RecName: Full=Hydroxysteroid 11-beta-dehydrogenase 1-like protein; AltName: Full=11-beta-hydroxysteroid dehydrogenase type 3; Short=11-DH3; Short=11-beta-HSD3; AltName: Full=Short chain dehydrogenase/reductase family 26C member 2; AltName: Full=Short-chain dehydrogenase/reductase 10; Flags: Precursor

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 ...
 27-229 2.15e-78

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 cd05332:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 257  Bit Score: 239.41  E-value: 2.15e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVPLDMSDLEDAEQVVEEALKLFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 107 GLDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTD-SKGSLVVVSSLLGRVPTSFSTPYSAAKFAL 185
Cdd:cd05332  81 GLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIErSQGSIVVVSSIAGKIGVPFRTAYAASKHAL 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 74750135 186 DGFFGSLRRELdvQDVNVAITMCVLGLRDRASAAEAVRSSTSRP 229
Cdd:cd05332 161 QGFFDSLRAEL--SEPNISVTVVCPGLIDTNIAMNALSGDGSMS 202
 
Name Accession Description Interval E-value
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 27-229 2.15e-78

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: 239.41  E-value: 2.15e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVPLDMSDLEDAEQVVEEALKLFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 107 GLDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTD-SKGSLVVVSSLLGRVPTSFSTPYSAAKFAL 185
Cdd:cd05332  81 GLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIErSQGSIVVVSSIAGKIGVPFRTAYAASKHAL 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 74750135 186 DGFFGSLRRELdvQDVNVAITMCVLGLRDRASAAEAVRSSTSRP 229
Cdd:cd05332 161 QGFFDSLRAEL--SEPNISVTVVCPGLIDTNIAMNALSGDGSMS 202
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
26-203 1.56e-42

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 146.94  E-value: 1.56e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:COG0300   2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGA-RVEVVALDVTDPDAVAALAEAVLARF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 106 GGLDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDS-KGSLVVVSSLLGRVPTSFSTPYSAAKFA 184
Cdd:COG0300  81 GPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARgRGRIVNVSSVAGLRGLPGMAAYAASKAA 160

                       170
                ....*....|....*....
gi 74750135 185 LDGFFGSLRRELDVQDVNV 203
Cdd:COG0300 161 LEGFSESLRAELAPTGVRV 179
PRK06181 PRK06181
SDR family oxidoreductase;
29-205 6.60e-37

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 132.79  E-value: 6.60e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   29 GARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPkVFYIAADMASPEAPESVVQFALDKLGGL 108
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGE-ALVVPTDVSDAEACERLIEAAVARFGGI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  109 DYLVLNhiggapAGTRARSPQAT-------RWLMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAA 181
Cdd:PRK06181  80 DILVNN------AGITMWSRFDEltdlsvfERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTRSGYAAS 153

                        170       180
                 ....*....|....*....|....
gi 74750135  182 KFALDGFFGSLRRELDVQDVNVAI 205
Cdd:PRK06181 154 KHALHGFFDSLRIELADDGVAVTV 177
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 32-196 1.39e-35

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 127.34  E-value: 1.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135    32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGaPKVFYIAADMASPEAPESVVQFALDKLGGLDYL 111
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALG-GKALFIQGDVTDRAQVKALVEQAVERLGRLDIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   112 VlNHIGGAPAGTRAR-SPQATRWLMQVNFVSYVQLTSRALPSLTD-SKGSLVVVSSLLGRVPTSFSTPYSAAKFALDGFF 189
Cdd:pfam00106  82 V-NNAGITGLGPFSElSDEDWERVIDVNLTGVFNLTRAVLPAMIKgSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160


                  ....*..
gi 74750135   190 GSLRREL 196
Cdd:pfam00106 161 RSLALEL 167
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 32-109 4.29e-03

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 37.46  E-value: 4.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135     32 VLLTGANAGVGEELAYHYARLG-SHLVLT---AHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLGG 107
Cdd:smart00822   3 YLITGGLGGLGRALARWLAERGaRRLVLLsrsGPDAPGAAALLAELEAAGA-RVTVVACDVADRDALAAVLAAIPAVEGP 81


                   ..
gi 74750135    108 LD 109
Cdd:smart00822  82 LT 83
 
Name Accession Description Interval E-value
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 27-229 2.15e-78

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: 239.41  E-value: 2.15e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVPLDMSDLEDAEQVVEEALKLFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 107 GLDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTD-SKGSLVVVSSLLGRVPTSFSTPYSAAKFAL 185
Cdd:cd05332  81 GLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIErSQGSIVVVSSIAGKIGVPFRTAYAASKHAL 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 74750135 186 DGFFGSLRRELdvQDVNVAITMCVLGLRDRASAAEAVRSSTSRP 229
Cdd:cd05332 161 QGFFDSLRAEL--SEPNISVTVVCPGLIDTNIAMNALSGDGSMS 202
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
26-203 1.56e-42

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 146.94  E-value: 1.56e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:COG0300   2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGA-RVEVVALDVTDPDAVAALAEAVLARF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 106 GGLDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDS-KGSLVVVSSLLGRVPTSFSTPYSAAKFA 184
Cdd:COG0300  81 GPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARgRGRIVNVSSVAGLRGLPGMAAYAASKAA 160

                       170
                ....*....|....*....
gi 74750135 185 LDGFFGSLRRELDVQDVNV 203
Cdd:COG0300 161 LEGFSESLRAELAPTGVRV 179
PRK06181 PRK06181
SDR family oxidoreductase;
29-205 6.60e-37

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 132.79  E-value: 6.60e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   29 GARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPkVFYIAADMASPEAPESVVQFALDKLGGL 108
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGE-ALVVPTDVSDAEACERLIEAAVARFGGI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  109 DYLVLNhiggapAGTRARSPQAT-------RWLMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAA 181
Cdd:PRK06181  80 DILVNN------AGITMWSRFDEltdlsvfERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTRSGYAAS 153

                        170       180
                 ....*....|....*....|....
gi 74750135  182 KFALDGFFGSLRRELDVQDVNVAI 205
Cdd:PRK06181 154 KHALHGFFDSLRIELADDGVAVTV 177
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 32-196 1.39e-35

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 127.34  E-value: 1.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135    32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGaPKVFYIAADMASPEAPESVVQFALDKLGGLDYL 111
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALG-GKALFIQGDVTDRAQVKALVEQAVERLGRLDIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   112 VlNHIGGAPAGTRAR-SPQATRWLMQVNFVSYVQLTSRALPSLTD-SKGSLVVVSSLLGRVPTSFSTPYSAAKFALDGFF 189
Cdd:pfam00106  82 V-NNAGITGLGPFSElSDEDWERVIDVNLTGVFNLTRAVLPAMIKgSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160


                  ....*..
gi 74750135   190 GSLRREL 196
Cdd:pfam00106 161 RSLALEL 167
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 32-203 3.18e-33

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: 122.39  E-value: 3.18e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNcrKLGAPKVFYIAADMASPEAPESVVQFALDKLGGLDYL 111
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAI--EALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDIL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 112 VLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSL-TDSKGSLVVVSSLLGRVPTSFSTPYSAAKFALDGFFG 190
Cdd:cd05233  79 VNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMkKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTR 158

                       170
                ....*....|...
gi 74750135 191 SLRRELDVQDVNV 203
Cdd:cd05233 159 SLALELAPYGIRV 171
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 25-196 1.25e-32

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


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 121.05  E-value: 1.25e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  25 ASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDK 104
Cdd:COG1028   2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGG-RALAVAADVTDEAAVEALVAAAVAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 105 LGGLDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAKF 183
Cdd:COG1028  81 FGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGgGRIVNISSIAGLRGSPGQAAYAASKA 160

                       170
                ....*....|...
gi 74750135 184 ALDGFFGSLRREL 196
Cdd:COG1028 161 AVVGLTRSLALEL 173
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 26-205 5.70e-30

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


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 113.74  E-value: 5.70e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVgncRKLGApKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:COG4221   2 SDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALA---AELGG-RALAVPLDVTDEAAVEAAVAAAVAEF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 106 GGLDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAKFA 184
Cdd:COG4221  78 GRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGsGHIVNISSIAGLRPYPGGAVYAATKAA 157

                       170       180
                ....*....|....*....|.
gi 74750135 185 LDGFFGSLRRELDVQDVNVAI 205
Cdd:COG4221 158 VRGLSESLRAELRPTGIRVTV 178
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 29-203 3.13e-29

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: 111.96  E-value: 3.13e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  29 GARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAP---KVFYIAADMASPEAPESVVQfALDKL 105
Cdd:cd08939   1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEANAsgqKVSYISADLSDYEEVEQAFA-QAVEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 106 GGLDYLVLNHIGGA-PAGTRARSPQATRWLMQVNFVSYVQLTSRALPS-LTDSKGSLVVVSSLLGRVPTSFSTPYSAAKF 183
Cdd:cd08939  80 GGPPDLVVNCAGISiPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLmKEQRPGHIVFVSSQAALVGIYGYSAYCPSKF 159

                       170       180
                ....*....|....*....|
gi 74750135 184 ALDGFFGSLRRELDVQDVNV 203
Cdd:cd08939 160 ALRGLAESLRQELKPYNIRV 179
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 32-207 8.54e-26

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: 102.46  E-value: 8.54e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLGGLDYL 111
Cdd:cd05360   3 VVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGG-EAIAVVADVADAAQVERAADTAVERFGRIDTW 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 112 VLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTD-SKGSLVVVSSLLGRVPTSFSTPYSAAKFALDGFFG 190
Cdd:cd05360  82 VNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRrGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTE 161

                       170
                ....*....|....*..
gi 74750135 191 SLRRELDVQDVNVAITM 207
Cdd:cd05360 162 SLRAELAHDGAPISVTL 178
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 32-241 4.96e-25

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: 100.77  E-value: 4.96e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVvgncRKLGAPKVFYIAADMASPEAPESVVQFALDKLGGLDYL 111
Cdd:cd05374   3 VLITGCSSGIGLALALALAAQGYRVIATARNPDKLESL----GELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 112 VLN---HIGGAPAGTrarSPQATRWLMQVNFVSYVQLTSRALPSL-TDSKGSLVVVSSLLGRVPTSFSTPYSAAKFALDG 187
Cdd:cd05374  79 VNNagyGLFGPLEET---SIEEVRELFEVNVFGPLRVTRAFLPLMrKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEA 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 74750135 188 FFGSLRRELdvQDVNVAITMCVLGlrdrasaaeAVRSSTSRPRQPEHRGVPLQS 241
Cdd:cd05374 156 LSESLRLEL--APFGIKVTIIEPG---------PVRTGFADNAAGSALEDPEIS 198
PRK09072 PRK09072
SDR family oxidoreductase;
27-203 3.39e-24

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 98.86  E-value: 3.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVvgnCRKLGAP-KVFYIAADMASPEAPESVVQFALdKL 105
Cdd:PRK09072   3 LKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEAL---AARLPYPgRHRWVVADLTSEAGREAVLARAR-EM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  106 GGLDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLT-DSKGSLVVVSSLLGRVPTSFSTPYSAAKFA 184
Cdd:PRK09072  79 GGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRaQPSAMVVNVGSTFGSIGYPGYASYCASKFA 158

                        170
                 ....*....|....*....
gi 74750135  185 LDGFFGSLRRELDVQDVNV 203
Cdd:PRK09072 159 LRGFSEALRRELADTGVRV 177
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 25-203 6.20e-24

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 98.21  E-value: 6.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   25 ASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVgncRKLGAPKVFYIAADMASPEAPESVVQFALDK 104
Cdd:PRK12829   7 KPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATA---ARLPGAKVTATVADVADPAQVERVFDTAVER 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  105 LGGLDYLVlNHIGGAP--AGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSK--GSLVVVSSLLGRVPTSFSTPYSA 180
Cdd:PRK12829  84 FGGLDVLV-NNAGIAGptGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGhgGVIIALSSVAGRLGYPGRTPYAA 162

                        170       180
                 ....*....|....*....|...
gi 74750135  181 AKFALDGFFGSLRRELDVQDVNV 203
Cdd:PRK12829 163 SKWAVVGLVKSLAIELGPLGIRV 185
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 27-203 9.92e-24

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: 97.48  E-value: 9.92e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAP--KVFYIAADMASPEAPESVVQFALDK 104
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVSekKILLVVADLTEEEGQDRIISTTLAK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 105 LGGLDYLVLNhiGGAPAGTRARSPQATRW--LMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAAK 182
Cdd:cd05364  81 FGRLDILVNN--AGILAKGGGEDQDIEEYdkVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGRSFPGVLYYCISK 158

                       170       180
                ....*....|....*....|.
gi 74750135 183 FALDGFFGSLRRELDVQDVNV 203
Cdd:cd05364 159 AALDQFTRCTALELAPKGVRV 179
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 26-229 5.02e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 93.50  E-value: 5.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVgncRKLGAP-KVFYIAADMASPEAPESVVQFALDK 104
Cdd:PRK05872   6 SLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALA---AELGGDdRVLTVVADVTDLAAMQAAAEEAVER 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  105 LGGLDYLVLNhIGGAPAGTRARS-PQATRWLMQVNFVSyVQLTSRA-LPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAAK 182
Cdd:PRK05872  83 FGGIDVVVAN-AGIASGGSVAQVdPDAFRRVIDVNLLG-VFHTVRAtLPALIERRGYVLQVSSLAAFAAAPGMAAYCASK 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 74750135  183 FALDGFFGSLRRELDVQDVNVAI-------TMCVLGLRDRASAAEAVRSSTSRP 229
Cdd:PRK05872 161 AGVEAFANALRLEVAHHGVTVGSaylswidTDLVRDADADLPAFRELRARLPWP 214
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 32-207 1.71e-20

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 89.98  E-value: 1.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLGGLDYL 111
Cdd:PRK07109  11 VVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGG-EALAVVADVADAEAVQAAADRAEEELGPIDTW 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  112 VLNhiggAPAGTRARSPQAT----RWLMQVNFVSYVQLTSRALPSLT-DSKGSLVVVSSLLGRVPTSFSTPYSAAKFALD 186
Cdd:PRK07109  90 VNN----AMVTVFGPFEDVTpeefRRVTEVTYLGVVHGTLAALRHMRpRDRGAIIQVGSALAYRSIPLQSAYCAAKHAIR 165

                        170       180
                 ....*....|....*....|.
gi 74750135  187 GFFGSLRRELDVQDVNVAITM 207
Cdd:PRK07109 166 GFTDSLRCELLHDGSPVSVTM 186
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 26-207 3.07e-20

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 87.44  E-value: 3.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:PRK07666   4 SLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAYGV-KVVIATADVSDYEEVTAAIEQLKNEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  106 GGLDYLVlNHIGGAPAGTRARSPQATrW--LMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAK 182
Cdd:PRK07666  83 GSIDILI-NNAGISKFGKFLELDPAE-WekIIQVNLMGVYYATRAVLPSMIERQsGDIINISSTAGQKGAAVTSAYSASK 160

                        170       180
                 ....*....|....*....|....*
gi 74750135  183 FALDGFFGSLRRELDVQDVNVaITM 207
Cdd:PRK07666 161 FGVLGLTESLMQEVRKHNIRV-TAL 184
PRK07454 PRK07454
SDR family oxidoreductase;
31-195 1.80e-19

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 85.40  E-value: 1.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   31 RVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLGGLDY 110
Cdd:PRK07454   8 RALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTGV-KAAAYSIDLSNPEAIAPGIAELLEQFGCPDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  111 LVlNHIGGAPAGTRARSPQAT-RWLMQVNFVSYVQLTSRALPSLTDSKGSLVV-VSSLLGRVPTSFSTPYSAAKFALDGF 188
Cdd:PRK07454  87 LI-NNAGMAYTGPLLEMPLSDwQWVIQLNLTSVFQCCSAVLPGMRARGGGLIInVSSIAARNAFPQWGAYCVSKAALAAF 165


                 ....*..
gi 74750135  189 FGSLRRE 195
Cdd:PRK07454 166 TKCLAEE 172
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 32-209 2.47e-19

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: 85.37  E-value: 2.47e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAaDMASPEAPESVVQFALDKLGGLDYL 111
Cdd:cd05339   2 VLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVHYYKC-DVSKREEVYEAAKKIKKEVGDVTIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 112 VLNhiggapAGTRAR------SPQATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAKFA 184
Cdd:cd05339  81 INN------AGVVSGkkllelPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNhGHIVTIASVAGLISPAGLADYCASKAA 154

                       170       180
                ....*....|....*....|....*
gi 74750135 185 LDGFFGSLRRELDVQDVNVAITMCV 209
Cdd:cd05339 155 AVGFHESLRLELKAYGKPGIKTTLV 179
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 29-196 2.61e-19

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: 85.40  E-value: 2.61e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  29 GARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLGGL 108
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGA-GVLAVVADLTDPEDIDRLVEKAGDAFGRV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 109 DYLVLNhIGGAPAGTRArspQATR--WL--MQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAKF 183
Cdd:cd05344  80 DILVNN-AGGPPPGPFA---ELTDedWLeaFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLTVKEPEPNLVLSNVARA 155

                       170
                ....*....|...
gi 74750135 184 ALDGFFGSLRREL 196
Cdd:cd05344 156 GLIGLVKTLSREL 168
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
26-196 3.39e-19

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 84.83  E-value: 3.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:PRK05653   2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGG-EARVLVFDVSDEAAVRALIEAAVEAF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  106 GGLDYLVLNhIGGAPAGTRAR-SPQATRWLMQVNFVSYVQLTSRALPSLTDS-KGSLVVVSSLLGRVPTSFSTPYSAAKF 183
Cdd:PRK05653  81 GALDILVNN-AGITRDALLPRmSEEDWDRVIDVNLTGTFNVVRAALPPMIKArYGRIVNISSVSGVTGNPGQTNYSAAKA 159

                        170
                 ....*....|...
gi 74750135  184 ALDGFFGSLRREL 196
Cdd:PRK05653 160 GVIGFTKALALEL 172
PRK06139 PRK06139
SDR family oxidoreductase;
25-196 3.67e-19

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 86.31  E-value: 3.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   25 ASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDK 104
Cdd:PRK06139   3 GPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALGA-EVLVVPTDVTDADQVKALATQAASF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  105 LGGLDYLVlNHIGGAPAGTRARSP-QATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAK 182
Cdd:PRK06139  82 GGRIDVWV-NNVGVGAVGRFEETPiEAHEQVIQTNLIGYMRDAHAALPIFKKQGhGIFINMISLGGFAAQPYAAAYSASK 160

                        170
                 ....*....|....
gi 74750135  183 FALDGFFGSLRREL 196
Cdd:PRK06139 161 FGLRGFSEALRGEL 174
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 32-208 4.90e-19

