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Conserved domains on  [gi|8567342|ref|NP_059501|]
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retinol dehydrogenase 7 [Mus musculus]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10176849)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase may catalyze isomerization, decarboxylation, epimerization, C=N bond reduction, dehydration, dehalogenation, enoyl-CoA reduction, and/or carbonyl-alcohol oxidoreduction; 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

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0051287|GO:0016491
PubMed:  12604210|19011748|19027726|20423462|19011750

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 30-305 2.59e-144

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: 407.82  E-value: 2.59e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE--KGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLW 107
Cdd:cd09805   1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  108 GLVNNAGICVF-AINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISSSMGRVSL-CGGGYCISKYGVEAF 185
Cdd:cd09805  81 GLVNNAGILGFgGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFpAGGAYCASKAAVEAF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  186 SDSLRREISYFGVKVAIIEPGGFRTNVSNYERLSHSIEK-LWDQTSSEVKEVYDKNFLDSYIKAIQSLTDTCSDDLSVVT 264
Cdd:cd09805 161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQAKkLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 8567342  265 DCMEHALTACHPRTRYSAGWDAKLFYLPLSYMPTFLVDAML 305
Cdd:cd09805 241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 30-305 2.59e-144

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: 407.82  E-value: 2.59e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE--KGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLW 107
Cdd:cd09805   1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  108 GLVNNAGICVF-AINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISSSMGRVSL-CGGGYCISKYGVEAF 185
Cdd:cd09805  81 GLVNNAGILGFgGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFpAGGAYCASKAAVEAF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  186 SDSLRREISYFGVKVAIIEPGGFRTNVSNYERLSHSIEK-LWDQTSSEVKEVYDKNFLDSYIKAIQSLTDTCSDDLSVVT 264
Cdd:cd09805 161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQAKkLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 8567342  265 DCMEHALTACHPRTRYSAGWDAKLFYLPLSYMPTFLVDAML 305
Cdd:cd09805 241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
27-211 1.96e-47

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 159.65  E-value: 1.96e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRN---KTSDRLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:COG0300   3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAelrAAGARVEVVALDVTDPDAVAALAEAVLARFG- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  104 rGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCG-GGYCISKYG 181
Cdd:COG0300  82 -PIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPlMRARGRGRIVNVSSVAGLRGLPGmAAYAASKAA 160

                       170       180       190
                ....*....|....*....|....*....|
gi 8567342  182 VEAFSDSLRREISYFGVKVAIIEPGGFRTN 211
Cdd:COG0300 161 LEGFSESLRAELAPTGVRVTAVCPGPVDTP 190
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 30-217 1.92e-43

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 147.76  E-value: 1.92e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342     30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNK---TSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKElgaLGGKALFIQGDVTDRAQVKALVEQAVERLG--RL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    107 WGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSL-CGGGYCISKYGVEA 184
Cdd:pfam00106  79 DILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPYpGGSAYSASKAAVIG 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 8567342    185 FSDSLRREISYFGVKVAIIEPGGFRTNVSNYER 217
Cdd:pfam00106 159 FTRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
PRK06914 PRK06914
SDR family oxidoreductase;
30-308 7.56e-41

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 143.63  E-value: 7.56e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKT-----SDRLETVILDVTKTESIVAATQWVKErVGNR 104
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQAtqlnlQQNIKVQQLDVTDQNSIHNFQLVLKE-IGRI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   105 GLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCG-GGYCISKYGV 182
Cdd:PRK06914  83 DL--LVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGlSPYVSSKYAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   183 EAFSDSLRREISYFGVKVAIIEPGGFRTNVSNyerLSHSIEKLWDQTSSEVKEVYDKnfldsYIKAIQSLTDTCSDDLSV 262
Cdd:PRK06914 161 EGFSESLRLELKPFGIDVALIEPGSYNTNIWE---VGKQLAENQSETTSPYKEYMKK-----IQKHINSGSDTFGNPIDV 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 8567342   263 VTDCMEHAlTACHPRTRYSAGWDAKLfylplsympTFLVDAMLYWS 308
Cdd:PRK06914 233 ANLIVEIA-ESKRPKLRYPIGKGVKL---------MILAKKILPWR 268
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 32-226 1.86e-20

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


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 88.03  E-value: 1.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342     32 VFITGCDSGFGNLLARQLDRRGMRVLAACLT-EKGAEQLRNKTSD---RLETVILDVTKTESIVAATQWVKERVGnrGLW 107
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSsEEGAEEVVEELKAlgvKALGVVLDVSDREDVKAVVEEIEEELG--TID 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    108 GLVNNAGIC--VFAINewLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGrvsLCGGG----YCISKY 180
Cdd:TIGR01830  79 ILVNNAGITrdNLLMR--MKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRsGRIINISSVVG---LMGNAgqanYAASKA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 8567342    181 GVEAFSDSLRREISYFGVKVAIIEPGGFRTNVSnyERLSHSIEKLW 226
Cdd:TIGR01830 154 GVIGFTKSLAKELASRNITVNAVAPGFIDTDMT--DKLSEKVKKKI 197
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 30-305 2.59e-144

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: 407.82  E-value: 2.59e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE--KGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLW 107
Cdd:cd09805   1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  108 GLVNNAGICVF-AINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISSSMGRVSL-CGGGYCISKYGVEAF 185
Cdd:cd09805  81 GLVNNAGILGFgGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFpAGGAYCASKAAVEAF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  186 SDSLRREISYFGVKVAIIEPGGFRTNVSNYERLSHSIEK-LWDQTSSEVKEVYDKNFLDSYIKAIQSLTDTCSDDLSVVT 264
Cdd:cd09805 161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQAKkLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 8567342  265 DCMEHALTACHPRTRYSAGWDAKLFYLPLSYMPTFLVDAML 305
Cdd:cd09805 241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 30-287 1.27e-64

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: 204.00  E-value: 1.27e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGLWGL 109
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFG--RIDVL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  110 VNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSL-CGGGYCISKYGVEAFSD 187
Cdd:cd05374  79 VNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGsGRIVNVSSVAGLVPTpFLGPYCASKAALEALSE 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  188 SLRREISYFGVKVAIIEPGGFRTNVSNYE---RLSHSIEKLWDQTSSEVKEVYDKNfldsyikaiqsltDTCSDDLSVVT 264
Cdd:cd05374 159 SLRLELAPFGIKVTIIEPGPVRTGFADNAagsALEDPEISPYAPERKEIKENAAGV-------------GSNPGDPEKVA 225

                       250       260
                ....*....|....*....|...
gi 8567342  265 DCMEHALTACHPRTRYSAGWDAK 287
Cdd:cd05374 226 DVIVKALTSESPPLRYFLGSDAL 248
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
27-211 1.96e-47

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 159.65  E-value: 1.96e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRN---KTSDRLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:COG0300   3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAelrAAGARVEVVALDVTDPDAVAALAEAVLARFG- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  104 rGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCG-GGYCISKYG 181
Cdd:COG0300  82 -PIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPlMRARGRGRIVNVSSVAGLRGLPGmAAYAASKAA 160

                       170       180       190
                ....*....|....*....|....*....|
gi 8567342  182 VEAFSDSLRREISYFGVKVAIIEPGGFRTN 211
Cdd:COG0300 161 LEGFSESLRAELAPTGVRVTAVCPGPVDTP 190
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 28-214 5.09e-46

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: 155.73  E-value: 5.09e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGLW 107
Cdd:COG4221   4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFG--RLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  108 GLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCGGG-YCISKYGVEAF 185
Cdd:COG4221  82 VLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPaMRARGSGHIVNISSIAGLRPYPGGAvYAATKAAVRGL 161

                       170       180
                ....*....|....*....|....*....
gi 8567342  186 SDSLRREISYFGVKVAIIEPGGFRTNVSN 214
Cdd:COG4221 162 SESLRAELRPTGIRVTVIEPGAVDTEFLD 190
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 30-217 1.92e-43

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 147.76  E-value: 1.92e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342     30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNK---TSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKElgaLGGKALFIQGDVTDRAQVKALVEQAVERLG--RL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    107 WGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSL-CGGGYCISKYGVEA 184
Cdd:pfam00106  79 DILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPYpGGSAYSASKAAVIG 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 8567342    185 FSDSLRREISYFGVKVAIIEPGGFRTNVSNYER 217
Cdd:pfam00106 159 FTRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
PRK06914 PRK06914
SDR family oxidoreductase;
30-308 7.56e-41

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 143.63  E-value: 7.56e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKT-----SDRLETVILDVTKTESIVAATQWVKErVGNR 104
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQAtqlnlQQNIKVQQLDVTDQNSIHNFQLVLKE-IGRI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   105 GLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCG-GGYCISKYGV 182
Cdd:PRK06914  83 DL--LVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGlSPYVSSKYAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   183 EAFSDSLRREISYFGVKVAIIEPGGFRTNVSNyerLSHSIEKLWDQTSSEVKEVYDKnfldsYIKAIQSLTDTCSDDLSV 262
Cdd:PRK06914 161 EGFSESLRLELKPFGIDVALIEPGSYNTNIWE---VGKQLAENQSETTSPYKEYMKK-----IQKHINSGSDTFGNPIDV 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 8567342   263 VTDCMEHAlTACHPRTRYSAGWDAKLfylplsympTFLVDAMLYWS 308
Cdd:PRK06914 233 ANLIVEIA-ESKRPKLRYPIGKGVKL---------MILAKKILPWR 268
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 33-211 2.22e-39

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 139.67  E-value: 2.22e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    33 FITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGLWGLVNN 112
Cdd:PRK06180   8 LITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFG--PIDVLVNN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   113 AGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCG-GGYCISKYGVEAFSDSLR 190
Cdd:PRK06180  86 AGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRrGHIVNITSMGGLITMPGiGYYCGSKFALEGISESLA 165

                        170       180
                 ....*....|....*....|.
gi 8567342   191 REISYFGVKVAIIEPGGFRTN 211
Cdd:PRK06180 166 KEVAPFGIHVTAVEPGSFRTD 186
PRK08017 PRK08017
SDR family oxidoreductase;
30-307 2.33e-39

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 139.07  E-value: 2.33e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    30 KYVFITGCDSGFGNLLARQLDRRGMRVLAAClteKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRgLWGL 109
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAAC---RKPDDVARMNSLGFTGILLDLDDPESVERAADEVIALTDNR-LYGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   110 VNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVR-KARGRVVNISSSMGRVSLCG-GGYCISKYGVEAFSD 187
Cdd:PRK08017  79 FNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLpHGEGRIVMTSSVMGLISTPGrGAYAASKYALEAWSD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   188 SLRREISYFGVKVAIIEPGGFRTnvsnyeRLSHSIeklwDQTSSevkevyDKNFLDSYIKAIQSLTDtcsddlSVVTDCM 267
Cdd:PRK08017 159 ALRMELRHSGIKVSLIEPGPIRT------RFTDNV----NQTQS------DKPVENPGIAARFTLGP------EAVVPKL 216

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 8567342   268 EHALTACHPRTRYSAGWDAKLFYLPLSYMPTFLVDAMLYW 307
Cdd:PRK08017 217 RHALESPKPKLRYPVTLVTHAVMVLKRLLPGRMMDKILRG 256
PRK06182 PRK06182
short chain dehydrogenase; Validated
 28-304 7.01e-39

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 138.17  E-value: 7.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAAClteKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLw 107
Cdd:PRK06182   2 QKKVALVTGASSGIGKATARRLAAQGYTVYGAA---RRVDKMEDLASLGVHPLSLDVTDEASIKAAVDTIIAEEGRIDV- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   108 gLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRV-SLCGGGYCISKYGVEAF 185
Cdd:PRK06182  78 -LVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIyTPLGAWYHATKFALEGF 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   186 SDSLRREISYFGVKVAIIEPGGFRTN--------------VSNYERLSHSIEKLWDQTssevkevYDKNFLdsyikaiqs 251
Cdd:PRK06182 157 SDALRLEVAPFGIDVVVIEPGGIKTEwgdiaadhllktsgNGAYAEQAQAVAASMRST-------YGSGRL--------- 220

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 8567342   252 ltdtcsDDLSVVTDCMEHALTACHPRTRYSAGWDAKlfylPLSYMPTFLVDAM 304
Cdd:PRK06182 221 ------SDPSVIADAISKAVTARRPKTRYAVGFGAK----PLIFLRRILPDRA 263
PRK05993 PRK05993
SDR family oxidoreductase;
30-309 1.63e-36