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: 83.95  E-value: 4.90e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKvvgncRKLGAPKVFYIAADMASPEAPESVVQFALDKLGGLDYL 111
Cdd:cd08932   3 ALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAA-----LSASGGDVEAVPYDARDPEDARALVDALRDRFGRIDVL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 112 VLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDS-KGSLVVVSSLLGRVPTSFSTPYSAAKFALDGFFG 190
Cdd:cd08932  78 VHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAgSGRVVFLNSLSGKRVLAGNAGYSASKFALRALAH 157

                       170
                ....*....|....*...
gi 74750135 191 SLRRELDVQDVNVAiTMC 208
Cdd:cd08932 158 ALRQEGWDHGVRVS-AVC 174
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 27-233 6.46e-19

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: 84.13  E-value: 6.46e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:cd08934   1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGG-KALVLELDVTDEQQVDAAVERTVEALG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 107 GLDYLVLNhiggapAGTRARSP----QATRW--LMQVNFVSYVQLTSRALP-SLTDSKGSLVVVSSLLGRVPTSFSTPYS 179
Cdd:cd08934  80 RLDILVNN------AGIMLLGPvedaDTTDWtrMIDTNLLGLMYTTHAALPhHLLRNKGTIVNISSVAGRVAVRNSAVYN 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74750135 180 AAKFALDGFFGSLRRELDVQDVNVAIT---MCVLGLRDRAS-----AAEAVRSSTSRPRQPE 233
Cdd:cd08934 154 ATKFGVNAFSEGLRQEVTERGVRVVVIepgTVDTELRDHIThtitkEAYEERISTIRKLQAE 215
PRK12826 PRK12826
SDR family oxidoreductase;
25-234 6.63e-19

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 84.20  E-value: 6.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   25 ASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGaPKVFYIAADMASPEAPESVVQFALDK 104
Cdd:PRK12826   2 RDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAG-GKARARQVDVRDRAALKAAVAAGVED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  105 LGGLDYLVLNhIGGAPAGTRAR-SPQATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGR-VPTSFSTPYSAA 181
Cdd:PRK12826  81 FGRLDILVAN-AGIFPLTPFAEmDDEQWERVIDVNLTGTFLLTQAALPALIRAGgGRIVLTSSVAGPrVGYPGLAHYAAS 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74750135  182 KFALDGFFGSLRRELDVQDVNV------AITMCVLGLRDRASAAEAVRSSTSRPR--QPEH 234
Cdd:PRK12826 160 KAGLVGFTRALALELAARNITVnsvhpgGVDTPMAGNLGDAQWAEAIAAAIPLGRlgEPED 220
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 32-205 4.22e-18

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: 82.33  E-value: 4.22e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHL---VLTAHT---EALlqkvvgncRKLGAPKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:cd09805   3 VLITGCDSGFGNLLAKKLDSLGFTVlagCLTKNGpgaKEL--------RRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 106 G--GLDYLVLN-HIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAAK 182
Cdd:cd09805  75 GekGLWGLVNNaGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASK 154

                       170       180
                ....*....|....*....|...
gi 74750135 183 FALDGFFGSLRRELDVQDVNVAI 205
Cdd:cd09805 155 AAVEAFSDSLRRELQPWGVKVSI 177
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 36-196 8.24e-17

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


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 77.86  E-value: 8.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135    36 GA--NAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPkvfYIAADMASPEAPESVVQFALDKLGGLDYLVl 113
Cdd:pfam13561   1 GAanESGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAEELGAA---VLPCDVTDEEQVEALVAAAVEKFGRLDILV- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   114 NHIGGAPAGTRA---RSPQATRWLMQVNFVSYVQLTSRALPSLTDsKGSLVVVSSLLGRVPTSFSTPYSAAKFALDGFFG 190
Cdd:pfam13561  77 NNAGFAPKLKGPfldTSREDFDRALDVNLYSLFLLAKAALPLMKE-GGSIVNLSSIGAERVVPNYNAYGAAKAALEALTR 155


                  ....*.
gi 74750135   191 SLRREL 196
Cdd:pfam13561 156 YLAVEL 161
PRK05866 PRK05866
SDR family oxidoreductase;
23-203 1.08e-16

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 78.63  E-value: 1.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   23 DPASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFAL 102
Cdd:PRK05866  34 QPVDLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGG-DAMAVPCDLSDLDAVDALVADVE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  103 DKLGGLDYLVLNhiggapAGTRARSPQAT---RW-----LMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSS--LLGRVP 171
Cdd:PRK05866 113 KRIGGVDILINN------AGRSIRRPLAEsldRWhdverTMVLNYYAPLRLIRGLAPGMLERGdGHIINVATwgVLSEAS 186

                        170       180       190
                 ....*....|....*....|....*....|..
gi 74750135  172 TSFSTpYSAAKFALDGFFGSLRRELDVQDVNV 203
Cdd:PRK05866 187 PLFSV-YNASKAALSAVSRVIETEWGDRGVHS 217
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 23-203 2.18e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 77.25  E-value: 2.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   23 DPASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTeallqkvvgnCRKLGAPKVFYIAADMASPEAPESVVQFAL 102
Cdd:PRK06523   3 FFLELAGKRALVTGGTKGIGAATVARLLEAGARVVTTARS----------RPDDLPEGVEFVAADLTTAEGCAAVARAVL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  103 DKLGGLDYLVlNHIGG--APAGTRARSPQAtRWL--MQVNFVSYVQLTSRALPSLTDS-KGSLVVVSSLLGRVPTSFST- 176
Cdd:PRK06523  73 ERLGGVDILV-HVLGGssAPAGGFAALTDE-EWQdeLNLNLLAAVRLDRALLPGMIARgSGVIIHVTSIQRRLPLPESTt 150

                        170       180
                 ....*....|....*....|....*..
gi 74750135  177 PYSAAKFALDGFFGSLRRELDVQDVNV 203
Cdd:PRK06523 151 AYAAAKAALSTYSKSLSKEVAPKGVRV 177
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 21-269 2.19e-16

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 77.19  E-value: 2.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   21 NFDPASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQF 100
Cdd:PRK06113   3 NSDNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGG-QAFACRCDITSEQELSALADF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  101 ALDKLGGLDYLVLNHIGGAPAGTRArsPQAT-RWLMQVNFVSYVQLTSRALPSLTDSKGSLVV-VSSLLGRVPTSFSTPY 178
Cdd:PRK06113  82 ALSKLGKVDILVNNAGGGGPKPFDM--PMADfRRAYELNVFSFFHLSQLVAPEMEKNGGGVILtITSMAAENKNINMTSY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  179 SAAKFALDgffgSLRReldvqdvNVAITMCVLGLRDRASAAEAVRSSTsrprqpehrgvplqsqTAMFLPPTVPGArTLT 258
Cdd:PRK06113 160 ASSKAAAS----HLVR-------NMAFDLGEKNIRVNGIAPGAILTDA----------------LKSVITPEIEQK-MLQ 211

                        250
                 ....*....|.
gi 74750135  259 ETPLRGWPQPK 269
Cdd:PRK06113 212 HTPIRRLGQPQ 222
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 29-183 2.22e-16

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: 77.26  E-value: 2.22e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  29 GARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRK-LGAPKVFYIAADMASpeaPESVVQFA---LDK 104
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKeTGNAKVEVIQLDLSS---LASVRQFAeefLAR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 105 LGGLDYLVLNhiGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSKGS-LVVVSSLLGRVPT--------SFS 175
Cdd:cd05327  78 FPRLDILINN--AGIMAPPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSrIVNVSSIAHRAGPidfndldlENN 155


                ....*...
gi 74750135 176 TPYSAAKF 183
Cdd:cd05327 156 KEYSPYKA 163
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 26-196 2.24e-16

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 77.22  E-value: 2.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAH-TEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDK 104
Cdd:PRK12825   3 SLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEAVEALGR-RAQAVQADVTDKAALEAAVAAAVER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  105 LGGLDYLVLNhiggapAGTRARSPQA----TRW--LMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTP 177
Cdd:PRK12825  82 FGRIDILVNN------AGIFEDKPLAdmsdDEWdeVIDVNLSGVFHLLRAVVPPMRKQRgGRIVNISSVAGLPGWPGRSN 155

                        170
                 ....*....|....*....
gi 74750135  178 YSAAKFALDGFFGSLRREL 196
Cdd:PRK12825 156 YAAAKAGLVGLTKALAREL 174
PRK07814 PRK07814
SDR family oxidoreductase;
23-185 2.38e-16

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 77.13  E-value: 2.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   23 DPASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFAL 102
Cdd:PRK07814   4 DRFRLDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGR-RAHVVAADLAHPEATAGLAGQAV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  103 DKLGGLDyLVLNHIGGA-PAGTRARSPQATRWLMQVNFVSYVQLTSRALPSL--TDSKGSLVVVSSLLGRVPTSFSTPYS 179
Cdd:PRK07814  83 EAFGRLD-IVVNNVGGTmPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMleHSGGGSVINISSTMGRLAGRGFAAYG 161


                 ....*.
gi 74750135  180 AAKFAL 185
Cdd:PRK07814 162 TAKAAL 167
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 32-208 2.88e-16

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: 76.57  E-value: 2.88e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVL-----TAHTEALLQkvvgncRKLGAPKVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:cd05323   3 AIITGGASGIGLATAKLLLKKGAKVAIldrneNPGAAAELQ------AINPKVKATFVQCDVTSWEQLAAAFKKAIEKFG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 107 GLDYLVLN--HIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSK----GSLVVVSSLLGRVPTSFSTPYSA 180
Cdd:cd05323  77 RVDILINNagILDEKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKggkgGVIVNIGSVAGLYPAPQFPVYSA 156

                       170       180
                ....*....|....*....|....*....
gi 74750135 181 AKFALDGFFGSLRRELDVQDvNVAI-TMC 208
Cdd:cd05323 157 SKHGVVGFTRSLADLLEYKT-GVRVnAIC 184
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-196 3.38e-16

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 76.42  E-value: 3.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHT-EALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDInEEAAQELLEEIKEEGG-DAIAVKADVSSEEDVENLVEQIVEKF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  106 GGLDYLVLN----HIGgaPAGTRarSPQATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSA 180
Cdd:PRK05565  82 GKIDILVNNagisNFG--LVTDM--TDEEWDRVIDVNLTGVMLLTRYALPYMIKRKsGVIVNISSIWGLIGASCEVLYSA 157

                        170
                 ....*....|....*.
gi 74750135  181 AKFALDGFFGSLRREL 196
Cdd:PRK05565 158 SKGAVNAFTKALAKEL 173
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 32-203 4.28e-16

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: 75.74  E-value: 4.28e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGS-HLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLGGLDY 110
Cdd:cd05324   3 ALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQAAVEKLRAEGL-SVRFHQLDVTDDASIEAAADFVEEKYGGLDI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 111 LVlNHIGGAPAGTRARSP--QATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVV-VSSLLGrvptSFSTPYSAAKFALDG 187
Cdd:cd05324  82 LV-NNAGIAFKGFDDSTPtrEQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVnVSSGLG----SLTSAYGVSKAALNA 156

                       170
                ....*....|....*.
gi 74750135 188 FFGSLRRELDVQDVNV 203
Cdd:cd05324 157 LTRILAKELKETGIKV 172
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 27-203 4.39e-16

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 76.53  E-value: 4.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGR-RALAVPTDITDEDQCANLVALALERFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  107 GLDYLVLNHIGGAPAGTRAR-SPQATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAAKFAL 185
Cdd:PRK07890  82 RVDALVNNAFRVPSMKPLADaDFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMINSMVLRHSQPKYGAYKMAKGAL 161

                        170
                 ....*....|....*...
gi 74750135  186 DGFFGSLRRELDVQDVNV 203
Cdd:PRK07890 162 LAASQSLATELGPQGIRV 179
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 32-203 4.97e-16

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: 75.85  E-value: 4.97e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVLT-AHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLGGLDY 110
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVVINyRKSKDAAAEVAAEIEELGG-KAVVVRADVSQPQDVEEMFAAVKERFGRLDV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 111 LVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLL-GRVPTSFsTPYSAAKFALDGF 188
Cdd:cd05359  80 LVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGgGRIVAISSLGsIRALPNY-LAVGTAKAALEAL 158

                       170
                ....*....|....*
gi 74750135 189 FGSLRRELDVQDVNV 203
Cdd:cd05359 159 VRYLAVELGPRGIRV 173
PRK07326 PRK07326
SDR family oxidoreductase;
26-207 5.73e-16

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 75.82  E-value: 5.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGapKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:PRK07326   3 SLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKG--NVLGLAADVRDEADVQRAVDAIVAAF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  106 GGLDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAAKFAL 185
Cdd:PRK07326  81 GGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGTNFFAGGAAYNASKFGL 160

                        170       180
                 ....*....|....*....|..
gi 74750135  186 DGFFGSLRRELDVQDVNVAITM 207
Cdd:PRK07326 161 VGFSEAAMLDLRQYGIKVSTIM 182
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 27-196 6.56e-16

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


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 75.58  E-value: 6.56e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVvgncrKLGAPKVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:COG3967   3 LTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEA-----AAANPGLHTIVLDVADPASIAALAEQVTAEFP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 107 GLDYLVLNhiggapAG--------TRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVV-VSSLLGRVPtSFSTP 177
Cdd:COG3967  78 DLNVLINN------AGimraedllDEAEDLADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVnVSSGLAFVP-LAVTP 150

                       170       180
                ....*....|....*....|
gi 74750135 178 -YSAAKFALDGFFGSLRREL 196
Cdd:COG3967 151 tYSATKAALHSYTQSLRHQL 170
PRK09242 PRK09242
SDR family oxidoreductase;
26-185 7.93e-16

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 75.55  E-value: 7.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCR-KLGAPKVFYIAADMASPEAPESVVQFALDK 104
Cdd:PRK09242   6 RLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAeEFPEREVHGLAADVSDDEDRRAILDWVEDH 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  105 LGGLDYLVLNhiggapAGTRAR------SPQATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTP 177
Cdd:PRK09242  86 WDGLHILVNN------AGGNIRkaaidyTEDEWRGIFETNLFSAFELSRYAHPLLKQHAsSAIVNIGSVSGLTHVRSGAP 159


                 ....*...
gi 74750135  178 YSAAKFAL 185
Cdd:PRK09242 160 YGMTKAAL 167
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 32-204 1.15e-15

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: 75.02  E-value: 1.15e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLG--SHLVLTAHTEALLQKVVGNCRklGAPKVFYIAADMASPEAPESVVQfALDKLGG-L 108
Cdd:cd05367   2 IILTGASRGIGRALAEELLKRGspSVVVLLARSEEPLQELKEELR--PGLRVTTVKADLSDAAGVEQLLE-AIRKLDGeR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 109 DYLVLNHIGGAPAGTRAR-SPQATRWLMQVNFVSYVQLTSRALPSLTDS--KGSLVVVSSLLGRVPTSFSTPYSAAKFAL 185
Cdd:cd05367  79 DLLINNAGSLGPVSKIEFiDLDELQKYFDLNLTSPVCLTSTLLRAFKKRglKKTVVNVSSGAAVNPFKGWGLYCSSKAAR 158

                       170       180
                ....*....|....*....|
gi 74750135 186 DGFFGSLRREL-DVQDVNVA 204
Cdd:cd05367 159 DMFFRVLAAEEpDVRVLSYA 178
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 26-203 2.49e-15

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 74.07  E-value: 2.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVL-TAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDK 104
Cdd:PRK05557   2 SLEGKVALVTGASRGIGRAIAERLAAQGANVVInYASSEAGAEALVAEIGALGG-KALAVQGDVSDAESVERAVDEAKAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  105 LGGLDYLVLNhiggapAGTRARSP---------QATrwlMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSF 174
Cdd:PRK05557  81 FGGVDILVNN------AGITRDNLlmrmkeedwDRV---IDTNLTGVFNLTKAVARPMMKQRsGRIINISSVVGLMGNPG 151

                        170       180
                 ....*....|....*....|....*....
gi 74750135  175 STPYSAAKFALDGFFGSLRRELDVQDVNV 203
Cdd:PRK05557 152 QANYAASKAGVIGFTKSLARELASRGITV 180
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 27-203 2.78e-15

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: 73.76  E-value: 2.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADM--ASPEAPESVVQFALDK 104
Cdd:cd05340   2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQPQWFILDLltCTSENCQQLAQRIAVN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 105 LGGLDYLVLN-HIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAK 182
Cdd:cd05340  82 YPRLDGVLHNaGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQGRANWGAYAVSK 161

                       170       180
                ....*....|....*....|.
gi 74750135 183 FALDGFFGSLRRELDVQDVNV 203
Cdd:cd05340 162 FATEGL*QVLADEYQQRNLRV 182
FabG-like PRK07231
SDR family oxidoreductase;
27-185 6.44e-15

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 72.94  E-value: 6.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRklGAPKVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEIL--AGGRAIAVAADVSDEADVEAAVAAALERFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  107 GLDYLVLNhiggapAGTRAR-------SPQATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVV-VSSLLGRVPTSFSTPY 178
Cdd:PRK07231  81 SVDILVNN------AGTTHRngplldvDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVnVASTAGLRPRPGLGWY 154


                 ....*..
gi 74750135  179 SAAKFAL 185
Cdd:PRK07231 155 NASKGAV 161
PRK05650 PRK05650
SDR family oxidoreductase;
31-203 7.07e-15

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 73.15  E-value: 7.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   31 RVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLGGLDY 110
Cdd:PRK05650   2 RVMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAGG-DGFYQRCDVRDYSQLTALAQACEEKWGGIDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  111 LVlNHIGGAPAGTRARSP-QATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAKFALDGF 188
Cdd:PRK05650  81 IV-NNAGVASGGFFEELSlEDWDWQIAINLMGVVKGCKAFLPLFKRQKsGRIVNIASMAGLMQGPAMSSYNVAKAGVVAL 159

                        170
                 ....*....|....*
gi 74750135  189 FGSLRRELDVQDVNV 203
Cdd:PRK05650 160 SETLLVELADDEIGV 174
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 24-197 1.68e-14

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 71.83  E-value: 1.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   24 PASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADM--ASPEAPESVVQFA 101
Cdd:PRK08945   7 PDLLKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIIPLDLltATPQNYQQLADTI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  102 LDKLGGLDYLVLNhiggapAGTR-ARSP----QATRW--LMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTS 173
Cdd:PRK08945  87 EEQFGRLDGVLHN------AGLLgELGPmeqqDPEVWqdVMQVNVNATFMLTQALLPLLLKSPaASLVFTSSSVGRQGRA 160

                        170       180
                 ....*....|....*....|....
gi 74750135  174 FSTPYSAAKFALDGFFGSLRRELD 197
Cdd:PRK08945 161 NWGAYAVSKFATEGMMQVLADEYQ 184
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 28-185 1.70e-14