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 132.07  E-value: 1.63e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNktsDRLETVILDVTKTESIVAATQWVKERVGNRgLWGL 109
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEA---EGLEAFQLDYAEPESIAALVAQVLELSGGR-LDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   110 VNN-----AGicvfAInEWLKKEDFANILDVNLLGMIEVTLSMLPLVRK-ARGRVVNISSSMGRVSL-CGGGYCISKYGV 182
Cdd:PRK05993  81 FNNgaygqPG----AV-EDLPTEALRAQFEANFFGWHDLTRRVIPVMRKqGQGRIVQCSSILGLVPMkYRGAYNASKFAI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   183 EAFSDSLRREISYFGVKVAIIEPGGFRTNVSnYERLSHsIEKLWDQTSSEVKEvydknfldSYIKAIQSLTDTCSDDLSV 262
Cdd:PRK05993 156 EGLSLTLRMELQGSGIHVSLIEPGPIETRFR-ANALAA-FKRWIDIENSVHRA--------AYQQQMARLEGGGSKSRFK 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 8567342   263 -----VTDCMEHALTACHPRTRYSAGWDAKLFYLPLSYMPTFLVDAMLYWSS 309
Cdd:PRK05993 226 lgpeaVYAVLLHALTAPRPRPHYRVTTPAKQGALLKRLLPARWLYRLLRKAA 277
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 28-305 4.08e-36

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 130.79  E-value: 4.08e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAAclTEKGAeqlRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLw 107
Cdd:PRK06179   3 NSKVALVTGASSGIGRATAEKLARAGYRVFGT--SRNPA---RAAPIPGVELLELDVTDDASVQAAVDEVIARAGRIDV- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   108 gLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSL-CGGGYCISKYGVEAF 185
Cdd:PRK06179  77 -LVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGsGRIINISSVLGFLPApYMALYAASKHAVEGY 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   186 SDSLRREISYFGVKVAIIEPGGFRTNvsnyerlshsieklWDQTSSEVK---EVYDKNFlDSYIKAIQSLTDTcSDDLSV 262
Cdd:PRK06179 156 SESLDHEVRQFGIRVSLVEPAYTKTN--------------FDANAPEPDsplAEYDRER-AVVSKAVAKAVKK-ADAPEV 219

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 8567342   263 VTDCMEHALTACHPRTRYSAGWDAKLFYLPLSYMPTFLVDAML 305
Cdd:PRK06179 220 VADTVVKAALGPWPKMRYTAGGQASLLSKLRRFMPAGAVDKSL 262
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 32-211 1.46e-34

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: 125.86  E-value: 1.46e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSD--RLETVILDVTKTESIVAATQWVKERVGnrGLWGL 109
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEALggNAVAVQADVSDEEDVEALVEEALEEFG--RLDIL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  110 VNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCG-GGYCISKYGVEAFSD 187
Cdd:cd05233  79 VNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGgGRIVNISSVAGLRPLPGqAAYAASKAALEGLTR 158

                       170       180
                ....*....|....*....|....
gi 8567342  188 SLRREISYFGVKVAIIEPGGFRTN 211
Cdd:cd05233 159 SLALELAPYGIRVNAVAPGLVDTP 182
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 25-210 2.76e-34

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: 125.28  E-value: 2.76e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   25 SHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLR---NKTSDRLETVILDVTKTESIVAATQWVKERV 101
Cdd:COG1028   2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAaelRAAGGRALAVAADVTDEAAVEALVAAAVAAF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  102 GnrGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCG-GGYCISK 179
Cdd:COG1028  82 G--RLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGgGRIVNISSIAGLRGSPGqAAYAASK 159

                       170       180       190
                ....*....|....*....|....*....|.
gi 8567342  180 YGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:COG1028 160 AAVVGLTRSLALELAPRGIRVNAVAPGPIDT 190
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 27-214 4.60e-33

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: 122.31  E-value: 4.60e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacLT-------EKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKE 99
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLV---LSarreerlEEVKSECLELGAPSPHVVPLDMSDLEDAEQVVEEALK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  100 RVGnrGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCG-GGYCI 177
Cdd:cd05332  78 LFG--GLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPhLIERSQGSIVVVSSIAGKIGVPFrTAYAA 155

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 8567342  178 SKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVSN 214
Cdd:cd05332 156 SKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAM 192
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 33-211 7.71e-33

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 122.45  E-value: 7.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    33 FITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNrgLWGLVNN 112
Cdd:PRK08263   7 FITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGR--LDIVVNN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   113 AGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCGGG-YCISKYGVEAFSDSLR 190
Cdd:PRK08263  85 AGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRsGHIIQISSIGGISAFPMSGiYHASKWALEGMSEALA 164

                        170       180
                 ....*....|....*....|.
gi 8567342   191 REISYFGVKVAIIEPGGFRTN 211
Cdd:PRK08263 165 QEVAEFGIKVTLVEPGGYSTD 185
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 27-224 1.06e-32

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: 121.11  E-value: 1.06e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNK---TSDRLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:cd08934   1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADEleaEGGKALVLELDVTDEQQVDAAVERTVEALG- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  104 rGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVR-KARGRVVNISSSMGRVSLCG-GGYCISKYG 181
Cdd:cd08934  80 -RLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLlRNKGTIVNISSVAGRVAVRNsAVYNATKFG 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 8567342  182 VEAFSDSLRREISYFGVKVAIIEPGGFRTNVSnyERLSHSIEK 224
Cdd:cd08934 159 VNAFSEGLRQEVTERGVRVVVIEPGTVDTELR--DHITHTITK 199
PRK06482 PRK06482
SDR family oxidoreductase;
33-211 4.57e-31

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 117.52  E-value: 4.57e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    33 FITGCDSGFGNLLARQLDRRGMRVlAACLTEKGA-EQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLwgLVN 111
Cdd:PRK06482   6 FITGASSGFGRGMTERLLARGDRV-AATVRRPDAlDDLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAALGRIDV--VVS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   112 NAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCGGG-YCISKYGVEAFSDSL 189
Cdd:PRK06482  83 NAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGgGRIVQVSSEGGQIAYPGFSlYHATKWGIEGFVEAV 162

                        170       180
                 ....*....|....*....|..
gi 8567342   190 RREISYFGVKVAIIEPGGFRTN 211
Cdd:PRK06482 163 AQEVAPFGIEFTIVEPGPARTN 184
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 30-215 4.20e-30

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: 113.87  E-value: 4.20e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRG--MRVLAACLTEKG---AEQLRNKTSDrLETVILDVTKTESIVAATQWVKERVGnr 104
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGpgTVILTARDVERGqaaVEKLRAEGLS-VRFHQLDVTDDASIEAAADFVEEKYG-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  105 GLWGLVNNAGICVFAINEWLKKEDFAN-ILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLcggGYCISKYGV 182
Cdd:cd05324  78 GLDILVNNAGIAFKGFDDSTPTREQAReTMKTNFFGTVDVTQALLPLLKKSPaGRIVNVSSGLGSLTS---AYGVSKAAL 154

                       170       180       190
                ....*....|....*....|....*....|...
gi 8567342  183 EAFSDSLRREISYFGVKVAIIEPGGFRTNVSNY 215
Cdd:cd05324 155 NALTRILAKELKETGIKVNACCPGWVKTDMGGG 187
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 27-211 7.73e-30

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 113.75  E-value: 7.73e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLT-EKGAEQLRNKTSD---RLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASsEAGAEALVAEIGAlggKALAVQGDVSDAESVERAVDEAKAEFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   103 nrGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCGGG-YCISKY 180
Cdd:PRK05557  83 --GVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRsGRIINISSVVGLMGNPGQAnYAASKA 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 8567342   181 GVEAFSDSLRREISYFGVKVAIIEPGGFRTN 211
Cdd:PRK05557 161 GVIGFTKSLARELASRGITVNAVAPGFIETD 191
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 32-213 5.71e-29

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


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 110.85  E-value: 5.71e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   32 VFITGCDSGFGNLLARQLDRRG-MRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLWGLV 110
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSAATELAALGASHSRLHILELDVTDEIAESAEAVAERLGDAGLDVLI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  111 NNAGIC-VFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKA-RGRVVNISSSMG----RVSLCGGGYCISKYGVEA 184
Cdd:cd05325  81 NNAGILhSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGaRAKIINISSRVGsigdNTSGGWYSYRASKAALNM 160

                       170       180
                ....*....|....*....|....*....
gi 8567342  185 FSDSLRREISYFGVKVAIIEPGGFRTNVS 213
Cdd:cd05325 161 LTKSLAVELKRDGITVVSLHPGWVRTDMG 189
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 29-210 9.53e-28

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: 107.72  E-value: 9.53e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQL-------RNKTSDRLETVILDVTKTESIVAATQWVKERV 101
Cdd:cd08939   1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAveeieaeANASGQKVSYISADLSDYEEVEQAFAQAVEKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  102 GNRGLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCG-GGYCISK 179
Cdd:cd08939  81 GPPDL--VVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRpGHIVFVSSQAALVGIYGySAYCPSK 158

                       170       180       190
                ....*....|....*....|....*....|.
gi 8567342  180 YGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd08939 159 FALRGLAESLRQELKPYNIRVSVVYPPDTDT 189
PRK09072 PRK09072
SDR family oxidoreductase;
26-210 1.89e-27

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 107.72  E-value: 1.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTS--DRLETVILDVTKTESIVAATQWVKErvgN 103
Cdd:PRK09072   2 DLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPypGRHRWVVADLTSEAGREAVLARARE---M 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   104 RGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKA-RGRVVNISSSMGRVSLCG-GGYCISKYG 181
Cdd:PRK09072  79 GGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQpSAMVVNVGSTFGSIGYPGyASYCASKFA 158

                        170       180
                 ....*....|....*....|....*....
gi 8567342   182 VEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK09072 159 LRGFSEALRRELADTGVRVLYLAPRATRT 187
PRK05650 PRK05650
SDR family oxidoreductase;
32-242 3.47e-26

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 104.35  E-value: 3.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAE---QLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGLWG 108
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLALADVNEEGGEetlKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKWG--GIDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   109 LVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCG-GGYCISKYGVEAFS 186
Cdd:PRK05650  81 IVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKsGRIVNIASMAGLMQGPAmSSYNVAKAGVVALS 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8567342   187 DSLRREISYFGVKVAIIEPGGFRTNV-----SNYERLSHSIEKLWDQ---TSSEVKE-----VYDKNFL 242
Cdd:PRK05650 161 ETLLVELADDEIGVHVVCPSFFQTNLldsfrGPNPAMKAQVGKLLEKspiTAADIADyiyqqVAKGEFL 229
PRK12826 PRK12826
SDR family oxidoreductase;
27-210 2.89e-25

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 101.53  E-value: 2.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLT----EKGAEQLRnKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK12826   4 LEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICgddaAATAELVE-AAGGKARARQVDVRDRAALKAAVAAGVEDFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   103 nrGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCGG--GYCISK 179
Cdd:PRK12826  83 --RLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPaLIRAGGGRIVLTSSVAGPRVGYPGlaHYAASK 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 8567342   180 YGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK12826 161 AGLVGFTRALALELAARNITVNSVHPGGVDT 191
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 27-202 3.72e-25

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 102.36  E-value: 3.72e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNK--TSDRLETVILDVTKTESIVAATQWVKERVGnr 104
Cdd:PRK05872   7 LAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAElgGDDRVLTVVADVTDLAAMQAAAEEAVERFG-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   105 GLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISS------SMGrvslcGGGYCIS 178
Cdd:PRK05872  85 GIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSlaafaaAPG-----MAAYCAS 159

                        170       180
                 ....*....|....*....|....
gi 8567342   179 KYGVEAFSDSLRREISYFGVKVAI 202
Cdd:PRK05872 160 KAGVEAFANALRLEVAHHGVTVGS 183
PRK09291 PRK09291
SDR family oxidoreductase;
30-210 3.87e-25

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 101.23  E-value: 3.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDR---LETVILDVTKTESIVAATQW---Vkervgn 103
Cdd:PRK09291   3 KTILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRglaLRVEKLDLTDAIDRAQAAEWdvdV------ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   104 rglwgLVNNAGI----CVFAINEWLKKEDFanilDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCGGG-YCI 177
Cdd:PRK09291  77 -----LLNNAGIgeagAVVDIPVELVRELF----ETNVFGPLELTQGFVRkMVARGKGKVVFTSSMAGLITGPFTGaYCA 147

                        170       180       190
                 ....*....|....*....|....*....|...
gi 8567342   178 SKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK09291 148 SKHALEAIAEAMHAELKPFGIQVATVNPGPYLT 180
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
27-211 9.57e-25