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: 72.18  E-value: 1.70e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  28 QGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFALDKLGG 107
Cdd:cd08933   8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGSCKFVPCDVTKEEDIKTLISVTVERFGR 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 108 LDYLVlNHIGGAP--AGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAAKFAL 185
Cdd:cd08933  88 IDCLV-NNAGWHPphQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIGQKQAAPYVATKGAI 166
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 23-203 1.75e-14

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 71.93  E-value: 1.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   23 DPASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFAL 102
Cdd:PRK12939   1 MASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGG-RAHAIAADLADPASVQRFFDAAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  103 DKLGGLDYLVlNHIGGAPAGTRAR-SPQATRWLMQVNfVSYVQLTSR-ALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYS 179
Cdd:PRK12939  80 AALGGLDGLV-NNAGITNSKSATElDIDTWDAVMNVN-VRGTFLMLRaALPHLRDSGrGRIVNLASDTALWGAPKLGAYV 157

                        170       180
                 ....*....|....*....|....
gi 74750135  180 AAKFALDGFFGSLRRELDVQDVNV 203
Cdd:PRK12939 158 ASKGAVIGMTRSLARELGGRGITV 181
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 27-188 2.71e-14

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 71.46  E-value: 2.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAGG-KAIGVAMDVTDEEAINAGIDYAVETFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  107 GLDYLVLNhiggapAGTRARSP----QATRW--LMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYS 179
Cdd:PRK12429  81 GVDILVNN------AGIQHVAPiedfPTEKWkkMIAIMLDGAFLTTKAALPIMKAQGgGRIINMASVHGLVGSAGKAAYV 154


                 ....*....
gi 74750135  180 AAKFALDGF 188
Cdd:PRK12429 155 SAKHGLIGL 163
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 32-203 6.20e-14

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: 70.05  E-value: 6.20e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVgNCRKLGAPKVFYIAADMASPEAPESVVQFALDKLGGLDYL 111
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELK-AELLNPNPSVEVEILDVTDEERNQLVIAELEAELGGLDLV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 112 VLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAKFALDGFFG 190
Cdd:cd05350  80 IINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGrGHLVLISSVAALRGLPGAAAYSASKAALSSLAE 159

                       170
                ....*....|...
gi 74750135 191 SLRRELDVQDVNV 203
Cdd:cd05350 160 SLRYDVKKRGIRV 172
PRK05993 PRK05993
SDR family oxidoreductase;
32-205 7.72e-14

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 70.44  E-value: 7.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   32 VLLTGANAGVGeelaYHYARlgshlvltahteALLQ---KVVGNCRK------LGAPKVFYIAADMASPEAPESVVQFAL 102
Cdd:PRK05993   7 ILITGCSSGIG----AYCAR------------ALQSdgwRVFATCRKeedvaaLEAEGLEAFQLDYAEPESIAALVAQVL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  103 DKLGG-LDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSL-TDSKGSLVVVSSLLGRVPTSFSTPYSA 180
Cdd:PRK05993  71 ELSGGrLDALFNNGAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMrKQGQGRIVQCSSILGLVPMKYRGAYNA 150

                        170       180
                 ....*....|....*....|....*
gi 74750135  181 AKFALDGFFGSLRRELDVQDVNVAI 205
Cdd:PRK05993 151 SKFAIEGLSLTLRMELQGSGIHVSL 175
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 32-196 9.46e-14

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: 69.50  E-value: 9.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLGGLDYL 111
Cdd:cd05333   3 ALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGG-NAAALEADVSDREAVEALVEKVEAEFGPVDIL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 112 VLNhiggapAG-TR-----ARSPQATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAKFA 184
Cdd:cd05333  82 VNN------AGiTRdnllmRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRsGRIINISSVVGLIGNPGQANYAASKAG 155

                       170
                ....*....|..
gi 74750135 185 LDGFFGSLRREL 196
Cdd:cd05333 156 VIGFTKSLAKEL 167
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 32-196 9.66e-14

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: 69.62  E-value: 9.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFALDKLGGLDYL 111
Cdd:cd05346   3 VLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPVKVLPLQLDVSDRESIEAALENLPEEFRDIDIL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 112 VLNhiGGAPAGT-RARSPQATRW--LMQVNFVSYVQLTSRALPSLTD-SKGSLVVVSSLLGRVPTSFSTPYSAAKFALDG 187
Cdd:cd05346  83 VNN--AGLALGLdPAQEADLEDWetMIDTNVKGLLNVTRLILPIMIArNQGHIINLGSIAGRYPYAGGNVYCATKAAVRQ 160


                ....*....
gi 74750135 188 FFGSLRREL 196
Cdd:cd05346 161 FSLNLRKDL 169
PRK07201 PRK07201
SDR family oxidoreductase;
17-188 1.13e-13

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 71.52  E-value: 1.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   17 YWDDNFDPA---------SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAAD 87
Cdd:PRK07201 350 YWERHLDPDrarrrdlrgPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGG-TAHAYTCD 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   88 MASPEAPESVVQFALDKLGGLDYLVLNhiggapAGtRA--RSPQAT--RW-----LMQVNFVSYVQLTSRALPSLTDSK- 157
Cdd:PRK07201 429 LTDSAAVDHTVKDILAEHGHVDYLVNN------AG-RSirRSVENStdRFhdyerTMAVNYFGAVRLILGLLPHMRERRf 501

                        170       180       190
                 ....*....|....*....|....*....|...
gi 74750135  158 GSLVVVSS--LLGRVPtSFSTpYSAAKFALDGF 188
Cdd:PRK07201 502 GHVVNVSSigVQTNAP-RFSA-YVASKAALDAF 532
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
26-205 1.44e-13

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 69.38  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEAL--LQKVVGNCRKlgapKVFYIAADMASPEAPESVVQFALD 103
Cdd:PRK06935  12 SLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWdeTRRLIEKEGR----KVTFVQVDLTKPESAEKVVKEALE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  104 KLGGLDYLVLNhiggapAGTRARSPQA----TRW--LMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFST 176
Cdd:PRK06935  88 EFGKIDILVNN------AGTIRRAPLLeykdEDWnaVMDINLNSVYHLSQAVAKVMAKQGsGKIINIASMLSFQGGKFVP 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 74750135  177 PYSAAKFALDGFFGSLRRELDVQDVNV-AI 205
Cdd:PRK06935 162 AYTASKHGVAGLTKAFANELAAYNIQVnAI 191
PRK06124 PRK06124
SDR family oxidoreductase;
22-196 1.89e-13

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 68.97  E-value: 1.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   22 FDPASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFA 101
Cdd:PRK06124   4 LQRFSLAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGG-AAEALAFDIADEEAVAAAFARI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  102 LDKLGGLDYLVLNhiggapAGTRARSP------QATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSF 174
Cdd:PRK06124  83 DAEHGRLDILVNN------VGARDRRPlaelddAAIRALLETDLVAPILLSRLAAQRMKRQGyGRIIAITSIAGQVARAG 156

                        170       180
                 ....*....|....*....|..
gi 74750135  175 STPYSAAKFALDGFFGSLRREL 196
Cdd:PRK06124 157 DAVYPAAKQGLTGLMRALAAEF 178
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 32-205 2.33e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 68.78  E-value: 2.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   32 VLLTGANAGVGEELAYHYARLGShlvltahteallqKVVGNCRKLGA----PKVFYIAADMASPEAPESVVQFALDKLGG 107
Cdd:PRK06179   7 ALVTGASSGIGRATAEKLARAGY-------------RVFGTSRNPARaapiPGVELLELDVTDDASVQAAVDEVIARAGR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  108 LDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSL-TDSKGSLVVVSSLLGRVPTSFSTPYSAAKFALD 186
Cdd:PRK06179  74 IDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMrAQGSGRIINISSVLGFLPAPYMALYAASKHAVE 153

                        170
                 ....*....|....*....
gi 74750135  187 GFFGSLRRELDVQDVNVAI 205
Cdd:PRK06179 154 GYSESLDHEVRQFGIRVSL 172
PRK08219 PRK08219
SDR family oxidoreductase;
32-195 2.61e-13

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 68.04  E-value: 2.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   32 VLLTGANAGVGEELAYHYARlGSHLVLTAHTEALLQKVVGncrklGAPKVFYIAADMASPEAPESvvqfALDKLGGLDYL 111
Cdd:PRK08219   6 ALITGASRGIGAAIARELAP-THTLLLGGRPAERLDELAA-----ELPGATPFPVDLTDPEAIAA----AVEQLGRLDVL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  112 VLNhIGGAPAGTRARS-PQATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAAKFALDGFFG 190
Cdd:PRK08219  76 VHN-AGVADLGPVAEStVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRANPGWGSYAASKFALRALAD 154


                 ....*
gi 74750135  191 SLRRE 195
Cdd:PRK08219 155 ALREE 159
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 26-203 2.86e-13

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: 68.15  E-value: 2.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:cd05347   2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGV-EATAFTCDVSDEEAIKAAVEAIEEDF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 106 GGLDYLVLNhiggapAGTRARSP----QATRW--LMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPY 178
Cdd:cd05347  81 GKIDILVNN------AGIIRRHPaeefPEAEWrdVIDVNLNGVFFVSQAVARHMIKQGhGKIINICSLLSELGGPPVPAY 154

                       170       180
                ....*....|....*....|....*
gi 74750135 179 SAAKFALDGFFGSLRRELDVQDVNV 203
Cdd:cd05347 155 AASKGGVAGLTKALATEWARHGIQV 179
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 32-207 3.01e-13

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: 67.92  E-value: 3.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRklgaPKVFYIAADMASPEAPESVVQFALDKLGGLDYL 111
Cdd:cd08929   3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQEL----EGVLGLAGDVRDEADVRRAVDAMEEAFGGLDAL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 112 VLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPS-LTDSKGSLVVVSSLLGRVPTSFSTPYSAAKFALDGFFG 190
Cdd:cd08929  79 VNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPAlLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSE 158

                       170
                ....*....|....*..
gi 74750135 191 SLRRELDVQDVNVAITM 207
Cdd:cd08929 159 AAMLDLREANIRVVNVM 175
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 26-203 3.92e-13

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: 67.72  E-value: 3.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNcrklgAPKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:cd05370   2 KLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKE-----LPNIHTIVLDVGDAESVEALAEALLSEY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 106 GGLDYLVLNhiggapAGTR--------ARSPQATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVV-VSSLLGRVPTSFST 176
Cdd:cd05370  77 PNLDILINN------AGIQrpidlrdpASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVnVSSGLAFVPMAANP 150

                       170       180
                ....*....|....*....|....*..
gi 74750135 177 PYSAAKFALDGFFGSLRRELDVQDVNV 203
Cdd:cd05370 151 VYCATKAALHSYTLALRHQLKDTGVEV 177
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 26-186 5.12e-13

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: 67.47  E-value: 5.12e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:cd05329   3 NLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGF-KVEGSVCDVSSRSERQELMDTVASHF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 106 GG-LDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDS-KGSLVVVSSLLGRVPTSFSTPYSAAKF 183
Cdd:cd05329  82 GGkLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASgNGNIVFISSVAGVIAVPSGAPYGATKG 161


                ...
gi 74750135 184 ALD 186
Cdd:cd05329 162 ALN 164
PRK07774 PRK07774
SDR family oxidoreductase;
33-240 5.25e-13

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 67.46  E-value: 5.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   33 LLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFyIAADMASPEAPESVVQFALDKLGGLDYLV 112
Cdd:PRK07774  10 IVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIA-VQVDVSDPDSAKAMADATVSAFGGIDYLV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  113 LNH--IGGAPAGTRARSPQAT-RWLMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPtsFSTPYSAAKFALDGFF 189
Cdd:PRK07774  89 NNAaiYGGMKLDLLITVPWDYyKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWL--YSNFYGLAKVGLNGLT 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 74750135  190 GSLRRELDVQDVNV-AITMcvlGLRDrasaAEAVRSSTSRP-RQPEHRGVPLQ 240
Cdd:PRK07774 167 QQLARELGGMNIRVnAIAP---GPID----TEATRTVTPKEfVADMVKGIPLS 212
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 32-203 5.78e-13

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: 67.21  E-value: 5.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLGGLDYL 111
Cdd:cd05365   2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGG-QAIGLECNVTSEQDLEAVVKATVSQFGGITIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 112 VLNHIGGAPAgtRARSPQAT---RWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAKFALDG 187
Cdd:cd05365  81 VNNAGGGGPK--PFDMPMTEedfEWAFKLNLFSAFRLSQLCAPHMQKAGgGAILNISSMSSENKNVRIAAYGSSKAAVNH 158

                       170
                ....*....|....*.
gi 74750135 188 FFGSLRRELDVQDVNV 203
Cdd:cd05365 159 MTRNLAFDLGPKGIRV 174
PRK07806 PRK07806
SDR family oxidoreductase;
24-165 1.28e-12

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 66.28  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   24 PASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEA-LLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFAL 102
Cdd:PRK07806   1 MGDLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKApRANKVVAEIEAAGG-RASAVGADLTDEESVAALMDTAR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74750135  103 DKLGGLDYLVLNHIGGAPAGTrarspqATRWLMQVNFVSYVQLTSRALPsLTDSKGSLVVVSS 165
Cdd:PRK07806  80 EEFGGLDALVLNASGGMESGM------DEDYAMRLNRDAQRNLARAALP-LMPAGSRVVFVTS 135
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 26-228 1.31e-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: 1.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCrklgaPKVFYIAADMASPEApesvVQFALDKL 105
Cdd:cd05351   4 DFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVREC-----PGIEPVCVDLSDWDA----TEEALGSV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 106 GGLDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDS--KGSLVVVSSLLGRVPTSFSTPYSAAKF 183
Cdd:cd05351  75 GPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARgvPGSIVNVSSQASQRALTNHTVYCSTKA 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 74750135 184 ALDGFFGSLRRELD-----VQDVNVAITMCVLGlRDRASAAEAVRSSTSR 228
Cdd:cd05351 155 ALDMLTKVMALELGphkirVNSVNPTVVMTDMG-RDNWSDPEKAKKMLNR 203
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 27-192 1.99e-12

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: 65.69  E-value: 1.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:cd05369   1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLKEFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 107 GLDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSK--GSLVVVSSLLGRVPTSFSTPYSAAKFA 184
Cdd:cd05369  81 KIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKhgGSILNISATYAYTGSPFQVHSAAAKAG 160


                ....*...
gi 74750135 185 LDGFFGSL 192
Cdd:cd05369 161 VDALTRSL 168
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 26-203 4.41e-12

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 65.03  E-value: 4.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:PRK12935   3 QLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  106 GGLDYLVLNhiggapAG-TRARSPQATR---W--LMQVNFVSYVQLTSRALPSLTDSKGSLVV-VSSLLGRVPTSFSTPY 178
Cdd:PRK12935  83 GKVDILVNN------AGiTRDRTFKKLNredWerVIDVNLSSVFNTTSAVLPYITEAEEGRIIsISSIIGQAGGFGQTNY 156

                        170       180
                 ....*....|....*....|....*
gi 74750135  179 SAAKFALDGFFGSLRRELDVQDVNV 203
Cdd:PRK12935 157 SAAKAGMLGFTKSLALELAKTNVTV 181
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 33-206 9.39e-12

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: 64.07  E-value: 9.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  33 LLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFALDKLGGLDYLV 112
Cdd:cd05343  10 LVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLFPYQCDLSNEEQILSMFSAIRTQHQGVDVCI 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 113 LNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSK---GSLVVVSSLLG-RVP-TSFSTPYSAAKFALDG 187
Cdd:cd05343  90 NNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNvddGHIININSMSGhRVPpVSVFHFYAATKHAVTA 169

                       170
                ....*....|....*....
gi 74750135 188 FFGSLRRELDVQDVNVAIT 206
Cdd:cd05343 170 LTEGLRQELREAKTHIRAT 188
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 25-195 1.89e-11

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 63.38  E-value: 1.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   25 ASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDK 104
Cdd:PRK13394   3 SNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGG-KAIGVAMDVTNEDAVNAGIDKVAER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  105 LGGLDYLVLNhiggapAGTRARSP----QATRW-LMQVNFVSYVQLTSR-ALPSLT--DSKGSLVVVSSLLGRVPTSFST 176
Cdd:PRK13394  82 FGSVDILVSN------AGIQIVNPienySFADWkKMQAIHVDGAFLTTKaALKHMYkdDRGGVVIYMGSVHSHEASPLKS 155

                        170
                 ....*....|....*....
gi 74750135  177 PYSAAKFALDGFFGSLRRE 195
Cdd:PRK13394 156 AYVTAKHGLLGLARVLAKE 174
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 24-187 2.59e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 62.72  E-value: 2.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   24 PASLQGARVLLTGANAGVGEELAYHYARLG-SHLVLTAHTEALLQKVVGNCRKLGAPKVFyIAADMASPEAPESVVQFAL 102
Cdd:PRK06198   1 MGRLDGKVALVTGGTQGLGAAIARAFAERGaAGLVICGRNAEKGEAQAAELEALGAKAVF-VQADLSDVEDCRRVVAAAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  103 DKLGGLDYLVlnhiggAPAGTRAR------SPQATRWLMQVNFVSYVQLTSRALPSLTDSK--GSLVVVSSLLGRVPTSF 174
Cdd:PRK06198  80 EAFGRLDALV------NAAGLTDRgtildtSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKaeGTIVNIGSMSAHGGQPF 153

                        170
                 ....*....|...
gi 74750135  175 STPYSAAKFALDG 187
Cdd:PRK06198 154 LAAYCASKGALAT 166
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
24-185 5.20e-11

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 63.33  E-value: 5.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   24 PASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVvgnCRKLGAPKVFY-IAADMASPEAPESVVQFAL 102
Cdd:PRK08324 417 PKPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAA---AAELGGPDRALgVACDVTDEAAVQAAFEEAA 493

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  103 DKLGGLDYLVLNhIGGAPAGTRA-RSPQATRWLMQVNFVSYvQLTSR-ALPSLTDSK--GSLVVVSSLLGRVPTSFSTPY 178
Cdd:PRK08324 494 LAFGGVDIVVSN-AGIAISGPIEeTSDEDWRRSFDVNATGH-FLVAReAVRIMKAQGlgGSIVFIASKNAVNPGPNFGAY 571


                 ....*..
gi 74750135  179 SAAKFAL 185
Cdd:PRK08324 572 GAAKAAE 578
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 27-163 5.43e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 61.98  E-value: 5.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFAldklG 106
Cdd:PRK06125   5 LAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGVDVAVHALDLSSPEAREQLAAEA----G 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  107 GLDYLVlNHIGGAPAGTRARSPQAT---RWLMQVnfVSYVQLTSRALPSLTdSKGSLVVV 163
Cdd:PRK06125  81 DIDILV-NNAGAIPGGGLDDVDDAAwraGWELKV--FGYIDLTRLAYPRMK-ARGSGVIV 136
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 27-196 7.06e-11

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: 61.32  E-value: 7.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVvgnCRKLGAPKVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:cd05326   2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAV---AAELGDPDISFVHCDVTVEADVRAAVDTAVARFG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 107 GLDYLVlNHIG--GAPAGtRARSPQATRW--LMQVNFVSYVQLTSRALPSLT-DSKGSLVVVSSLLGRVPTSFSTPYSAA 181
Cdd:cd05326  79 RLDIMF-NNAGvlGAPCY-SILETSLEEFerVLDVNVYGAFLGTKHAARVMIpAKKGSIVSVASVAGVVGGLGPHAYTAS 156

                       170
                ....*....|....*
gi 74750135 182 KFALDGFFGSLRREL 196
Cdd:cd05326 157 KHAVLGLTRSAATEL 171
PRK07832 PRK07832
SDR family oxidoreductase;
30-196 8.14e-11

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 61.60  E-value: 8.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   30 ARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEApesVVQFALD---KLG 106
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVPEHRALDISDYDA---VAAFAADihaAHG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  107 GLDyLVLNHIGGAPAGTRARSP-QATRWLMQVNFVSYVQLTSRALPSLTDSK--GSLVVVSSLLGRVPTSFSTPYSAAKF 183
Cdd:PRK07832  78 SMD-VVMNIAGISAWGTVDRLThEQWRRMVDVNLMGPIHVIETFVPPMVAAGrgGHLVNVSSAAGLVALPWHAAYSASKF 156

                        170
                 ....*....|...
gi 74750135  184 ALDGFFGSLRREL 196
Cdd:PRK07832 157 GLRGLSEVLRFDL 169
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
27-239 8.37e-11

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 61.35  E-value: 8.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVL---TAHTEALLQKVVGNCRKLGApkvfyIAADMASPEAPESVVQFALD 103
Cdd:PRK08226   4 LTGKTALITGALQGIGEGIARVFARHGANLILldiSPEIEKLADELCGRGHRCTA-----VVADVRDPASVAAAIKRAKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  104 KLGGLDYLVlNHIGGAPAGTRARSPQATRWL-MQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGR-VPTSFSTPYSA 180
Cdd:PRK08226  79 KEGRIDILV-NNAGVCRLGSFLDMSDEDRDFhIDINIKGVWNVTKAVLPEMIARKdGRIVMMSSVTGDmVADPGETAYAL 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74750135  181 AKFALDGFFGSLRREldVQDVNVAITMCVLGLRdRASAAEAVrSSTSRPRQPEH------RGVPL 239
Cdd:PRK08226 158 TKAAIVGLTKSLAVE--YAQSGIRVNAICPGYV-RTPMAESI-ARQSNPEDPESvltemaKAIPL 218
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 32-192 1.00e-10

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


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 60.94  E-value: 1.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAyhyarlgshlVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEA----------PESVVQfA 101
Cdd:cd09806   3 VLITGCSSGIGLHLA----------VRLASDPSKRFKVYATMRDLKKKGRLWEAAGALAGGTletlqldvcdSKSVAA-A 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 102 LDKLGG--LDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPY 178
Cdd:cd09806  72 VERVTErhVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGsGRILVTSSVGGLQGLPFNDVY 151

                       170
                ....*....|....
gi 74750135 179 SAAKFALDGFFGSL 192
Cdd:cd09806 152 CASKFALEGLCESL 165
PRK06138 PRK06138
SDR family oxidoreductase;
27-247 1.27e-10

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 60.55  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVgnCRKLGAPKVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:PRK06138   3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVA--AAIAAGGRAFARQGDVGSAEAVEALVDFVAARWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  107 GLDYLVlNHIGGAPAGTRARSPQATrW--LMQVNfVSYVQLTSR-ALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAK 182
Cdd:PRK06138  81 RLDVLV-NNAGFGCGGTVVTTDEAD-WdaVMRVN-VGGVFLWAKyAIPIMQRQGgGSIVNTASQLALAGGRGRAAYVASK 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74750135  183 faldGFFGSLRR--ELDVQDVNVAITMCVLGLRD---------RASAAEAVRSStSRPRQPEHR-GVPLQ-SQTAMFL 247
Cdd:PRK06138 158 ----GAIASLTRamALDHATDGIRVNAVAPGTIDtpyfrrifaRHADPEALREA-LRARHPMNRfGTAEEvAQAALFL 230
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 27-196 1.65e-10

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: 60.38  E-value: 1.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLT---------AHTEALLQKVVGNCrklgapkvFYIAADMASPEAPESV 97
Cdd:cd05355  24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINylpeeeddaEETKKLIEEEGRKC--------LLIPGDLGDESFCRDL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  98 VQFALDKLGGLDYLVLNHIGGAPAGTRAR--SPQATRwLMQVNFVSYVQLTSRALPSLtDSKGSLVVVSSLLGRVPTSFS 175
Cdd:cd05355  96 VKEVVKEFGKLDILVNNAAYQHPQESIEDitTEQLEK-TFRTNIFSMFYLTKAALPHL-KKGSSIINTTSVTAYKGSPHL 173

                       170       180
                ....*....|....*....|.
gi 74750135 176 TPYSAAKFALDGFFGSLRREL 196
Cdd:cd05355 174 LDYAATKGAIVAFTRGLSLQL 194
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 27-203 1.80e-10

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: 59.98  E-value: 1.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHT-EALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:cd05362   1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNYASsKAAAEEVVAEIEAAGG-KAIAVQADVSDPSQVARLFDAAEKAF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 106 GGLDYLVLN---HIGGAPAGTrarSPQATRWLMQVNFVSYVQLTSRALPSLTDSkGSLVVVSSLLGRVPTSFSTPYSAAK 182
Cdd:cd05362  80 GGVDILVNNagvMLKKPIAET---SEEEFDRMFTVNTKGAFFVLQEAAKRLRDG-GRIINISSSLTAAYTPNYGAYAGSK 155

                       170       180
                ....*....|....*....|.
gi 74750135 183 FALDGFFGSLRRELDVQDVNV 203
Cdd:cd05362 156 AAVEAFTRVLAKELGGRGITV 176
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 27-196 4.48e-10

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: 58.93  E-value: 4.48e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEA-LLQKVVGNCRKLGAPKVFYiAADMASPEAPESVVQFALDKL 105
Cdd:cd05358   1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEdAAEEVVEEIKAVGGKAIAV-QADVSKEEDVVALFQSAIKEF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 106 GGLDYLVLNhiggapAGTRARSPQATRWLMQVNFVSYVQLT-----SR-ALPSLTDSK--GSLVVVSSLLGRVPTSFSTP 177
Cdd:cd05358  80 GTLDILVNN------AGLQGDASSHEMTLEDWNKVIDVNLTgqflcAReAIKRFRKSKikGKIINMSSVHEKIPWPGHVN 153

                       170
                ....*....|....*....
gi 74750135 178 YSAAKFALDGFFGSLRREL 196
Cdd:cd05358 154 YAASKGGVKMMTKTLAQEY 172
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 33-188 4.85e-10

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: 59.00  E-value: 4.85e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  33 LLTGANAGVGEELAYHYARLGSHLVLT-----AHTEALLQKVVGncrKLGApKVFYIAADMASPEAPESVVQFALDKLGG 107
Cdd:cd08940   6 LVTGSTSGIGLGIARALAAAGANIVLNgfgdaAEIEAVRAGLAA---KHGV-KVLYHGADLSKPAAIEDMVAYAQRQFGG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 108 LDYLVLNhiggapAGTRARSP----QATRW--LMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSA 180
Cdd:cd08940  82 VDILVNN------AGIQHVAPiedfPTEKWdaIIALNLSAVFHTTRLALPHMKKQGwGRIINIASVHGLVASANKSAYVA 155


                ....*...
gi 74750135 181 AKFALDGF 188
Cdd:cd08940 156 AKHGVVGL 163
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 25-203 5.20e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 58.79  E-value: 5.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   25 ASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDK 104
Cdd:PRK07478   2 MRLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGG-EAVALAGDVRDEAYAKALVALAVER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  105 LGGLDyLVLNHIG--GAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPS-LTDSKGSLVVVSSLLGrvpTSFSTP---- 177
Cdd:PRK07478  81 FGGLD-IAFNNAGtlGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAmLARGGGSLIFTSTFVG---HTAGFPgmaa 156

                        170       180
                 ....*....|....*....|....*.
gi 74750135  178 YSAAKFALDGFFGSLRRELDVQDVNV 203
Cdd:PRK07478 157 YAASKAGLIGLTQVLAAEYGAQGIRV 182
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 26-207 6.67e-10

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 58.80  E-value: 6.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGncrKLGApkVFYIAADMASPEAPESVVQFALDKL 105
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAA---ELGL--VVGGPLDVTDPASFAAFLDAVEADL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  106 GGLDYLVlNHIGGAPAGTRA-RSPQATRWLMQVNFVSYVQLTSRALPSLTD-SKGSLVVVSSLLGRVPTSFSTPYSAAKF 183
Cdd:PRK07825  77 GPIDVLV-NNAGVMPVGPFLdEPDAVTRRILDVNVYGVILGSKLAAPRMVPrGRGHVVNVASLAGKIPVPGMATYCASKH 155

                        170       180
                 ....*....|....*....|....
gi 74750135  184 ALDGFFGSLRRELDVQDVNVAITM 207
Cdd:PRK07825 156 AVVGFTDAARLELRGTGVHVSVVL 179
PRK07775 PRK07775
SDR family oxidoreductase;
32-197 7.61e-10

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 58.61  E-value: 7.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLGGLDYL 111
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGG-EAVAFPLDVTDPDSVKSFVAQAEEALGEIEVL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  112 VLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTD-SKGSLVVVSSLLGRVPTSFSTPYSAAKFALDGFFG 190
Cdd:PRK07775  92 VSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIErRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEAMVT 171


                 ....*..
gi 74750135  191 SLRRELD 197
Cdd:PRK07775 172 NLQMELE 178
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 26-203 7.86e-10

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 58.27  E-value: 7.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVV----GNCRKLGApkvfyiaADMASPEAPESVVQFA 101
Cdd:PRK12828   4 SLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLpgvpADALRIGG-------IDLVDPQAARRAVDEV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  102 LDKLGGLDYLVlNHIGGAPAGTRARSPQATrW--LMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPY 178
Cdd:PRK12828  77 NRQFGRLDALV-NIAGAFVWGTIADGDADT-WdrMYGVNVKTTLNASKAALPALTASGgGRIVNIGAGAALKAGPGMGAY 154

                        170       180
                 ....*....|....*....|....*
gi 74750135  179 SAAKFALDGFFGSLRRELDVQDVNV 203
Cdd:PRK12828 155 AAAKAGVARLTEALAAELLDRGITV 179
PRK09291 PRK09291
SDR family oxidoreductase;
31-204 8.80e-10

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 58.09  E-value: 8.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   31 RVLLTGANAGVGEELAYHYARLGSHLVLTAHTeallqkvvgncrklgAPKVFYIAADMASPEAPESVVQfaLD------- 103
Cdd:PRK09291   4 TILITGAGSGFGREVALRLARKGHNVIAGVQI---------------APQVTALRAEAARRGLALRVEK--LDltdaidr 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  104 -KLGGLDYLVL-NHIGGAPAGTRARSPQA-TRWLMQVNFVSYVQLTSRALPSLT-DSKGSLVVVSSLLGRVPTSFSTPYS 179
Cdd:PRK09291  67 aQAAEWDVDVLlNNAGIGEAGAVVDIPVElVRELFETNVFGPLELTQGFVRKMVaRGKGKVVFTSSMAGLITGPFTGAYC 146

                        170       180
                 ....*....|....*....|....*
gi 74750135  180 AAKFALDGFFGSLRRELDVQDVNVA 204
Cdd:PRK09291 147 ASKHALEAIAEAMHAELKPFGIQVA 171
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-114 9.66e-10

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 58.05  E-value: 9.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:PRK08217   3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGT-EVRGYAANVTDEEDVEATFAQIAEDFG 81


                 ....*...
gi 74750135  107 GLDYLVLN 114
Cdd:PRK08217  82 QLNGLINN 89
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 27-204 9.81e-10

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: 58.17  E-value: 9.81e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHT------------EALLQKVVGNCRKLGApKVFYIAADMASPEAP 94
Cdd:cd05338   1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTasegdngsakslPGTIEETAEEIEAAGG-QALPIVVDVRDEDQV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  95 ESVVQFALDKLGGLDYLVLNhiGGAPAGTRARSPQATRW--LMQVNF-VSYVqLTSRALPSLTDS-KGSLVVVSSLLGRV 170
Cdd:cd05338  80 RALVEATVDQFGRLDILVNN--AGAIWLSLVEDTPAKRFdlMQRVNLrGTYL-LSQAALPHMVKAgQGHILNISPPLSLR 156

                       170       180       190
                ....*....|....*....|....*....|....
gi 74750135 171 PTSFSTPYSAAKFALDGFFGSLRRELDVQDVNVA 204
Cdd:cd05338 157 PARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVN 190
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 24-203 1.03e-09

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


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 57.94  E-value: 1.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  24 PASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALD 103
Cdd:cd08936   5 RDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGL-SVTGTVCHVGKAEDRERLVATAVN 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 104 KLGGLDYLVLNHIGGAPAGTRARSPQATrW--LMQVNFVSYVQLTSRALPSLTD-SKGSLVVVSSLLGRVPTSFSTPYSA 180
Cdd:cd08936  84 LHGGVDILVSNAAVNPFFGNILDSTEEV-WdkILDVNVKATALMTKAVVPEMEKrGGGSVVIVSSVAAFHPFPGLGPYNV 162

                       170       180
                ....*....|....*....|...
gi 74750135 181 AKFALDGFFGSLRRELDVQDVNV 203
Cdd:cd08936 163 SKTALLGLTKNLAPELAPRNIRV 185
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 33-196 1.27e-09

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: 57.93  E-value: 1.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  33 LLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLGGLDYLV 112
Cdd:cd08945   7 LVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGV-EADGRTCDVRSVPEIEALVAAAVARYGPIDVLV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 113 LNhiGGAPAGTRARSPQATRWL--MQVNFVSYVQLTSRALPS---LTDSKGSLVVVSSLLGRVPTSFSTPYSAAKFALDG 187
Cdd:cd08945  86 NN--AGRSGGGATAELADELWLdvVETNLTGVFRVTKEVLKAggmLERGTGRIINIASTGGKQGVVHAAPYSASKHGVVG 163


                ....*....
gi 74750135 188 FFGSLRREL 196
Cdd:cd08945 164 FTKALGLEL 172
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 32-204 1.67e-09

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: 57.39  E-value: 1.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFALDKLGGLDYL 111
Cdd:cd05373   2 AAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEVL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 112 VLNHIGGAPAGTRARSPQATRWLMQVN----FVSYVQLTSRALPsltDSKGSLV---VVSSLLGRVPTSfstPYSAAKFA 184
Cdd:cd05373  82 VYNAGANVWFPILETTPRVFEKVWEMAafggFLAAREAAKRMLA---RGRGTIIftgATASLRGRAGFA---AFAGAKFA 155

                       170       180
                ....*....|....*....|
gi 74750135 185 LDGFFGSLRRELDVQDVNVA 204
Cdd:cd05373 156 LRALAQSMARELGPKGIHVA 175
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 35-203 1.69e-09

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: 57.23  E-value: 1.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  35 TGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMAspeAPESVVQFALDKLGGLDYLVL- 113
Cdd:cd05356   7 TGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFS---AGDDIYERIEKELEGLDIGILv 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 114 NHIGGAP--AGTRARSPQATRW-LMQVNFVSYVQLTSRALPSLTD-SKGSLVVVSSLLGRVPTSFSTPYSAAKFALDGFF 189
Cdd:cd05356  84 NNVGISHsiPEYFLETPEDELQdIINVNVMATLKMTRLILPGMVKrKKGAIVNISSFAGLIPTPLLATYSASKAFLDFFS 163

                       170
                ....*....|....
gi 74750135 190 GSLRRELDVQDVNV 203
Cdd:cd05356 164 RALYEEYKSQGIDV 177
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 33-196 1.85e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 57.62  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   33 LLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVgncrKLGAPKVFYIAADMASPEAPESVVQFALDKLGGLDYLV 112
Cdd:PRK06180   8 LITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFE----ALHPDRALARLLDVTDFDAIDAVVADAEATFGPIDVLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  113 lNHIGGAPAGTRARSPQA-TRWLMQVNFVSYVQLTSRALPSL-TDSKGSLVVVSSLLGRVPTSFSTPYSAAKFALDGFFG 190
Cdd:PRK06180  84 -NNAGYGHEGAIEESPLAeMRRQFEVNVFGAVAMTKAVLPGMrARRRGHIVNITSMGGLITMPGIGYYCGSKFALEGISE 162


                 ....*.
gi 74750135  191 SLRREL 196
Cdd:PRK06180 163 SLAKEV 168
PRK05867 PRK05867
SDR family oxidoreductase;
20-203 1.86e-09

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 57.35  E-value: 1.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   20 DNFDpasLQGARVLLTGANAGVGEELAYHYARLGSHLVLTA-HTEALlqKVVGNCRKLGAPKVFYIAADMASPEAPESVV 98
Cdd:PRK05867   3 DLFD---LHGKRALITGASTGIGKRVALAYVEAGAQVAIAArHLDAL--EKLADEIGTSGGKVVPVCCDVSQHQQVTSML 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   99 QFALDKLGGLDYLVLNhIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALP-SLTDS--KGSLVVVSSLLGR---VPT 172
Cdd:PRK05867  78 DQVTAELGGIDIAVCN-AGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAkAMVKQgqGGVIINTASMSGHiinVPQ 156

                        170       180       190
                 ....*....|....*....|....*....|.
gi 74750135  173 SFSTpYSAAKFALDGFFGSLRRELDVQDVNV 203
Cdd:PRK05867 157 QVSH-YCASKAAVIHLTKAMAVELAPHKIRV 186
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 29-207 2.20e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 57.03  E-value: 2.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   29 GARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGN--CRKlgapkvfyIAADMASPEApesvVQFALDKLG 106
Cdd:PRK07060   9 GKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGEtgCEP--------LRLDVGDDAA----IRAALAAAG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  107 GLDYLVLNhiGGAPAGTRARSPQATRW--LMQVNFVSYVQLTSRALPSLTDS--KGSLVVVSSLLGRVPTSFSTPYSAAK 182
Cdd:PRK07060  77 AFDGLVNC--AGIASLESALDMTAEGFdrVMAVNARGAALVARHVARAMIAAgrGGSIVNVSSQAALVGLPDHLAYCASK 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 74750135  183 FALDGFFGSLRREL-----DVQDVNVAITM 207
Cdd:PRK07060 155 AALDAITRVLCVELgphgiRVNSVNPTVTL 184
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-185 2.36e-09