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 99.85  E-value: 9.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTS---DRLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRaagGEARVLVFDVSDEAAVRALIEAAVEAFG- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   104 rGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCGGG-YCISKYG 181
Cdd:PRK05653  82 -ALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARyGRIVNISSVSGVTGNPGQTnYSAAKAG 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 8567342   182 VEAFSDSLRREISYFGVKVAIIEPGGFRTN 211
Cdd:PRK05653 161 VIGFTKALALELASRGITVNAVAPGFIDTD 190
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
30-206 1.09e-24

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 99.84  E-value: 1.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGA----EQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRG 105
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCakdwFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGPVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   106 LwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVR-KARGRVVNISSSMGRVSLCGG-GYCISKYGVE 183
Cdd:PRK12824  83 I--LVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCeQGYGRIINISSVNGLKGQFGQtNYSAAKAGMI 160

                        170       180
                 ....*....|....*....|...
gi 8567342   184 AFSDSLRREISYFGVKVAIIEPG 206
Cdd:PRK12824 161 GFTKALASEGARYGITVNCIAPG 183
PRK07326 PRK07326
SDR family oxidoreductase;
27-217 1.26e-24

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 99.31  E-value: 1.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVIL--DVTKTESIVAATQWVKERVGnr 104
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGNVLGLaaDVRDEADVQRAVDAIVAAFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   105 GLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISSSMGRVSLCGG-GYCISKYGVE 183
Cdd:PRK07326  82 GLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGTNFFAGGaAYNASKFGLV 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 8567342   184 AFSDSLRREISYFGVKVAIIEPGGFRTNVSNYER 217
Cdd:PRK07326 162 GFSEAAMLDLRQYGIKVSTIMPGSVATHFNGHTP 195
PRK05693 PRK05693
SDR family oxidoreductase;
32-230 1.28e-24

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 100.25  E-value: 1.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    32 VFITGCDSGFGNLLARQLDRRGMRVLAaclTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGLWGLVN 111
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWA---TARKAEDVEALAAAGFTAVQLDVNDGAALARLAEELEAEHG--GLDVLIN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   112 NAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISSSMG-RVSLCGGGYCISKYGVEAFSDSLR 190
Cdd:PRK05693  79 NAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGvLVTPFAGAYCASKAAVHALSDALR 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 8567342   191 REISYFGVKVAIIEPGGFRTNVSnyERLSHSIEKLWDQTS 230
Cdd:PRK05693 159 LELAPFGVQVMEVQPGAIASQFA--SNASREAEQLLAEQS 196
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 30-206 1.31e-24

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: 99.54  E-value: 1.31e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGA---EQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAaetVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFG--PV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  107 WGLVNNAGIC--VFAINewLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCG-GGYCISKYGV 182
Cdd:cd05333  79 DILVNNAGITrdNLLMR--MSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRsGRIINISSVVGLIGNPGqANYAASKAGV 156

                       170       180
                ....*....|....*....|....
gi 8567342  183 EAFSDSLRREISYFGVKVAIIEPG 206
Cdd:cd05333 157 IGFTKSLAKELASRGITVNAVAPG 180
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 32-206 1.32e-24

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: 99.62  E-value: 1.32e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRN---KTSDRLETVILDVTKTESIVAATQWVKERVGNRGLwg 108
Cdd:cd05339   2 VLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANnvrKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTI-- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  109 LVNNAGICvfAINEWLK--KEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCGGG-YCISKYGVEA 184
Cdd:cd05339  80 LINNAGVV--SGKKLLElpDEEIEKTFEVNTLAHFWTTKAFLPdMLERNHGHIVTIASVAGLISPAGLAdYCASKAAAVG 157

                       170       180
                ....*....|....*....|....*
gi 8567342  185 FSDSLRREISYF---GVKVAIIEPG 206
Cdd:cd05339 158 FHESLRLELKAYgkpGIKTTLVCPY 182
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 30-213 1.83e-24

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


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 98.73  E-value: 1.83e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGLWGL 109
Cdd:cd08929   1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFG--GLDAL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  110 VNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTL-SMLPLVRKARGRVVNISSSMGRVSLCGG-GYCISKYGVEAFSD 187
Cdd:cd08929  79 VNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHkAAPALLRRGGGTIVNVGSLAGKNAFKGGaAYNASKFGLLGLSE 158

                       170       180
                ....*....|....*....|....*.
gi 8567342  188 SLRREISYFGVKVAIIEPGGFRTNVS 213
Cdd:cd08929 159 AAMLDLREANIRVVNVMPGSVDTGFA 184
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 27-210 2.48e-24

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: 98.63  E-value: 2.48e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGM-RVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKErvgnrg 105
Cdd:cd05354   1 IKDKTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAAQAKD------ 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  106 LWGLVNNAGIcvFAINEWLKKEDFAN---ILDVNLLGMIEVTLSMLPLVRKA-RGRVVNISSSMGRVSLCG-GGYCISKY 180
Cdd:cd05354  75 VDVVINNAGV--LKPATLLEEGALEAlkqEMDVNVFGLLRLAQAFAPVLKANgGGAIVNLNSVASLKNFPAmGTYSASKS 152

                       170       180       190
                ....*....|....*....|....*....|
gi 8567342  181 GVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd05354 153 AAYSLTQGLRAELAAQGTLVLSVHPGPIDT 182
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 30-214 4.45e-24

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: 98.12  E-value: 4.45e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRGMRVLaacLT-------EKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:cd05346   1 KTVLITGASSGIGEATARRFAKAGAKLI---LTgrraerlQELADELGAKFPVKVLPLQLDVSDRESIEAALENLPEEFR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  103 NrgLWGLVNNAGICVFAINEW-LKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCGGG-YCISK 179
Cdd:cd05346  78 D--IDILVNNAGLALGLDPAQeADLEDWETMIDTNVKGLLNVTRLILPiMIARNQGHIINLGSIAGRYPYAGGNvYCATK 155

                       170       180       190
                ....*....|....*....|....*....|....*
gi 8567342  180 YGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVSN 214
Cdd:cd05346 156 AAVRQFSLNLRKDLIGTGIRVTNIEPGLVETEFSL 190
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 32-210 4.67e-24