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 56.69  E-value: 2.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGapKVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:PRK05786   3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYG--NIHYVVGDVSSTESARNVIEKAAKVLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  107 GLDYLVLNhIGGAPAGTrARSPQATRWLMQVNFVSYVQLTSRALPSLtdSKGSLVVVSSLLGRVPTSFST--PYSAAKFA 184
Cdd:PRK05786  81 AIDGLVVT-VGGYVEDT-VEEFSGLEEMLTNHIKIPLYAVNASLRFL--KEGSSIVLVSSMSGIYKASPDqlSYAVAKAG 156


                 .
gi 74750135  185 L 185
Cdd:PRK05786 157 L 157
PRK06182 PRK06182
short chain dehydrogenase; Validated
 32-205 2.64e-09

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 56.89  E-value: 2.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   32 VLLTGANAGVGEELAYHYARLGsHLVLTAhteallQKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFALDKLGGLDYL 111
Cdd:PRK06182   6 ALVTGASSGIGKATARRLAAQG-YTVYGA------ARRVDKMEDLASLGVHPLSLDVTDEASIKAAVDTIIAEEGRIDVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  112 VlNHIGGAPAGTRARSPQA-TRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAKFALDGFF 189
Cdd:PRK06182  79 V-NNAGYGSYGAIEDVPIDeARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIYTPLGAWYHATKFALEGFS 157

                        170
                 ....*....|....*.
gi 74750135  190 GSLRRELDVQDVNVAI 205
Cdd:PRK06182 158 DALRLEVAPFGIDVVV 173
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 26-185 2.85e-09

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 56.65  E-value: 2.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEAL-LQKVVGNCRKLGAPKVFyIAADMASPEAPESVVQFALDK 104
Cdd:PRK06077   3 SLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEeMNETLKMVKENGGEGIG-VLADVSTREGCETLAKATIDR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  105 LGGLDYLVLNhiggapAGTRARSP------QATRWLMQVNFVSYVQLTSRALPSLTDSkGSLVVVSSLLGRVPTSFSTPY 178
Cdd:PRK06077  82 YGVADILVNN------AGLGLFSPflnvddKLIDKHISTDFKSVIYCSQELAKEMREG-GAIVNIASVAGIRPAYGLSIY 154


                 ....*..
gi 74750135  179 SAAKFAL 185
Cdd:PRK06077 155 GAMKAAV 161
PRK05693 PRK05693
SDR family oxidoreductase;
32-196 3.17e-09

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 56.72  E-value: 3.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEAllqkvvgNCRKLGAPKVFYIAADMASPEAPESVVQFALDKLGGLDYL 111
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWATARKAE-------DVEALAAAGFTAVQLDVNDGAALARLAEELEAEHGGLDVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  112 VLNhiggapAGTRARSP------QATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAAKFAL 185
Cdd:PRK05693  77 INN------AGYGAMGPlldggvEAMRRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAV 150

                        170
                 ....*....|.
gi 74750135  186 DGFFGSLRREL 196
Cdd:PRK05693 151 HALSDALRLEL 161
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 26-196 3.40e-09

(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: 56.56  E-value: 3.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVL---------TAHTEALLQKVVGNCRKLGAPKVfyiaADMASPEAPES 96
Cdd:cd05353   2 RFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVndlggdrkgSGKSSSAADKVVDEIKAAGGKAV----ANYDSVEDGEK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  97 VVQFALDKLGGLDYLVLNhiggapAGT-RARSPQATR---W--LMQVNFVSYVQLTSRALPSLTD-SKGSLVVVSSLLGr 169
Cdd:cd05353  78 IVKTAIDAFGRVDILVNN------AGIlRDRSFAKMSeedWdlVMRVHLKGSFKVTRAAWPYMRKqKFGRIINTSSAAG- 150

                       170       180
                ....*....|....*....|....*...
gi 74750135 170 VPTSF-STPYSAAKFALDGFFGSLRREL 196
Cdd:cd05353 151 LYGNFgQANYSAAKLGLLGLSNTLAIEG 178
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 26-203 3.75e-09

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: 56.24  E-value: 3.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVgncRKLGApKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:cd05341   2 RLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAA---AELGD-AARFFHLDVTDEDGWTAVVDTAREAF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 106 GGLDYLVlNHIGGAPAGTRARSPqATRW--LMQVNFVSYVQLTSRALPSLTDS-KGSLVVVSSLLGRVPTSFSTPYSAAK 182
Cdd:cd05341  78 GRLDVLV-NNAGILTGGTVETTT-LEEWrrLLDINLTGVFLGTRAVIPPMKEAgGGSIINMSSIEGLVGDPALAAYNASK 155

                       170       180
                ....*....|....*....|.
gi 74750135 183 FALDGFFGSLRRELDVQDVNV 203
Cdd:cd05341 156 GAVRGLTKSAALECATQGYGI 176
PRK08264 PRK08264
SDR family oxidoreductase;
26-204 5.30e-09

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 55.67  E-value: 5.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAyhyarlgshlvltahtEALL----QKVVGNCR-----KLGAPKVFYIAADMASPEAPES 96
Cdd:PRK08264   3 DIKGKVVLVTGANRGIGRAFV----------------EQLLargaAKVYAAARdpesvTDLGPRVVPLQLDVTDPASVAA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   97 VVQFALDklggLDyLVLNHIGGAPAGTR--ARSPQATRWLMQVNFVSYVQLTSRALPSLTDS-KGSLVVVSSLLGRVPTS 173
Cdd:PRK08264  67 AAEAASD----VT-ILVNNAGIFRTGSLllEGDEDALRAEMETNYFGPLAMARAFAPVLAANgGGAIVNVLSVLSWVNFP 141

                        170       180       190
                 ....*....|....*....|....*....|.
gi 74750135  174 FSTPYSAAKFALDGFFGSLRRELDVQDVNVA 204
Cdd:PRK08264 142 NLGTYSASKAAAWSLTQALRAELAPQGTRVL 172
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 32-203 5.78e-09

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: 55.49  E-value: 5.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEelayhyarlgshlvltAHTEALLQ----KVVGNCRKLGA---------PKVFYIAADMASPEApesvV 98
Cdd:cd05354   6 VLVTGANRGIGK----------------AFVESLLAhgakKVYAAVRDPGSaahlvakygDKVVPLRLDVTDPES----I 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  99 QFALDKLGGLDYLVLNHIGGAPAG-TRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVV-VSSLLGRVPTSFST 176
Cdd:cd05354  66 KAAAAQAKDVDVVINNAGVLKPATlLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVnLNSVASLKNFPAMG 145

                       170       180
                ....*....|....*....|....*..
gi 74750135 177 PYSAAKFALDGFFGSLRRELDVQDVNV 203
Cdd:cd05354 146 TYSASKSAAYSLTQGLRAELAAQGTLV 172
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 27-196 8.02e-09

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 55.35  E-value: 8.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHY----ARLGShLVLTAHTEALLQKVVGNcrklgapKVFYIAADMASPEAPESVVQFAL 102
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFlaegARVAV-LERSAEKLASLRQRFGD-------HVLVVEGDVTSYADNQRAVDQTV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  103 DKLGGLDYLVLN--------HIGGAPAGTRARSPQAtrwLMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSF 174
Cdd:PRK06200  76 DAFGKLDCFVGNagiwdyntSLVDIPAETLDTAFDE---IFNVNVKGYLLGAKAALPALKASGGSMIFTLSNSSFYPGGG 152

                        170       180
                 ....*....|....*....|..
gi 74750135  175 STPYSAAKFALDGFFGSLRREL 196
Cdd:PRK06200 153 GPLYTASKHAVVGLVRQLAYEL 174
PRK06914 PRK06914
SDR family oxidoreductase;
33-205 1.41e-08

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 55.03  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   33 LLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAA-DMASPEAPESVvQFALDKLGGLDYL 111
Cdd:PRK06914   7 IVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATQLNLQQNIKVQQlDVTDQNSIHNF-QLVLKEIGRIDLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  112 VlNHIGGAPAGTRARSPQAT-RWLMQVNFVSYVQLTSRALPSLTDSKGSLVV-VSSLLGRV-PTSFStPYSAAKFALDGF 188
Cdd:PRK06914  86 V-NNAGYANGGFVEEIPVEEyRKQFETNVFGAISVTQAVLPYMRKQKSGKIInISSISGRVgFPGLS-PYVSSKYALEGF 163

                        170
                 ....*....|....*..
gi 74750135  189 FGSLRRELDVQDVNVAI 205
Cdd:PRK06914 164 SESLRLELKPFGIDVAL 180
PRK07063 PRK07063
SDR family oxidoreductase;
24-114 1.49e-08

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 54.67  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   24 PASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAP-KVFYIAADMASPEAPESVVQFAL 102
Cdd:PRK07063   2 MNRLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDVAGaRVLAVPADVTDAASVAAAVAAAE 81

                         90
                 ....*....|..
gi 74750135  103 DKLGGLDYLVLN 114
Cdd:PRK07063  82 EAFGPLDVLVNN 93
PRK08628 PRK08628
SDR family oxidoreductase;
27-195 1.62e-08

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 54.58  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGS-HLVLTAHTEALlqKVVGNCRKLGaPKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:PRK08628   5 LKDKVVIVTGGASGIGAAISLRLAEEGAiPVIFGRSAPDD--EFAEELRALQ-PRAEFVQVDLTDDAQCRDAVEQTVAKF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  106 GGLDYLVlNHIG-----GAPAGTRA--RSpqatrwlMQVNFVSYVQLTSRALPSLTDSKGSLVVVSS---LLGRVPTSfs 175
Cdd:PRK08628  82 GRIDGLV-NNAGvndgvGLEAGREAfvAS-------LERNLIHYYVMAHYCLPHLKASRGAIVNISSktaLTGQGGTS-- 151

                        170       180
                 ....*....|....*....|
gi 74750135  176 tPYSAAKFALDGffgsLRRE 195
Cdd:PRK08628 152 -GYAAAKGAQLA----LTRE 166
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 25-185 2.18e-08

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 54.24  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   25 ASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGncrKLGAPKVFyIAADMASPEAPESVVQFALDK 104
Cdd:PRK08265   2 IGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAA---SLGERARF-IATDITDDAAIERAVATVVAR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  105 LGGLDYLVLNHIGGAPAGtrARSPQATrWL--MQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAAK 182
Cdd:PRK08265  78 FGRVDILVNLACTYLDDG--LASSRAD-WLaaLDVNLVSAAMLAQAAHPHLARGGGAIVNFTSISAKFAQTGRWLYPASK 154


                 ...
gi 74750135  183 FAL 185
Cdd:PRK08265 155 AAI 157
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
27-203 2.79e-08

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 53.57  E-value: 2.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLT-AHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:PRK08063   2 FSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEIEALGR-KALAVKANVGDVEKIKEMFAQIDEEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  106 GGLDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLG--RVPTSFSTpYSAAKF 183
Cdd:PRK08063  81 GRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGsiRYLENYTT-VGVSKA 159

                        170       180
                 ....*....|....*....|
gi 74750135  184 ALDGFFGSLRRELDVQDVNV 203
Cdd:PRK08063 160 ALEALTRYLAVELAPKGIAV 179
PRK08703 PRK08703
SDR family oxidoreductase;
24-185 2.82e-08

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 53.78  E-value: 2.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   24 PASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEAPEsVVQFAL- 102
Cdd:PRK08703   1 MATLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHPEPFAIRFDLMSAEEKE-FEQFAAt 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  103 ---DKLGGLDYLVlnHIGGA-PAGTRARSPQATRWLMQ--VNFVSYVQLTSRALPSLTDS-KGSLVVVSSLLGRVPTSFS 175
Cdd:PRK08703  80 iaeATQGKLDGIV--HCAGYfYALSPLDFQTVAEWVNQyrINTVAPMGLTRALFPLLKQSpDASVIFVGESHGETPKAYW 157

                        170
                 ....*....|
gi 74750135  176 TPYSAAKFAL 185
Cdd:PRK08703 158 GGFGASKAAL 167
PRK07069 PRK07069
short chain dehydrogenase; Validated
 31-239 3.31e-08

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 53.56  E-value: 3.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   31 RVLLTGANAGVGEELAYHYARLGSHLVLT-----AHTEALLQKVVGNCrklGAPKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:PRK07069   1 RAFITGAAGGLGRAIARRMAEQGAKVFLTdindaAGLDAFAAEINAAH---GEGVAFAAVQDVTDEAQWQALLAQAADAM 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  106 GGLDYLVlNHIGGAPAGTRARSPQAT-RWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAKF 183
Cdd:PRK07069  78 GGLSVLV-NNAGVGSFGAIEQIELDEwRRVMAINVESIFLGCKHALPYLRASQpASIVNISSVAAFKAEPDYTAYNASKA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74750135  184 ALDGFFGSL-----RRELDVQDVNV----AITMCVLGLRDRASAAEAVRSSTsrprqpehRGVPL 239
Cdd:PRK07069 157 AVASLTKSIaldcaRRGLDVRCNSIhptfIRTGIVDPIFQRLGEEEATRKLA--------RGVPL 213
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 32-207 3.98e-08

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: 52.84  E-value: 3.98e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGncrKLGAPKVFYIAADMASPEAPESVV-QFALDKLGGLDY 110
Cdd:cd08931   3 IFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAA---ELGAENVVAGALDVTDRAAWAAALaDFAAATGGRLDA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 111 LvLNHIGGAPAGTRARSP-QATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVV-VSSLLGRVPTSFSTPYSAAKFALDGF 188
Cdd:cd08931  80 L-FNNAGVGRGGPFEDVPlAAHDRMVDINVKGVLNGAYAALPYLKATPGARVInTASSSAIYGQPDLAVYSATKFAVRGL 158

                       170
                ....*....|....*....
gi 74750135 189 FGSLRRELDVQDVNVAITM 207
Cdd:cd08931 159 TEALDVEWARHGIRVADVW 177
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 27-203 4.40e-08

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 53.00  E-value: 4.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAY----HYARLGSHLVLTAHTEALlqkvvgnCRKLGApKVFYIAADMASPEAPESVVQFAL 102
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARllhaQGAIVGLHGTRVEKLEAL-------AAELGE-RVKIFPANLSDRDEVKALGQKAE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  103 DKLGGLDYLVlNHIGGAPAGTRARSPQATrW--LMQVNFVSYVQLTsRAL--PSLTDSKGSLVVVSSLLGRVPTSFSTPY 178
Cdd:PRK12936  76 ADLEGVDILV-NNAGITKDGLFVRMSDED-WdsVLEVNLTATFRLT-RELthPMMRRRYGRIINITSVVGVTGNPGQANY 152

                        170       180
                 ....*....|....*....|....*
gi 74750135  179 SAAKFALDGFFGSLRRELDVQDVNV 203
Cdd:PRK12936 153 CASKAGMIGFSKSLAQEIATRNVTV 177
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 28-195 4.61e-08

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 53.02  E-value: 4.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   28 QGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEaLLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLGG 107
Cdd:PRK12823   7 AGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSE-LVHEVAAELRAAGG-EALALTADLETYAGAQAAMAAAVEAFGR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  108 LDYLVlNHIGGA----------PAGTRA---RSPQATRWlmqvnfvsyvqlTSRA-LPSLTDS-KGSLVVVSSL----LG 168
Cdd:PRK12823  85 IDVLI-NNVGGTiwakpfeeyeEEQIEAeirRSLFPTLW------------CCRAvLPHMLAQgGGAIVNVSSIatrgIN 151

                        170       180
                 ....*....|....*....|....*..
gi 74750135  169 RVptsfstPYSAAKFALDGFFGSLRRE 195
Cdd:PRK12823 152 RV------PYSAAKGGVNALTASLAFE 172
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 25-233 6.94e-08

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 52.41  E-value: 6.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   25 ASLQGARVLLTGANAGVGEELAYHYARLGSHL-VLTAH---TEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQF 100
Cdd:PRK12827   2 ASLDSRRVLITGGSGGLGRAIAVRLAADGADViVLDIHpmrGRAEADAVAAGIEAAGG-KALGLAFDVRDFAATRAALDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  101 ALDKLGGLDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSK--GSLVVVSSLLGRVPTSFSTPY 178
Cdd:PRK12827  81 GVEEFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARrgGRIVNIASVAGVRGNRGQVNY 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  179 SAAKFALDGFFGSLRRELDVQD--VN-VAITMCVLGLRDRASAAEAVRS--STSRPRQPE 233
Cdd:PRK12827 161 AASKAGLIGLTKTLANELAPRGitVNaVAPGAINTPMADNAAPTEHLLNpvPVQRLGEPD 220
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 27-196 8.06e-08

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: 52.35  E-value: 8.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLG---SHLVLTAHTEALLQKVVGNcrklgapKVFYIAADMASPEAPESVVQFALD 103
Cdd:cd05348   2 LKGEVALITGGGSGLGRALVERFVAEGakvAVLDRSAEKVAELRADFGD-------AVVGVEGDVRSLADNERAVARCVE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 104 KLGGLDYLVLN-----HIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPY 178
Cdd:cd05348  75 RFGKLDCFIGNagiwdYSTSLVDIPEEKLDEAFDELFHINVKGYILGAKAALPALYATEGSVIFTVSNAGFYPGGGGPLY 154

                       170
                ....*....|....*...
gi 74750135 179 SAAKFALDGFFGSLRREL 196
Cdd:cd05348 155 TASKHAVVGLVKQLAYEL 172
PRK06484 PRK06484
short chain dehydrogenase; Validated
 28-203 8.06e-08

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 53.31  E-value: 8.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   28 QGARVLLTGANAGVGEELAYHYARLGsHLVLTAHTEalLQKVVGNCRKLGAPKVFYiAADMASPEAPESVVQFALDKLGG 107
Cdd:PRK06484   4 QSRVVLVTGAAGGIGRAACQRFARAG-DQVVVADRN--VERARERADSLGPDHHAL-AMDVSDEAQIREGFEQLHREFGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  108 LDYLVLNH--IGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSK--GSLVVVSSLLGRVPTSFSTPYSAAKF 183
Cdd:PRK06484  80 IDVLVNNAgvTDPTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGhgAAIVNVASGAGLVALPKRTAYSASKA 159

                        170       180
                 ....*....|....*....|
gi 74750135  184 ALDGFFGSLRRELDVQDVNV 203
Cdd:PRK06484 160 AVISLTRSLACEWAAKGIRV 179
PRK09135 PRK09135
pteridine reductase; Provisional
 24-196 8.69e-08

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 52.24  E-value: 8.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   24 PASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHT-EALLQKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFAL 102
Cdd:PRK09135   1 MMTDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRsAAEADALAAELNALRPGSAAALQADLLDPDALPELVAACV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  103 DKLGGLDYLVLNhiggapAGTRARSP----QATRW--LMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFST 176
Cdd:PRK09135  81 AAFGRLDALVNN------ASSFYPTPlgsiTEAQWddLFASNLKAPFFLSQAAAPQLRKQRGAIVNITDIHAERPLKGYP 154

                        170       180
                 ....*....|....*....|
gi 74750135  177 PYSAAKFALDGFFGSLRREL 196
Cdd:PRK09135 155 VYCAAKAALEMLTRSLALEL 174
PRK07074 PRK07074
SDR family oxidoreductase;
32-196 9.06e-08

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 52.46  E-value: 9.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVgncRKLGAPKVFYIAADMASPEAPESVVQFALDKLGGLDYL 111
Cdd:PRK07074   5 ALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFA---DALGDARFVPVACDLTDAASLAAALANAAAERGPVDVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  112 VLNhiGGAPAGTRARSPQATRWLMQVNF-VSYVQLTSRAL--PSLTDSKGSLVVVSSLLGRvpTSFSTP-YSAAKFALDG 187
Cdd:PRK07074  82 VAN--AGAARAASLHDTTPASWRADNALnLEAAYLCVEAVleGMLKRSRGAVVNIGSVNGM--AALGHPaYSAAKAGLIH 157


                 ....*....
gi 74750135  188 FFGSLRREL 196
Cdd:PRK07074 158 YTKLLAVEY 166
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 32-196 1.02e-07

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: 51.99  E-value: 1.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVLTA-HTEALLQKVVGNCRKLGAPKVFYiAADMASPEAPESVVQFALDKLGGLDY 110
Cdd:cd05366   5 AIITGAAQGIGRAIAERLAADGFNIVLADlNLEEAAKSTIQEISEAGYNAVAV-GADVTDKDDVEALIDQAVEKFGSFDV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 111 LVLNhiggapAGTRARSPQAT------RWLMQVNFVSY---VQLTSRALPSLtDSKGSLVVVSSLLGRVPTSFSTPYSAA 181
Cdd:cd05366  84 MVNN------AGIAPITPLLTiteedlKKVYAVNVFGVlfgIQAAARQFKKL-GHGGKIINASSIAGVQGFPNLGAYSAS 156

                       170
                ....*....|....*
gi 74750135 182 KFALDGFFGSLRREL 196
Cdd:cd05366 157 KFAVRGLTQTAAQEL 171
PLN02253 PLN02253
xanthoxin dehydrogenase
 27-203 1.09e-07

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 52.13  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVvgnCRKLG-APKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:PLN02253  16 LLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNV---CDSLGgEPNVCFFHCDVTVEDDVSRAVDFTVDKF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  106 GGLDYLVLNH-IGGAP-AGTRARSPQATRWLMQVNFV-SYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAAK 182
Cdd:PLN02253  93 GTLDIMVNNAgLTGPPcPDIRNVELSEFEKVFDVNVKgVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGPHAYTGSK 172

                        170       180
                 ....*....|....*....|.
gi 74750135  183 FALDGFFGSLRRELDVQDVNV 203
Cdd:PLN02253 173 HAVLGLTRSVAAELGKHGIRV 193
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 32-196 1.23e-07

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: 51.70  E-value: 1.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKlgapkvfyIAADMASPEAPESVVQFALDKLGGLDYL 111
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYGDPLRL--------TPLDVADAAAVREVCSRLLAEHGPIDAL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 112 VlnHIGGA--PAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAKFALDGF 188
Cdd:cd05331  73 V--NCAGVlrPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRtGAIVTVASNAAHVPRISMAAYGASKAALASL 150


                ....*...
gi 74750135 189 FGSLRREL 196
Cdd:cd05331 151 SKCLGLEL 158
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 32-211 1.33e-07

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 51.96  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCR-KLGAPKVFYIAADMASPEAPESVVQFALDKLGGLDY 110
Cdd:PRK12384   5 AVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINaEYGEGMAYGFGADATSEQSVLALSRGVDEIFGRVDL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  111 LVLNhiggapAGTrARSPQATRW-------LMQVNFVSYVqLTSRALPSLT---DSKGSLVVVSSLLGRVPTSFSTPYSA 180
Cdd:PRK12384  85 LVYN------AGI-AKAAFITDFqlgdfdrSLQVNLVGYF-LCAREFSRLMirdGIQGRIIQINSKSGKVGSKHNSGYSA 156

                        170       180       190
                 ....*....|....*....|....*....|.
gi 74750135  181 AKFALDGFFGSLrrELDVQDVNVAITMCVLG 211
Cdd:PRK12384 157 AKFGGVGLTQSL--ALDLAEYGITVHSLMLG 185
PRK07985 PRK07985
SDR family oxidoreductase;
27-205 1.35e-07

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 51.92  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLT--AHTEALLQKVVGNCRKLGAPKVFyIAADMASPEAPESVVQFALDK 104
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISylPVEEEDAQDVKKIIEECGRKAVL-LPGDLSDEKFARSLVHEAHKA 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  105 LGGLDYLVLnhIGG---APAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTdSKGSLVVVSSLLGRVPTSFSTPYSAA 181
Cdd:PRK07985 126 LGGLDIMAL--VAGkqvAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLP-KGASIITTSSIQAYQPSPHLLDYAAT 202

                        170       180
                 ....*....|....*....|....
gi 74750135  182 KFALDGFFGSLRRELDVQDVNVAI 205
Cdd:PRK07985 203 KAAILNYSRGLAKQVAEKGIRVNI 226
PRK08251 PRK08251
SDR family oxidoreductase;
31-203 1.54e-07

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 51.47  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   31 RVLLTGANAGVGEELAYHYARLGSHLVLTAHT----EALLQKVVGNcrklgAP--KVFYIAADMASPEAPESVVQFALDK 104
Cdd:PRK08251   4 KILITGASSGLGAGMAREFAAKGRDLALCARRtdrlEELKAELLAR-----YPgiKVAVAALDVNDHDQVFEVFAEFRDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  105 LGGLDYLVLNH-IG-GAPAGT-RARSPQATrwlMQVNFVSYVQLTSRALPSLTDS-KGSLVVVSSLLG-RVPTSFSTPYS 179
Cdd:PRK08251  79 LGGLDRVIVNAgIGkGARLGTgKFWANKAT---AETNFVAALAQCEAAMEIFREQgSGHLVLISSVSAvRGLPGVKAAYA 155

                        170       180
                 ....*....|....*....|....
gi 74750135  180 AAKFALDGFFGSLRRELDVQDVNV 203
Cdd:PRK08251 156 ASKAGVASLGEGLRAELAKTPIKV 179
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 29-185 1.55e-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: 51.62  E-value: 1.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  29 GARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRklGAPKVFYIAADMASPEAPESVVQFALDKLGGL 108
Cdd:cd08943   1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQ--GGPRALGVQCDVTSEAQVQSAFEQAVLEFGGL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 109 DYLVLNhIGGAPAGTRARSPQAT-RWLMQVNFVSYvQLTSR-ALPSLTDSK--GSLVVVSSLLGRVPTSFSTPYSAAKFA 184
Cdd:cd08943  79 DIVVSN-AGIATSSPIAETSLEDwNRSMDINLTGH-FLVSReAFRIMKSQGigGNIVFNASKNAVAPGPNAAAYSAAKAA 156


                .
gi 74750135 185 L 185
Cdd:cd08943 157 E 157
PRK06482 PRK06482
SDR family oxidoreductase;
33-195 2.16e-07

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 51.27  E-value: 2.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   33 LLTGANAGVGEELayhyarlgshlvltahTEALLQK---VVGNCRKLGA--------PKVFYIAA-DMASPEAPESVVQF 100
Cdd:PRK06482   6 FITGASSGFGRGM----------------TERLLARgdrVAATVRRPDAlddlkaryGDRLWVLQlDVTDSAAVRAVVDR 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  101 ALDKLGGLDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSL-TDSKGSLVVVSSLLGRV--PTsFSTp 177
Cdd:PRK06482  70 AFAALGRIDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLrRQGGGRIVQVSSEGGQIayPG-FSL- 147

                        170
                 ....*....|....*...
gi 74750135  178 YSAAKFALDGFFGSLRRE 195
Cdd:PRK06482 148 YHATKWGIEGFVEAVAQE 165
PRK07577 PRK07577
SDR family oxidoreductase;
31-187 2.25e-07

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 50.88  E-value: 2.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   31 RVLLTGANAGVGEELAYHYARLGSHLVLTAHTEAllqkvvgncrkLGAPKVFYiAADMASPEAPESVVQFALDKlGGLDY 110
Cdd:PRK07577   5 TVLVTGATKGIGLALSLRLANLGHQVIGIARSAI-----------DDFPGELF-ACDLADIEQTAATLAQINEI-HPVDA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  111 LVlNHIGGA-PAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSL--LGrvpTSFSTPYSAAKFALD 186
Cdd:PRK07577  72 IV-NNVGIAlPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREqGRIVNICSRaiFG---ALDRTSYSAAKSALV 147


                 .
gi 74750135  187 G 187
Cdd:PRK07577 148 G 148
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 32-196 3.59e-07

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: 50.37  E-value: 3.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVL-TAHTEALLQKVvgncRKLGA--PKVFYIAADMASP--EAPESVVQfaLDKLG 106
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGNNTVIaTCRDPSAATEL----AALGAshSRLHILELDVTDEiaESAEAVAE--RLGDA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 107 GLDYLVlNHIGGAPAGTRARSPQATRW--LMQVNFVSYVQLTSRALPSLTDSKGSLVV-VSSLLGRVP--TSF-STPYSA 180
Cdd:cd05325  75 GLDVLI-NNAGILHSYGPASEVDSEDLleVFQVNVLGPLLLTQAFLPLLLKGARAKIInISSRVGSIGdnTSGgWYSYRA 153

                       170
                ....*....|....*.
gi 74750135 181 AKFALDGFFGSLRREL 196
Cdd:cd05325 154 SKAALNMLTKSLAVEL 169
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 26-224 4.50e-07

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: 50.17  E-value: 4.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGapKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:cd08942   3 SVAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYG--ECIAIPADLSSEEGIEALVARVAERS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 106 GGLDYLVLNhiGGAPAGTRARSPQATRW--LMQVNFVSYVQLTSRALPSLTDSK-----GSLVVVSSLLG-RVPTSFSTP 177
Cdd:cd08942  81 DRLDVLVNN--AGATWGAPLEAFPESGWdkVMDINVKSVFFLTQALLPLLRAAAtaenpARVINIGSIAGiVVSGLENYS 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 74750135 178 YSAAKFALDGFFGSLRRELDVQDVNV-AIT-------MCVLGLRDRASAAEAVRS 224
Cdd:cd08942 159 YGASKAAVHQLTRKLAKELAGEHITVnAIApgrfpskMTAFLLNDPAALEAEEKS 213
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 27-203 4.66e-07

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: 50.22  E-value: 4.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEaLLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:cd08937   2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSE-LVHEVLAEILAAGD-AAHVHTADLETYAGAQGVVRAAVERFG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 107 GLDYLVlNHIGGA----------PAGTRA---RSPQATRWlmqvnfvsyvqlTSRA-LPSLTDSK-GSLVVVSSLLGRvp 171
Cdd:cd08937  80 RVDVLI-NNVGGTiwakpyehyeEEQIEAeirRSLFPTLW------------CCRAvLPHMLERQqGVIVNVSSIATR-- 144

                       170       180       190
                ....*....|....*....|....*....|..
gi 74750135 172 TSFSTPYSAAKFALDGFFGSLRRELDVQDVNV 203
Cdd:cd08937 145 GIYRIPYSAAKGGVNALTASLAFEHARDGIRV 176
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 17-120 5.24e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 50.04  E-value: 5.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   17 YWDDNFDpasLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEAllqkVVGNCRKLGAPKVFYIAADMASPEAPES 96
Cdd:PRK06841   6 QFDLAFD---LSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSED----VAEVAAQLLGGNAKGLVCDVSDSQSVEA 78

                         90       100
                 ....*....|....*....|....
gi 74750135   97 VVQFALDKLGGLDYLVlNHIGGAP 120
Cdd:PRK06841  79 AVAAVISAFGRIDILV-NSAGVAL 101
PRK06953 PRK06953
SDR family oxidoreductase;
32-186 5.73e-07

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 49.69  E-value: 5.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVvgncRKLGAPKvfyIAADMAspeAPESVVQFALdKLGG--LD 109
Cdd:PRK06953   4 VLIVGASRGIGREFVRQYRADGWRVIATARDAAALAAL----QALGAEA---LALDVA---DPASVAGLAW-KLDGeaLD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  110 YLVLNH--IGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVVVSS---LLGRVPTSFSTPYSAAKFA 184
Cdd:PRK06953  73 AAVYVAgvYGPRTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSrmgSIGDATGTTGWLYRASKAA 152


                 ..
gi 74750135  185 LD 186
Cdd:PRK06953 153 LN 154
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 32-221 6.03e-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: 49.76  E-value: 6.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVLTAH-TEALLQKVVgncRKLGApKVFYIAADMASPEAPESVVQFALDKLGGLDY 110
Cdd:cd05349   3 VLVTGASRGLGAAIARSFAREGARVVVNYYrSTESAEAVA---AEAGE-RAIAIQADVRDRDQVQAMIEEAKNHFGPVDT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 111 LVLNHIGGAPAGTRARSPQAT----RWLMQVNFV--SYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAKF 183
Cdd:cd05349  79 IVNNALIDFPFDPDQRKTFDTidweDYQQQLEGAvkGALNLLQAVLPDFKERGsGRVINIGTNLFQNPVVPYHDYTTAKA 158

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 74750135 184 ALDGFFGSLRRELDVQDVNVaiTMCVLGLRDRASAAEA 221
Cdd:cd05349 159 ALLGFTRNMAKELGPYGITV--NMVSGGLLKVTDASAA 194
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 29-225 6.21e-07

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 49.95  E-value: 6.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   29 GARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGapkvFYIAADMASPEAPESVVQFALDK---L 105
Cdd:PRK05876   6 GRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEG----FDVHGVMCDVRHREEVTHLADEAfrlL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  106 GGLDyLVLNHIGGAPAGTRARSPQAT-RWLMQVNFVSYVQLTSRALPSLTD--SKGSLVVVSSLLGRVPTSFSTPYSAAK 182
Cdd:PRK05876  82 GHVD-VVFSNAGIVVGGPIVEMTHDDwRWVIDVDLWGSIHTVEAFLPRLLEqgTGGHVVFTASFAGLVPNAGLGAYGVAK 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 74750135  183 FALDGFFGSLRRELDVQDVNVAItMCVLGLRDR-ASAAEAVRSS 225
Cdd:PRK05876 161 YGVVGLAETLAREVTADGIGVSV-LCPMVVETNlVANSERIRGA 203
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 33-205 7.39e-07

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 49.65  E-value: 7.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   33 LLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVvgnCRKLGApKVFYIAADMASPEAPESVVQFALDKLGGLDyLV 112
Cdd:PRK08263   7 FITGASRGFGRAWTEAALERGDRVVATARDTATLADL---AEKYGD-RLLPLALDVTDRAAVFAAVETAVEHFGRLD-IV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  113 LNHIGGAPAGTRARSPQA-TRWLMQVNFVSYVQLTSRALPSL-TDSKGSLVVVSSLLGRVPTSFSTPYSAAKFALDGFFG 190
Cdd:PRK08263  82 VNNAGYGLFGMIEEVTESeARAQIDTNFFGALWVTQAVLPYLrEQRSGHIIQISSIGGISAFPMSGIYHASKWALEGMSE 161

                        170
                 ....*....|....*
gi 74750135  191 SLRRELDVQDVNVAI 205
Cdd:PRK08263 162 ALAQEVAEFGIKVTL 176
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 32-196 1.25e-06

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 48.81  E-value: 1.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVL---TAHTEALLQKVVGNCRKLGApkvFYIAADMASPEAPESVVQFALDKLGGL 108
Cdd:cd05357   3 ALVTGAAKRIGRAIAEALAAEGYRVVVhynRSEAEAQRLKDELNALRNSA---VLVQADLSDFAACADLVAAAFRAFGRC 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 109 DYLVlNHIGGAPAGTRARSP-QATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVV--VSSLLGRvPTSFSTPYSAAKFAL 185
Cdd:cd05357  80 DVLV-NNASAFYPTPLGQGSeDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIIniIDAMTDR-PLTGYFAYCMSKAAL 157

                       170
                ....*....|.
gi 74750135 186 DGFFGSLRREL 196
Cdd:cd05357 158 EGLTRSAALEL 168
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
33-195 1.26e-06

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 48.61  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   33 LLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFALDKLGGLDYLV 112
Cdd:PRK12824   6 LVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAKDWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGPVDILV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  113 LNhiggapAG-TRAR-----SPQATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAKFAL 185
Cdd:PRK12824  86 NN------AGiTRDSvfkrmSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGyGRIINISSVNGLKGQFGQTNYSAAKAGM 159

                        170
                 ....*....|
gi 74750135  186 DGFFGSLRRE 195
Cdd:PRK12824 160 IGFTKALASE 169
PRK06114 PRK06114
SDR family oxidoreductase;
26-168 1.55e-06

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 48.62  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAH-TEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDK 104
Cdd:PRK06114   5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLrTDDGLAETAEHIEAAGR-RAIQIAADVTSKADLRAAVARTEAE 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  105 LGGLDyLVLNHIGGAPAGTrARSPQATRW--LMQVN----FVSyVQLTSRALpsLTDSKGSLVVVSSLLG 168
Cdd:PRK06114  84 LGALT-LAVNAAGIANANP-AEEMEEEQWqtVMDINltgvFLS-CQAEARAM--LENGGGSIVNIASMSG 148
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 26-182 1.58e-06

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 48.57  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHT-EALLQKVVGNCRKLGAPKVFyIAADMASPEAPESVVQFALDK 104
Cdd:PRK08936   4 DLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSdEEEANDVAEEIKKAGGEAIA-VKGDVTVESDVVNLIQTAVKE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  105 LGGLDYLVLNhiggapAGTRARSPQATRWLMQVNFVSYVQLT-----SR-ALPSLTDS--KGSLVVVSSLLGRVPTSFST 176
Cdd:PRK08936  83 FGTLDVMINN------AGIENAVPSHEMSLEDWNKVINTNLTgaflgSReAIKYFVEHdiKGNIINMSSVHEQIPWPLFV 156


                 ....*.
gi 74750135  177 PYSAAK 182
Cdd:PRK08936 157 HYAASK 162
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 27-196 1.98e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 48.49  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLV---LTAHTEAllQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALD 103
Cdd:PRK06701  44 LKGKVALITGGDSGIGRAVAVLFAKEGADIAivyLDEHEDA--NETKQRVEKEGV-KCLLIPGDVSDEAFCKDAVEETVR 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  104 KLGGLDYLVLNHIGGAPAgTRARSPQATRW--LMQVNFVSYVQLTSRALPSLTdSKGSLVVVSSLLGRVPTSFSTPYSAA 181
Cdd:PRK06701 121 ELGRLDILVNNAAFQYPQ-QSLEDITAEQLdkTFKTNIYSYFHMTKAALPHLK-QGSAIINTGSITGYEGNETLIDYSAT 198