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: 97.84  E-value: 4.67e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG----AEQLRNKTSDRLeTVILDVTKTESIVAATQWVKERVGNRGLW 107
Cdd:cd05360   3 VVITGASSGIGRATALAFAERGAKVVLAARSAEAlhelAREVRELGGEAI-AVVADVADAAQVERAADTAVERFGRIDTW 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  108 glVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMG-RVSLCGGGYCISKYGVEAF 185
Cdd:cd05360  82 --VNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPhLRRRGGGALINVGSLLGyRSAPLQAAYSASKHAVRGF 159

                       170       180
                ....*....|....*....|....*..
gi 8567342  186 SDSLRREISYFGVKVAI--IEPGGFRT 210
Cdd:cd05360 160 TESLRAELAHDGAPISVtlVQPTAMNT 186
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 30-280 5.83e-24

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: 98.30  E-value: 5.83e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDR---RGMRVLAACLTEKGAEQLRNKTSDR----LETVILDVTKTESIVAATQWVKERVG 102
Cdd:cd09806   1 TVVLITGCSSGIGLHLAVRLASdpsKRFKVYATMRDLKKKGRLWEAAGALaggtLETLQLDVCDSKSVAAAVERVTERHV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  103 NRglwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCGGG-YCISKY 180
Cdd:cd09806  81 DV----LVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGsGRILVTSSVGGLQGLPFNDvYCASKF 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  181 GVEAFSDSLRREISYFGVKVAIIEPGGFRTNVSnyERLSHSIEKLWDQTSSEVKEVYDKN-FLDSYIKAIQSLTDTCSDd 259
Cdd:cd09806 157 ALEGLCESLAVQLLPFNVHLSLIECGPVHTAFM--EKVLGSPEEVLDRTADDITTFHFFYqYLAHSKQVFREAAQNPEE- 233

                       250       260
                ....*....|....*....|.
gi 8567342  260 lsvVTDCMEHALTACHPRTRY 280
Cdd:cd09806 234 ---VAEVFLTAIRAPKPPLRY 251
PRK07832 PRK07832
SDR family oxidoreductase;
30-210 1.97e-23

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 97.04  E-value: 1.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    30 KYVFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEQLRNKTSD---RLETVI----LDVTKTESIVAATQWVKERVG 102
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELF---LTDRDADGLAQTVADaraLGGTVPehraLDISDYDAVAAFAADIHAAHG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   103 NRGLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGR-VVNISSSMGRVSL-CGGGYCISK 179
Cdd:PRK07832  78 SMDV--VMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPpMVAAGRGGhLVNVSSAAGLVALpWHAAYSASK 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 8567342   180 YGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK07832 156 FGLRGLSEVLRFDLARHGIGVSVVVPGAVKT 186
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 30-223 6.86e-23

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: 94.35  E-value: 6.86e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRnKTSDRLETVILDVTKTESIVAATQWVKERVGnrGLWGL 109
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALS-ASGGDVEAVPYDARDPEDARALVDALRDRFG--RIDVL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  110 VNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCG-GGYCISKYGVEAFSD 187
Cdd:cd08932  78 VHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPaLREAGSGRVVFLNSLSGKRVLAGnAGYSASKFALRALAH 157

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 8567342  188 SLRREISYFGVKVAIIEPGGFRTNVSNYERLSHSIE 223
Cdd:cd08932 158 ALRQEGWDHGVRVSAVCPGFVDTPMAQGLTLVGAFP 193
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 27-210 1.22e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 96.14  E-value: 1.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG----AEQLRNKTSDRLeTVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK07109   6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGlealAAEIRAAGGEAL-AVVADVADAEAVQAAADRAEEELG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   103 NRGLWglVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSL-CGGGYCISKY 180
Cdd:PRK07109  85 PIDTW--VNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRhMRPRDRGAIIQVGSALAYRSIpLQSAYCAAKH 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 8567342   181 GVEAFSDSLRREISYFG--VKVAIIEPGGFRT 210
Cdd:PRK07109 163 AIRGFTDSLRCELLHDGspVSVTMVQPPAVNT 194
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 38-264 5.53e-22

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: 92.11  E-value: 5.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342     38 DSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRnKTSDRLETVIL--DVTKTESIVAATQWVKERVGnrGLWGLVNNAGI 115
Cdd:pfam13561   5 ESGIGWAIARALAEEGAEVVLTDLNEALAKRVE-ELAEELGAAVLpcDVTDEEQVEALVAAAVEKFG--RLDILVNNAGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    116 CVFAINEWLK--KEDFANILDVNLLGMIEVTLSMLPLvRKARGRVVNISSSMGRVSLCGGG-YCISKYGVEAFSDSLRRE 192
Cdd:pfam13561  82 APKLKGPFLDtsREDFDRALDVNLYSLFLLAKAALPL-MKEGGSIVNLSSIGAERVVPNYNaYGAAKAALEALTRYLAVE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    193 ISYFGVKVAIIEPGGFRT----NVSNYERLSHSIEKL----WDQTSSEVKEVYdkNFLdsyikaiqsltdtCSDDLSVVT 264
Cdd:pfam13561 161 LGPRGIRVNAISPGPIKTlaasGIPGFDELLAAAEARaplgRLGTPEEVANAA--AFL-------------ASDLASYIT 225
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 27-213 7.91e-22

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 92.70  E-value: 7.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV----LAACLTEKGAEQLrnktsDRLETVILDVTKTESIVAATQWVkervg 102
Cdd:PRK07825   3 LRGKVVAITGGARGIGLATARALAALGARVaigdLDEALAKETAAEL-----GLVVGGPLDVTDPASFAAFLDAV----- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   103 nRGLWG----LVNNAGicVFAINEWLKKEDFAN--ILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCGGG- 174
Cdd:PRK07825  73 -EADLGpidvLVNNAG--VMPVGPFLDEPDAVTrrILDVNVYGVILGSKLAAPrMVPRGRGHVVNVASLAGKIPVPGMAt 149

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 8567342   175 YCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVS 213
Cdd:PRK07825 150 YCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELI 188
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 27-205 1.83e-21

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: 90.83  E-value: 1.83e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDrLETVILDVTKTESIVAATQWVKERvgNRGL 106
Cdd:cd05370   3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN-IHTIVLDVGDAESVEALAEALLSE--YPNL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  107 WGLVNNAGICVfaiNEWLKK-----EDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCGGG-YCISK 179
Cdd:cd05370  80 DILINNAGIQR---PIDLRDpasdlDKADTEIDTNLIGPIRLIKAFLPhLKKQPEATIVNVSSGLAFVPMAANPvYCATK 156