                        170
                 ....*....|....*
gi 74750135  182 KFALDGFFGSLRREL 196
Cdd:PRK06701 199 KGAIHAFTRSLAQSL 213
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 32-117 2.07e-06

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 48.14  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVgncRKLGAP--KVFYIAADMASPEAPESVVQFALDKLGGLD 109
Cdd:PRK07677   4 VIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAK---LEIEQFpgQVLTVQMDVRNPEDVQKMVEQIDEKFGRID 80


                 ....*...
gi 74750135  110 YLVLNHIG 117
Cdd:PRK07677  81 ALINNAAG 88
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 27-203 2.51e-06

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: 47.87  E-value: 2.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVgncRKLGAPKVfYIAADMASPEAPESVVQFALDKLG 106
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVV---AQIAGGAL-ALRVDVTDEQQVAALFERAVEEFG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 107 GLDYLVLNHIGGAPAGTRARSPQAT-RWLMQVNFVSYVQLTSRALPSLTDS-KGSLVVVSSLLGRVPTSFSTPYSAAKFA 184
Cdd:cd08944  77 GLDLLVNNAGAMHLTPAIIDTDLAVwDQTMAINLRGTFLCCRHAAPRMIARgGGSIVNLSSIAGQSGDPGYGAYGASKAA 156

                       170
                ....*....|....*....
gi 74750135 185 LDGFFGSLRRELDVQDVNV 203
Cdd:cd08944 157 IRNLTRTLAAELRHAGIRC 175
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 26-185 3.01e-06

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 47.83  E-value: 3.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:PRK08085   6 SLAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGI-KAHAAPFNVTHKQEVEAAIEHIEKDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  106 GGLDYLVLNhiggapAGTRARSP----QATRW--LMQVNFVSyVQLTSRALPS--LTDSKGSLVVVSSL---LGRvptSF 174
Cdd:PRK08085  85 GPIDVLINN------AGIQRRHPftefPEQEWndVIAVNQTA-VFLVSQAVARymVKRQAGKIINICSMqseLGR---DT 154

                        170
                 ....*....|.
gi 74750135  175 STPYSAAKFAL 185
Cdd:PRK08085 155 ITPYAASKGAV 165
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
24-114 3.08e-06

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 47.71  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   24 PASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVvgncRKLGAPKVFYIAADMASPEAPESVVQFALD 103
Cdd:PRK07067   1 MMRLQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLA----ALEIGPAAIAVSLDVTRQDSIDRIVAAAVE 76

                         90
                 ....*....|.
gi 74750135  104 KLGGLDYLVLN 114
Cdd:PRK07067  77 RFGGIDILFNN 87
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
23-238 3.20e-06

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 47.59  E-value: 3.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   23 DPASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEAllQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFAL 102
Cdd:PRK12481   2 QLFDLNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEA--PETQAQVEALGR-KFHFITADLIQQKDIDSIVSQAV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  103 DKLGGLDYLVLNhiggapAGTRAR------SPQATRWLMQVNFVSYVQLTSRALPSLTD--SKGSLVVVSSLLG-----R 169
Cdd:PRK12481  79 EVMGHIDILINN------AGIIRRqdllefGNKDWDDVININQKTVFFLSQAVAKQFVKqgNGGKIINIASMLSfqggiR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74750135  170 VPTsfstpYSAAKFALDGFFGSLRRELDVQDVNV-AITMCVLGLRDRAS-AAEAVRSSTSRPRQPEHR-GVP 238
Cdd:PRK12481 153 VPS-----YTASKSAVMGLTRALATELSQYNINVnAIAPGYMATDNTAAlRADTARNEAILERIPASRwGTP 219
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 26-184 3.40e-06

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: 47.33  E-value: 3.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:cd05352   5 SLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDF 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 106 GGLDYLVLNhiGGAPAGTRARSPQATRW--LMQVN-FVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPT--SFSTPYSA 180
Cdd:cd05352  85 GKIDILIAN--AGITVHKPALDYTYEQWnkVIDVNlNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIVNrpQPQAAYNA 162


                ....
gi 74750135 181 AKFA 184
Cdd:cd05352 163 SKAA 166
PRK08340 PRK08340
SDR family oxidoreductase;
31-114 4.96e-06

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 47.11  E-value: 4.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   31 RVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGapKVFYIAADMASPEAPESVVQFALDKLGGLDY 110
Cdd:PRK08340   2 NVLVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYG--EVYAVKADLSDKDDLKNLVKEAWELLGGIDA 79


                 ....
gi 74750135  111 LVLN 114
Cdd:PRK08340  80 LVWN 83
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 27-212 5.50e-06

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 46.67  E-value: 5.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGN-------CRKLGApKVFYIAADMASPEAPESVVQ 99
Cdd:cd09762   1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEPHPKLPGTiytaaeeIEAAGG-KALPCIVDIRDEDQVRAAVE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 100 FALDKLGGLDYLVLNHIGGAPAGTRARSPQATRWLMQVNfVSYVQLTSRA-LPSLTDSKGSLVV-VSSLLGRVPTSFS-- 175
Cdd:cd09762  80 KAVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVN-TRGTYLCSKAcLPYLKKSKNPHILnLSPPLNLNPKWFKnh 158

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 74750135 176 TPYSAAKFALdgffgslrreldvqdvnvaiTMCVLGL 212
Cdd:cd09762 159 TAYTMAKYGM--------------------SMCVLGM 175
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 29-182 6.21e-06

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: 46.80  E-value: 6.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  29 GARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEallqKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFALDKLGGL 108
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDE----ERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRI 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74750135 109 DYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAAK 182
Cdd:cd09761  77 DVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAFQSEPDSEAYAASK 150
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 26-196 8.82e-06

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 46.22  E-value: 8.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGAN--AGVGEELAYHYARLGSHLVLTAH--------------TEALLQKVVGNcrklGAPKVFYIAADMA 89
Cdd:PRK12748   2 PLMKKIALVTGASrlNGIGAAVCRRLAAKGIDIFFTYWspydktmpwgmhdkEPVLLKEEIES----YGVRCEHMEIDLS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   90 SPEAPESVVQFALDKLGGLDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVqLTSRALPSLTDSK--GSLVVVSSLL 167
Cdd:PRK12748  78 QPYAPNRVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATM-LLSSAFAKQYDGKagGRIINLTSGQ 156

                        170       180
                 ....*....|....*....|....*....
gi 74750135  168 GRVPTSFSTPYSAAKFALDGFFGSLRREL 196
Cdd:PRK12748 157 SLGPMPDELAYAATKGAIEAFTKSLAPEL 185
PRK06172 PRK06172
SDR family oxidoreductase;
25-187 1.13e-05

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 45.90  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   25 ASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDK 104
Cdd:PRK06172   3 MTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGG-EALFVACDVTRDAEVKALVEQTIAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  105 LGGLDYLVLNH-IGGAPAGTRARSPQATRWLMQVNfVSYVQLTSR-ALPS-LTDSKGSLVVVSSLLGRVPTSFSTPYSAA 181
Cdd:PRK06172  82 YGRLDYAFNNAgIEIEQGRLAEGSEAEFDAIMGVN-VKGVWLCMKyQIPLmLAQGGGAIVNTASVAGLGAAPKMSIYAAS 160


                 ....*.
gi 74750135  182 KFALDG 187
Cdd:PRK06172 161 KHAVIG 166
PRK05855 PRK05855
SDR family oxidoreductase;
29-208 1.18e-05

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 46.51  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   29 GARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYiAADMASPEAPESVVQFALDKLGGL 108
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAGAVAHAY-RVDVSDADAMEAFAEWVRAEHGVP 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  109 DYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYV--------QLTSRALPsltdskGSLVVVSSLLGRVPTSFSTPYSA 180
Cdd:PRK05855 394 DIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIhgcrlfgrQMVERGTG------GHIVNVASAAAYAPSRSLPAYAT 467

                        170       180
                 ....*....|....*....|....*...
gi 74750135  181 AKFALDGFFGSLRRELDVQDVNVAiTMC 208
Cdd:PRK05855 468 SKAAVLMLSECLRAELAAAGIGVT-AIC 494
PRK07035 PRK07035
SDR family oxidoreductase;
20-185 1.34e-05

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 45.78  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   20 DNFDpasLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQ 99
Cdd:PRK07035   2 NLFD---LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGG-KAEALACHIGEMEQIDALFA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  100 FALDKLGGLDYLVLN--------HIGGAPAGtrarspqATRWLMQVNFVSYVQLTSRALPSLTDS-KGSLVVVSSLLGRV 170
Cdd:PRK07035  78 HIRERHGRLDILVNNaaanpyfgHILDTDLG-------AFQKTVDVNIRGYFFMSVEAGKLMKEQgGGSIVNVASVNGVS 150

                        170
                 ....*....|....*
gi 74750135  171 PTSFSTPYSAAKFAL 185
Cdd:PRK07035 151 PGDFQGIYSITKAAV 165
PRK07024 PRK07024
SDR family oxidoreductase;
31-196 1.49e-05

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 45.69  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   31 RVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFyiAADMASPEAPESVVQFALDKLGGLDY 110
Cdd:PRK07024   4 KVFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAARVSVY--AADVRDADALAAAAADFIAAHGLPDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  111 LVLNhiGGAPAGTRARSP---QATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAKFALD 186
Cdd:PRK07024  82 VIAN--AGISVGTLTEERedlAVFREVMDTNYFGMVATFQPFIAPMRAARrGTLVGIASVAGVRGLPGAGAYSASKAAAI 159

                        170
                 ....*....|
gi 74750135  187 GFFGSLRREL 196
Cdd:PRK07024 160 KYLESLRVEL 169
PRK07831 PRK07831
SDR family oxidoreductase;
27-182 1.64e-05

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 45.41  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGA-NAGVGEELAYHYARLGSHLVLT-AHTEALLQKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFALDK 104
Cdd:PRK07831  15 LAGKVVLVTAAaGTGIGSATARRALEEGARVVISdIHERRLGETADELAAELGLGRVEAVVCDVTSEAQVDALIDAAVER 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  105 LGGLDYLVLNhiggAPAGTRARSPQAT--RW--LMQVNFVSYVQLTSRALPSLTDSKGSLVVV--SSLLGRVPTSFSTPY 178
Cdd:PRK07831  95 LGRLDVLVNN----AGLGGQTPVVDMTddEWsrVLDVTLTGTFRATRAALRYMRARGHGGVIVnnASVLGWRAQHGQAHY 170


                 ....
gi 74750135  179 SAAK 182
Cdd:PRK07831 171 AAAK 174
PRK06128 PRK06128
SDR family oxidoreductase;
27-114 1.91e-05

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 45.62  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLT--AHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDK 104
Cdd:PRK06128  53 LQGRKALITGADSGIGRATAIAFAREGADIALNylPEEEQDAAEVVQLIQAEGR-KAVALPGDLKDEAFCRQLVERAVKE 131

                         90
                 ....*....|
gi 74750135  105 LGGLDYLVLN 114
Cdd:PRK06128 132 LGGLDILVNI 141
PRK08017 PRK08017
SDR family oxidoreductase;
32-196 1.92e-05

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 45.08  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   32 VLLTGANAGVGEELAYHYARLGSHlVLTAHTEAllqKVVGNCRKLGAPKVFYiaaDMASPEAPESVVQFALDKLGGLDYL 111
Cdd:PRK08017   5 VLITGCSSGIGLEAALELKRRGYR-VLAACRKP---DDVARMNSLGFTGILL---DLDDPESVERAADEVIALTDNRLYG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  112 VLNHIGGA---PAGTRARspQATRWLMQVNFVSYVQLTSRALPSLTDS-KGSLVVVSSLLGRVPTSFSTPYSAAKFALDG 187
Cdd:PRK08017  78 LFNNAGFGvygPLSTISR--QQMEQQFSTNFFGTHQLTMLLLPAMLPHgEGRIVMTSSVMGLISTPGRGAYAASKYALEA 155


                 ....*....
gi 74750135  188 FFGSLRREL 196
Cdd:PRK08017 156 WSDALRMEL 164
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-168 2.01e-05

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 45.98  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLT---AHTEAlLQKVVgncRKLGAPKVfyiAADMASPEAPESVVQFALD 103
Cdd:PRK08261 208 LAGKVALVTGAARGIGAAIAEVLARDGAHVVCLdvpAAGEA-LAAVA---NRVGGTAL---ALDITAPDAPARIAEHLAE 280

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74750135  104 KLGGLDYLVLNhiggapAG-TR----ARSPQAtRW--LMQVNFVSYVQLTSRALPS--LTDSkGSLVVVSSLLG 168
Cdd:PRK08261 281 RHGGLDIVVHN------AGiTRdktlANMDEA-RWdsVLAVNLLAPLRITEALLAAgaLGDG-GRIVGVSSISG 346
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 25-203 2.46e-05

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 44.73  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   25 ASLQGARVLLTGANAGVGEELAYHYARLGSHLVLT-AHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALD 103
Cdd:PRK12937   1 MTLSNKVAIVTGASRGIGAAIARRLAADGFAVAVNyAGSAAAADELVAEIEAAGG-RAIAVQADVADAAAVTRLFDAAET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  104 KLGGLDYLVlNHIGGAPAGTRARSPQAT-RWLMQVNfVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAAK 182
Cdd:PRK12937  80 AFGRIDVLV-NNAGVMPLGTIADFDLEDfDRTIATN-LRGAFVVLREAARHLGQGGRIINLSTSVIALPLPGYGPYAASK 157

                        170       180
                 ....*....|....*....|.
gi 74750135  183 FALDGFFGSLRRELDVQDVNV 203
Cdd:PRK12937 158 AAVEGLVHVLANELRGRGITV 178
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 33-211 2.95e-05

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: 44.76  E-value: 2.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  33 LLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFALDKLGGLDYLV 112
Cdd:cd05322   6 VVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKRVDLLV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 113 LNhiggapAGTrARSPQATRW-------LMQVNFVSYVqLTSRALPSLT---DSKGSLVVVSSLLGRVPTSFSTPYSAAK 182
Cdd:cd05322  86 YS------AGI-AKSAKITDFelgdfdrSLQVNLVGYF-LCAREFSKLMirdGIQGRIIQINSKSGKVGSKHNSGYSAAK 157

                       170       180
                ....*....|....*....|....*....
gi 74750135 183 FALDGFFGSLrrELDVQDVNVAITMCVLG 211
Cdd:cd05322 158 FGGVGLTQSL--ALDLAEHGITVNSLMLG 184
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 26-205 3.32e-05

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: 44.76  E-value: 3.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:cd08935   2 SLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGG-RAIALAADVLDRASLERAREEIVAQF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 106 GGLDYLVLNHIGGAPAGT---RARSPQATRWLMQ-----VNFVSYVQLTSRALPS-------LTDSKGSLVVVSSLLGRV 170
Cdd:cd08935  81 GTVDILINGAGGNHPDATtdpEHYEPETEQNFFDldeegWEFVFDLNLNGSFLPSqvfgkdmLEQKGGSIINISSMNAFS 160

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 74750135 171 PTSFSTPYSAAKFALDGFFGSLRRELDVQDVNV-AI 205
Cdd:cd08935 161 PLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVnAI 196
PRK06500 PRK06500
SDR family oxidoreductase;
27-114 5.79e-05

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 43.79  E-value: 5.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVgncRKLGApKVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:PRK06500   4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAAR---AELGE-SALVIRADAGDVAAQKALAQALAEAFG 79


                 ....*...
gi 74750135  107 GLDYLVLN 114
Cdd:PRK06500  80 RLDAVFIN 87
PRK08589 PRK08589
SDR family oxidoreductase;
33-188 8.42e-05

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 43.23  E-value: 8.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   33 LLTGANAGVGEELAYHYARLGSHlVLTAHTEALLQKVVGNCRKLGAPKVFYIAaDMASPEAPESVVQFALDKLGGLDYLv 112
Cdd:PRK08589  10 VITGASTGIGQASAIALAQEGAY-VLAVDIAEAVSETVDKIKSNGGKAKAYHV-DISDEQQVKDFASEIKEQFGRVDVL- 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74750135  113 LNHIGGAPAGTRARSPQATRW--LMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAAKFALDGF 188
Cdd:PRK08589  87 FNNAGVDNAAGRIHEYPVDVFdkIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAADLYRSGYNAAKGAVINF 164
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-114 1.02e-04

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 43.23  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   23 DPASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEAL-LQKVVGNCRKLGAPKVFyIAADMASPEAPESVVQFA 101
Cdd:PRK07792   6 NTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALdASDVLDEIRAAGAKAVA-VAGDISQRATADELVATA 84

                         90
                 ....*....|...
gi 74750135  102 lDKLGGLDYLVLN 114
Cdd:PRK07792  85 -VGLGGLDIVVNN 96
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 27-114 1.11e-04

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: 42.99  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLtahTEALLQKVVGNCRKLGaPKVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAI---ADINLEAARATAAEIG-PAACAISLDVTDQASIDRCVAALVDRWG 76


                ....*...
gi 74750135 107 GLDYLVLN 114
Cdd:cd05363  77 SIDILVNN 84
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 26-185 1.28e-04

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 42.83  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:PRK07523   7 DLTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGL-SAHALAFDVTDHDAVRAAIDAFEAEI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  106 GGLDYLVLNhiggapAGTRARSP----QATRW--LMQVNFVS--YV-QLTSRALpsLTDSKGSLVVVSSLLGRVPTSFST 176
Cdd:PRK07523  86 GPIDILVNN------AGMQFRTPledfPADAFerLLRTNISSvfYVgQAVARHM--IARGAGKIINIASVQSALARPGIA 157


                 ....*....
gi 74750135  177 PYSAAKFAL 185
Cdd:PRK07523 158 PYTATKGAV 166
PRK06484 PRK06484
short chain dehydrogenase; Validated
 24-204 1.31e-04

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 43.30  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   24 PASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVvgncRKLGAPKVFYIAADMASPEAPESVVQFALD 103
Cdd:PRK06484 264 PLAESPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKL----AEALGDEHLSVQADITDEAAVESAFAQIQA 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  104 KLGGLDYLVlNHIGGAP--AGTRARSPQATRWLMQVNFVSYVQlTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAA 181
Cdd:PRK06484 340 RWGRLDVLV-NNAGIAEvfKPSLEQSAEDFTRVYDVNLSGAFA-CARAAARLMSQGGVIVNLGSIASLLALPPRNAYCAS 417

                        170       180
                 ....*....|....*....|...
gi 74750135  182 KFALDGFFGSLRRELDVQDVNVA 204
Cdd:PRK06484 418 KAAVTMLSRSLACEWAPAGIRVN 440
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 26-182 1.44e-04

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: 42.38  E-value: 1.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCrklgAPKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:cd05345   2 RLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADI----GEAAIAIQADVTKRADVEAMVEAALSKF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 106 GGLDYLVLNH-IGGAPAGTRARSPQATRWLMQVNfVSYVQLTSRAL-PSLTD-SKGSLVVVSSLLGRVPTSFSTPYSAAK 182
Cdd:cd05345  78 GRLDILVNNAgITHRNKPMLEVDEEEFDRVFAVN-VKSIYLSAQALvPHMEEqGGGVIINIASTAGLRPRPGLTWYNASK 156
PRK08278 PRK08278
SDR family oxidoreductase;
25-212 2.00e-04

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 42.20  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   25 ASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHT-------EALLQKVVGNCRKLGApKVFYIAADMASPEAPESV 97
Cdd:PRK08278   2 MSLSGKTLFITGASRGIGLAIALRAARDGANIVIAAKTaephpklPGTIHTAAEEIEAAGG-QALPLVGDVRDEDQVAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   98 VQFALDKLGGLDYLVLNHIGGAPAGTRARSPQATRWLMQVNfVSYVQLTSRA-LPSLTDSKGS-LVVVSSLLGRVPTSF- 174
Cdd:PRK08278  81 VAKAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQIN-VRGTFLVSQAcLPHLKKSENPhILTLSPPLNLDPKWFa 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 74750135  175 -STPYSAAKFALdgffgslrreldvqdvnvaiTMCVLGL 212
Cdd:PRK08278 160 pHTAYTMAKYGM--------------------SLCTLGL 178
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 28-235 2.02e-04

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: 42.07  E-value: 2.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  28 QGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVgncrklGAPKVFYIAADMASPEApesvVQFALDKLGG 107
Cdd:cd05368   1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELE------RGPGITTRVLDVTDKEQ----VAALAKEEGR 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 108 LDYLVlNHIGGAPAGTRAR-SPQATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGR---VPTSFStpYSAAK 182
Cdd:cd05368  71 IDVLF-NCAGFVHHGSILDcEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKdGSIINMSSVASSikgVPNRFV--YSTTK 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 183 FALDGFFGSLRRELDVQDVNV-AI---TMCVLGLRDRASAA---EAVRSSTSRpRQPEHR 235
Cdd:cd05368 148 AAVIGLTKSVAADFAQQGIRCnAIcpgTVDTPSLEERIQAQpdpEEALKAFAA-RQPLGR 206
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 26-203 2.18e-04

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 41.92  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQkvvgncrklgAPKVFYIAADMASPEAPESVVQFALDKL 105
Cdd:PRK06171   6 NLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQ----------HENYQFVPTDVSSAEEVNHTVAEIIEKF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  106 GGLDYLVlNHIG----------GAPAGTRARSPQATRWLMQVNfVSYVQLTSRALPSLTDSKGSLVVV-----SSLLGRV 170
Cdd:PRK06171  76 GRIDGLV-NNAGiniprllvdeKDPAGKYELNEAAFDKMFNIN-QKGVFLMSQAVARQMVKQHDGVIVnmsseAGLEGSE 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 74750135  171 PTSFstpYSAAKFALDGFFGSLRRELDVQDVNV 203
Cdd:PRK06171 154 GQSC---YAATKAALNSFTRSWAKELGKHNIRV 183
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
28-165 2.27e-04

Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 42.29  E-value: 2.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  28 QGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTealLQKVVGNCRKLGAPKVFYIAA--DMASpeaPESVVQF--ALD 103
Cdd:COG5748   5 QKSTVIITGASSGVGLYAAKALADRGWHVIMACRD---LEKAEAAAQELGIPPDSYTIIhiDLAS---LESVRRFvaDFR 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74750135 104 KLG-GLDYLVLNHIGGAPAGTRA-RSPQATRWLMQVNFVSYVQLTSRALPSLTDSKGS---LVVVSS 165
Cdd:COG5748  79 ALGrPLDALVCNAAVYYPLLKEPlRSPDGYELSVATNHLGHFLLCNLLLEDLKKSPASdprLVILGT 145
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 32-208 2.39e-04

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 41.35  E-value: 2.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAyhyARLGSHlvltahteallqkvvgncrklGAPKVFYIAADmaspeapESVVQFAldklggldyl 111
Cdd:cd02266   1 VLVTGGSGGIGGAIA---RWLASR---------------------GSPKVLVVSRR-------DVVVHNA---------- 39

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 112 VLNHIGGAPAGTRARSPQATRwlmqVNFVSYVQLTSRALPSLTD-SKGSLVVVSSLLGRVPTSFSTPYSAAKFALDGFFG 190
Cdd:cd02266  40 AILDDGRLIDLTGSRIERAIR----ANVVGTRRLLEAARELMKAkRLGRFILISSVAGLFGAPGLGGYAASKAALDGLAQ 115

                       170
                ....*....|....*...
gi 74750135 191 SLRRELDVQDVNVAITMC 208
Cdd:cd02266 116 QWASEGWGNGLPATAVAC 133
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 27-186 4.13e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 41.09  E-value: 4.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTealLQKVVGNCRKLGA--PKVFYIAADMASPEAPESVVQFALDK 104
Cdd:PRK07576   7 FAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRS---QEKVDAAVAQLQQagPEGLGVSADVRDYAAVEAAFAQIADE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  105 LGGLDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAAKFA 184
Cdd:PRK07576  84 FGPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPGASIIQISAPQAFVPMPMQAHVCAAKAG 163


                 ..
gi 74750135  185 LD 186
Cdd:PRK07576 164 VD 165
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 26-196 4.27e-04

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 41.02  E-value: 4.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   26 SLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLgapkvfyiaaDMASPEAPESVVQFALDKL 105
Cdd:PRK08220   5 DFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDYPFATFVL----------DVSDAAAVAQVCQRLLAET 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  106 GGLDYLVlnhiGGA----PAGTRARSPQATRWLMQVNfVSYVQLTSRAL-PSLTDSK-GSLVVVSSLLGRVPTSFSTPYS 179
Cdd:PRK08220  75 GPLDVLV----NAAgilrMGATDSLSDEDWQQTFAVN-AGGAFNLFRAVmPQFRRQRsGAIVTVGSNAAHVPRIGMAAYG 149

                        170
                 ....*....|....*..
gi 74750135  180 AAKFALDGFFGSLRREL 196
Cdd:PRK08220 150 ASKAALTSLAKCVGLEL 166
PRK06123 PRK06123
SDR family oxidoreductase;
32-203 5.95e-04

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 40.53  E-value: 5.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   32 VLLTGANAGVGEELAYHYARLGSHLVLT-AHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLGGLDY 110
Cdd:PRK06123   5 MIITGASRGIGAATALLAAERGYAVCLNyLRNRDAAEAVVQAIRRQGG-EALAVAADVADEADVLRLFEAVDRELGRLDA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  111 LVlNHIGGAPAGTRARSPQATRW--LMQVNFVSYVQLTSRALPSLTDSK----GSLVVVSSLLGRV--PTSFsTPYSAAK 182
Cdd:PRK06123  84 LV-NNAGILEAQMRLEQMDAARLtrIFATNVVGSFLCAREAVKRMSTRHggrgGAIVNVSSMAARLgsPGEY-IDYAASK 161

                        170       180
                 ....*....|....*....|.
gi 74750135  183 FALDGFFGSLRRELDVQDVNV 203
Cdd:PRK06123 162 GAIDTMTIGLAKEVAAEGIRV 182
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 29-165 7.78e-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: 40.66  E-value: 7.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  29 GARVLLTGANAGVGEELAYHYARLGSHLVLT----AHTEALLQKVVGNCRKlgaPKVFYIAADMASPEAPESVVQFALDK 104
Cdd:cd09809   1 GKVIIITGANSGIGFETARSFALHGAHVILAcrnmSRASAAVSRILEEWHK---ARVEAMTLDLASLRSVQRFAEAFKAK 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74750135 105 LGGLDYLVLNhiGGAPAGTRARSPQATRWLMQVNFVSYVQLTsRALPSLTD--SKGSLVVVSS 165
Cdd:cd09809  78 NSPLHVLVCN--AAVFALPWTLTEDGLETTFQVNHLGHFYLV-QLLEDVLRrsAPARVIVVSS 137
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 31-168 8.20e-04

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 40.17  E-value: 8.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  31 RVLLTGANAGVGEELAYHYARLGSHlvltahteallqkVVGNCRKLGapkvfYIAADMASPEAPESVVQFALDKL-GGLD 109
Cdd:cd05328   1 TIVITGAASGIGAATAELLEDAGHT-------------VIGIDLREA-----DVIADLSTPEGRAAAIADVLARCsGVLD 62

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 110 YLVlnHIGGAPAGTRARSpqatrwLMQVNFVSYVQLTSRALPSLTDSKG-SLVVVSSLLG 168
Cdd:cd05328  63 GLV--NCAGVGGTTVAGL------VLKVNYFGLRALMEALLPRLRKGHGpAAVVVSSIAG 114
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 20-185 8.84e-04

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 40.05  E-value: 8.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   20 DNFdpaSLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIaADMASPEAPESVVQ 99
Cdd:PRK07097   4 NLF---SLKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHGYV-CDVTDEDGVQAMVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  100 FALDKLGGLDYLVLNhiggapAGTRARSPQAT------RWLMQVNFVSYVQLTSRALPSLTD-SKGSLVVVSSL---LGR 169
Cdd:PRK07097  80 QIEKEVGVIDILVNN------AGIIKRIPMLEmsaedfRQVIDIDLNAPFIVSKAVIPSMIKkGHGKIINICSMmseLGR 153

                        170
                 ....*....|....*.
gi 74750135  170 VPTSfstPYSAAKFAL 185
Cdd:PRK07097 154 ETVS---AYAAAKGGL 166
PRK06194 PRK06194
hypothetical protein; Provisional
 27-138 1.19e-03

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 40.00  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPkVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:PRK06194   4 FAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAE-VLGVRTDVSDAAQVEALADAALERFG 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 74750135  107 GLDyLVLNHIG-GAPAGTRARSPQATRWLMQVN 138
Cdd:PRK06194  83 AVH-LLFNNAGvGAGGLVWENSLADWEWVLGVN 114
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 27-114 1.62e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 39.66  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVL---------TAHTEALLQKVVGNCRKLGAPKVFYiAADMASPEAPESV 97
Cdd:PRK07791   4 LDGRVVIVTGAGGGIGRAHALAFAAEGARVVVndigvgldgSASGGSAAQAVVDEIVAAGGEAVAN-GDDIADWDGAANL 82

                         90
                 ....*....|....*..
gi 74750135   98 VQFALDKLGGLDYLVLN 114
Cdd:PRK07791  83 VDAAVETFGGLDVLVNN 99
PRK06947 PRK06947
SDR family oxidoreductase;
32-203 1.68e-03

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 39.40  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   32 VLLTGANAGVGEELAYHYARLG-SHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLGGLDY 110
Cdd:PRK06947   5 VLITGASRGIGRATAVLAAARGwSVGINYARDAAAAEETADAVRAAGG-RACVVAGDVANEADVIAMFDAVQSAFGRLDA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  111 LVLNHIGGAPAGTRARSPQA-TRWLMQVNFVSYVQLTSRALPSLTDSK----GSLVVVSSLLGRVPTSFS-TPYSAAKFA 184
Cdd:PRK06947  84 LVNNAGIVAPSMPLADMDAArLRRMFDTNVLGAYLCAREAARRLSTDRggrgGAIVNVSSIASRLGSPNEyVDYAGSKGA 163

                        170
                 ....*....|....*....
gi 74750135  185 LDGFFGSLRRELDVQDVNV 203
Cdd:PRK06947 164 VDTLTLGLAKELGPHGVRV 182
PRK08862 PRK08862
SDR family oxidoreductase;
32-117 2.12e-03

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 38.94  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLG-GLDY 110
Cdd:PRK08862   8 ILITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQCSALTD-NVYSFQLKDFSQESIRHLFDAIEQQFNrAPDV 86


                 ....*..
gi 74750135  111 LVLNHIG 117
Cdd:PRK08862  87 LVNNWTS 93
PRK06196 PRK06196
oxidoreductase; Provisional
 27-168 2.31e-03

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 39.28  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGncrklGAPKVFYIAADMASPEAPESVVQFALDKLG 106
Cdd:PRK06196  24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALA-----GIDGVEVVMLDLADLESVRAFAERFLDSGR 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74750135  107 GLDYLVLNhiggapAGTRArSPQaTR----WLMQ--VNFVSYVQLTSRALPSLTDSKGSLVVVSSLLG 168
Cdd:PRK06196  99 RIDILINN------AGVMA-CPE-TRvgdgWEAQfaTNHLGHFALVNLLWPALAAGAGARVVALSSAG 158
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 32-196 2.35e-03

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: 38.66  E-value: 2.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQkvvGNCRKLGAPKVfyiAADMASpeapESVVQFALDKLGGLDYL 111
Cdd:cd11730   1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALA---GLAAEVGALAR---PADVAA----ELEVWALAQELGPLDLL 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 112 VlnHIGGA--PAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLtdSKGSLVVvssLLGRVPTSFSTP----YSAAKFAL 185
Cdd:cd11730  71 V--YAAGAilGKPLARTKPAAWRRILDANLTGAALVLKHALALL--AAGARLV---FLGAYPELVMLPglsaYAAAKAAL 143

                       170
                ....*....|.
gi 74750135 186 DGFFGSLRREL 196
Cdd:cd11730 144 EAYVEVARKEV 154
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 27-186 2.62e-03

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: 38.97  E-value: 2.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTA-HTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVV-QFALDK 104
Cdd:cd09763   1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGrTILPQLPGTAEEIEARGG-KCIPVRCDHSDDDEVEALFeRVAREQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 105 LGGLDYLVLNHIGGAPAGTRARSP-----QATRW--LMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTP 177
Cdd:cd09763  80 QGRLDILVNNAYAAVQLILVGVAKpfweePPTIWddINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVA 159


                ....*....
gi 74750135 178 YSAAKFALD 186
Cdd:cd09763 160 YGVGKAAID 168
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 33-194 3.80e-03

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 38.89  E-value: 3.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  33 LLTGANAGVGEELAYHYARL-GSHLVLTAHT------EALLQKVVGnCRKLGAPkVFYIAADMASPEAPESVVQFALDKL 105
Cdd:cd08953 209 LVTGGAGGIGRALARALARRyGARLVLLGRSplppeeEWKAQTLAA-LEALGAR-VLYISADVTDAAAVRRLLEKVRERY 286

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135 106 GGLDYLVlnHIGGAPAGTRARSPQATRWLmQVnFVSYVQLTsRALPSLT--DSKGSLVVVSSLLGRVPTSFSTPYSAAKF 183
Cdd:cd08953 287 GAIDGVI--HAAGVLRDALLAQKTAEDFE-AV-LAPKVDGL-LNLAQALadEPLDFFVLFSSVSAFFGGAGQADYAAANA 361

                       170
                ....*....|.
gi 74750135 184 ALDGFFGSLRR 194
Cdd:cd08953 362 FLDAFAAYLRQ 372
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 32-109 4.29e-03

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 37.46  E-value: 4.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135     32 VLLTGANAGVGEELAYHYARLG-SHLVLT---AHTEALLQKVVGNCRKLGApKVFYIAADMASPEAPESVVQFALDKLGG 107
Cdd:smart00822   3 YLITGGLGGLGRALARWLAERGaRRLVLLsrsGPDAPGAAALLAELEAAGA-RVTVVACDVADRDALAAVLAAIPAVEGP 81


                   ..
gi 74750135    108 LD 109
Cdd:smart00822  82 LT 83
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 27-199 5.68e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 37.79  E-value: 5.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   27 LQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLgapkvfYIAADMASPEAPESVVQFALDKLG 106
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGGL------FVPTDVTDEDAVNALFDTAAETYG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  107 GLDyLVLNHIGGAP---AGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDS-KGSLVVVSSLLGRVPTSFST-PYSAA 181
Cdd:PRK06057  79 SVD-IAFNNAGISPpedDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQgKGSIINTASFVAVMGSATSQiSYTAS 157

                        170
                 ....*....|....*...
gi 74750135  182 KfaldGFFGSLRRELDVQ 199
Cdd:PRK06057 158 K----GGVLAMSRELGVQ 171
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
23-203 6.11e-03

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 37.55  E-value: 6.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   23 DPASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEAL--LQKVVGNCRKLgapkvFYIAADMASPEAPESVVQF 100
Cdd:PRK08993   4 DAFSLEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEPTetIEQVTALGRRF-----LSLTADLRKIDGIPALLER 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  101 ALDKLGGLDYLVLNhiggapAGTRAR------SPQATRWLMQVNFVSyVQLTSRALPSLTDSKGS---LVVVSSLLG--- 168
Cdd:PRK08993  79 AVAEFGHIDILVNN------AGLIRRedaiefSEKDWDDVMNLNIKS-VFFMSQAAAKHFIAQGNggkIINIASMLSfqg 151

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 74750135  169 --RVPTsfstpYSAAKFALDGFFGSLRRELDVQDVNV 203
Cdd:PRK08993 152 giRVPS-----YTASKSGVMGVTRLMANEWAKHNINV 183
PRK07102 PRK07102
SDR family oxidoreductase;
32-203 6.24e-03

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 37.60  E-value: 6.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEAPESVvqfaLDKLGGLDYL 111
Cdd:PRK07102   4 ILIIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARGAVAVSTHELDILDTASHAAF----LDSLPALPDI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  112 VLNHIGGAPAGTRA-RSPQATRWLMQVNFVSYVQLTSRALPSLTDSK-GSLVVVSSLLGRVPTSFSTPYSAAKFALDGFF 189
Cdd:PRK07102  80 VLIAVGTLGDQAACeADPALALREFRTNFEGPIALLTLLANRFEARGsGTIVGISSVAGDRGRASNYVYGSAKAALTAFL 159

                        170
                 ....*....|....
gi 74750135  190 GSLRRELDVQDVNV 203
Cdd:PRK07102 160 SGLRNRLFKSGVHV 173
PRK08267 PRK08267
SDR family oxidoreductase;
32-207 8.96e-03

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 37.22  E-value: 8.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135   32 VLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVgncRKLGAPKVFYIAADMASPEA-PESVVQFALDKLGGLDY 110
Cdd:PRK08267   4 IFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALA---AELGAGNAWTGALDVTDRAAwDAALADFAAATGGRLDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74750135  111 LVlNHIGGAPAGT-RARSPQATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVV---VSSLLGRVPTsfSTPYSAAKFALD 186
Cdd:PRK08267  81 LF-NNAGILRGGPfEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVIntsSASAIYGQPG--LAVYSATKFAVR 157

                        170       180
                 ....*....|....*....|.
gi 74750135  187 GFFGSLRRELDVQDVNVAITM 207
Cdd:PRK08267 158 GLTEALDLEWRRHGIRVADVM 178
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

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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