                       170       180
                ....*....|....*....|....*.
gi 8567342  180 YGVEAFSDSLRREISYFGVKVAIIEP 205
Cdd:cd05370 157 AALHSYTLALRHQLKDTGVEVVEIVP 182
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 27-210 2.70e-21

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: 90.52  E-value: 2.70e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:cd05341   3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFG--RL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  107 WGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKA-RGRVVNISSSMGRVSLCG-GGYCISKYGVEA 184
Cdd:cd05341  81 DVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAgGGSIINMSSIEGLVGDPAlAAYNASKGAVRG 160

                       170       180
                ....*....|....*....|....*...
gi 8567342  185 FSDSLRREI--SYFGVKVAIIEPGGFRT 210
Cdd:cd05341 161 LTKSAALECatQGYGIRVNSVHPGYIYT 188
PRK07024 PRK07024
SDR family oxidoreductase;
32-210 7.76e-21

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 89.60  E-value: 7.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    32 VFITGCDSGFGNLLARQLDRRGMRV-LAACLTE---KGAEQLRNktSDRLETVILDVTKTESIVAATQWVKERVGNRGLw 107
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLgLVARRTDalqAFAARLPK--AARVSVYAADVRDADALAAAAADFIAAHGLPDV- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   108 gLVNNAGICVFAINEwlKKED---FANILDVNLLGMIEVTLSML-PLVRKARGRVVNISSSMGRVSLCGGG-YCISKYGV 182
Cdd:PRK07024  82 -VIANAGISVGTLTE--EREDlavFREVMDTNYFGMVATFQPFIaPMRAARRGTLVGIASVAGVRGLPGAGaYSASKAAA 158

                        170       180
                 ....*....|....*....|....*...
gi 8567342   183 EAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK07024 159 IKYLESLRVELRPAGVRVVTIAPGYIRT 186
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-210 1.17e-20

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 88.77  E-value: 1.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACL-TEKGAEQLRNK---TSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK12825   4 LMGRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEAveaLGRRAQAVQADVTDKAALEAAVAAAVERFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   103 nrGLWGLVNNAGicvfaINEW-----LKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSS------MGRVsl 170
Cdd:PRK12825  84 --RIDILVNNAG-----IFEDkpladMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRgGRIVNISSVaglpgwPGRS-- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 8567342   171 cggGYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK12825 155 ---NYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDT 191
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 32-226 1.86e-20

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


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 88.03  E-value: 1.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342     32 VFITGCDSGFGNLLARQLDRRGMRVLAACLT-EKGAEQLRNKTSD---RLETVILDVTKTESIVAATQWVKERVGnrGLW 107
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSsEEGAEEVVEELKAlgvKALGVVLDVSDREDVKAVVEEIEEELG--TID 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    108 GLVNNAGIC--VFAINewLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGrvsLCGGG----YCISKY 180
Cdd:TIGR01830  79 ILVNNAGITrdNLLMR--MKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRsGRIINISSVVG---LMGNAgqanYAASKA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 8567342    181 GVEAFSDSLRREISYFGVKVAIIEPGGFRTNVSnyERLSHSIEKLW 226
Cdd:TIGR01830 154 GVIGFTKSLAKELASRNITVNAVAPGFIDTDMT--DKLSEKVKKKI 197
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-211 1.87e-20

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 88.36  E-value: 1.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAC-LTEKGAEQLRNKTSDRLETVIL---DVTKTESIVAATQWVKERVG 102
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYdINEEAAQELLEEIKEEGGDAIAvkaDVSSEEDVENLVEQIVEKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   103 nrGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSL-CGGGYCISKY 180
Cdd:PRK05565  83 --KIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPyMIKRKSGVIVNISSIWGLIGAsCEVLYSASKG 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 8567342   181 GVEAFSDSLRREISYFGVKVAIIEPGGFRTN 211
Cdd:PRK05565 161 AVNAFTKALAKELAPSGIRVNAVAPGAIDTE 191
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 20-210 2.07e-20

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 88.58  E-value: 2.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    20 ERQVVSHLQDKYVFITGCDSGFGNLLARQLDRRGMRV--LAACLTEKGAEQLRNKTSDRLETViLDVTKTESIVAATQWV 97
Cdd:PRK12829   2 AIDLLKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVhvCDVSEAALAATAARLPGAKVTATV-ADVADPAQVERVFDTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    98 KERVGnrGLWGLVNNAGICV--FAINEwLKKEDFANILDVNLLGMIEVTLSMLPLVRKA-RGRVV-NISSSMGRVSLCGG 173
Cdd:PRK12829  81 VERFG--GLDVLVNNAGIAGptGGIDE-ITPEQWEQTLAVNLNGQFYFARAAVPLLKASgHGGVIiALSSVAGRLGYPGR 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 8567342   174 -GYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK12829 158 tPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRG 195
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 25-225 2.38e-20

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 88.30  E-value: 2.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    25 SHLQDKYVFITGCDSGFGNLLARQLDRRGMRVlaACL---TEKGAEQLRNKTSdrlETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK06463   3 MRFKGKVALITGGTRGIGRAIAEAFLREGAKV--AVLynsAENEAKELREKGV---FTIKCDVGNRDQVKKSKEVVEKEF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   102 GNRGLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCGGG--YCIS 178
Cdd:PRK06463  78 GRVDV--LVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKnGAIVNIASNAGIGTAAEGTtfYAIT 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 8567342   179 KYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVSNYERLSHSIEKL 225
Cdd:PRK06463 156 KAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLSGKSQEEAEKL 202
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-205 3.08e-20

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 87.44  E-value: 3.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSD---RLETVILDVTKTESIVAATQWVKERVGN 103
Cdd:PRK07666   5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAygvKVVIATADVSDYEEVTAAIEQLKNELGS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   104 RGLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMG-RVSLCGGGYCISKYG 181
Cdd:PRK07666  85 IDI--LINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPsMIERQSGDIINISSTAGqKGAAVTSAYSASKFG 162

                        170       180
                 ....*....|....*....|....
gi 8567342   182 VEAFSDSLRREISYFGVKVAIIEP 205
Cdd:PRK07666 163 VLGLTESLMQEVRKHNIRVTALTP 186
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 27-211 5.16e-20

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: 87.03  E-value: 5.16e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE---KGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGN 103
Cdd:cd05347   3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEekaEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  104 RGLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMgrvSLCGG----GYCIS 178
Cdd:cd05347  83 IDI--LVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARhMIKQGHGKIINICSLL---SELGGppvpAYAAS 157

                       170       180       190
                ....*....|....*....|....*....|...
gi 8567342  179 KYGVEAFSDSLRREISYFGVKVAIIEPGGFRTN 211
Cdd:cd05347 158 KGGVAGLTKALATEWARHGIQVNAIAPGYFATE 190
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 24-228 7.19e-20

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 86.95  E-value: 7.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    24 VSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSD---RLETVILDVTKTESIVAATQWVKER 100
Cdd:PRK12939   2 ASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAaggRAHAIAADLADPASVQRFFDAAAAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   101 VGnrGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVR-KARGRVVNISSSMGRVSLCGGG-YCIS 178
Cdd:PRK12939  82 LG--GLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRdSGRGRIVNLASDTALWGAPKLGaYVAS 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 8567342   179 KYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVSNYERLSHSIEKLWDQ 228
Cdd:PRK12939 160 KGAVIGMTRSLARELGGRGITVNAIAPGLTATEATAYVPADERHAYYLKG 209
PRK06181 PRK06181
SDR family oxidoreductase;
29-212 1.08e-19

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 86.57  E-value: 1.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG----AEQLRNKTSDRLeTVILDVTKTESIVAATQWVKERVGnr 104
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRlaslAQELADHGGEAL-VVPTDVSDAEACERLIEAAVARFG-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   105 GLWGLVNNAGICVFA-INEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISSSMGRVSLCG-GGYCISKYGV 182
Cdd:PRK06181  78 GIDILVNNAGITMWSrFDELTDLSVFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTrSGYAASKHAL 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 8567342   183 EAFSDSLRREISYFGVKVAIIEPGGFRTNV 212
Cdd:PRK06181 158 HGFFDSLRIELADDGVAVTVVCPGFVATDI 187
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 27-204 2.37e-19

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


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 85.21  E-value: 2.37e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAcltekG--AEQLRNKTSDR--LETVILDVTKTESIVAATQWVKERVG 102
Cdd:COG3967   3 LTGNTILITGGTSGIGLALAKRLHARGNTVIIT-----GrrEEKLEEAAAANpgLHTIVLDVADPASIAALAEQVTAEFP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  103 nrGLWGLVNNAGIcVFAINeWLK-KEDFANI---LDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCG-GGYC 176
Cdd:COG3967  78 --DLNVLINNAGI-MRAED-LLDeAEDLADAereITTNLLGPIRLTAAFLPhLKAQPEAAIVNVSSGLAFVPLAVtPTYS 153

                       170       180
                ....*....|....*....|....*...
gi 8567342  177 ISKYGVEAFSDSLRREISYFGVKVaiIE 204
Cdd:COG3967 154 ATKAALHSYTQSLRHQLKDTSVKV--IE 179
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
27-210 8.30e-19

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 84.08  E-value: 8.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLT---EKGAEQLRNKTSdRLETVILDVTKTESIVAATQWVKERVGN 103
Cdd:PRK08226   4 LTGKTALITGALQGIGEGIARVFARHGANLILLDISpeiEKLADELCGRGH-RCTAVVADVRDPASVAAAIKRAKEKEGR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   104 RGLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCGG--GYCISKY 180
Cdd:PRK08226  83 IDI--LVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPeMIARKDGRIVMMSSVTGDMVADPGetAYALTKA 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 8567342   181 GVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK08226 161 AIVGLTKSLAVEYAQSGIRVNAICPGYVRT 190
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 29-216 8.32e-19

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: 84.20  E-value: 8.32e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNK-----TSDRLETVILDVTKTESIVAATQWVKERVgn 103
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEikketGNAKVEVIQLDLSSLASVRQFAEEFLARF-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  104 RGLWGLVNNAGIcvFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVS------LCGGG-- 174
Cdd:cd05327  79 PRLDILINNAGI--MAPPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASApSRIVNVSSIAHRAGpidfndLDLENnk 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 8567342  175 -------YCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVSNYE 216
Cdd:cd05327 157 eyspykaYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRN 205
PRK06484 PRK06484
short chain dehydrogenase; Validated
 32-210 1.75e-18

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 85.67  E-value: 1.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLwgLVN 111
Cdd:PRK06484 272 VAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRLDV--LVN 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   112 NAGIC-VFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKArGRVVNISSSMGRVSLCG-GGYCISKYGVEAFSDSL 189
Cdd:PRK06484 350 NAGIAeVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG-GVIVNLGSIASLLALPPrNAYCASKAAVTMLSRSL 428

                        170       180
                 ....*....|....*....|.
gi 8567342   190 RREISYFGVKVAIIEPGGFRT 210
Cdd:PRK06484 429 ACEWAPAGIRVNTVAPGYIET 449
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 30-210 1.78e-18

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


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 82.50  E-value: 1.78e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKT-SDRLETVILDVTKTESIVAATQWVKERVGNRgLWG 108
Cdd:cd08931   1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELgAENVVAGALDVTDRAAWAAALADFAAATGGR-LDA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  109 LVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKARG-RVVNISSSMGRVSLCG-GGYCISKYGVEAFS 186
Cdd:cd08931  80 LFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGaRVINTASSSAIYGQPDlAVYSATKFAVRGLT 159

                       170       180
                ....*....|....*....|....
gi 8567342  187 DSLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd08931 160 EALDVEWARHGIRVADVWPWFVDT 183
PRK08264 PRK08264
SDR family oxidoreductase;
26-206 3.13e-18

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 81.86  E-value: 3.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    26 HLQDKYVFITGCDSGFGNLLARQLDRRG-MRVLAACltekgaeqlRNKTS-----DRLETVILDVTKTESIVAATqwvkE 99
Cdd:PRK08264   3 DIKGKVVLVTGANRGIGRAFVEQLLARGaAKVYAAA---------RDPESvtdlgPRVVPLQLDVTDPASVAAAA----E 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   100 RVGNRGLwgLVNNAGIcvFAINEWLKKEDFANI---LDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLC-GGG 174
Cdd:PRK08264  70 AASDVTI--LVNNAGI--FRTGSLLLEGDEDALraeMETNYFGPLAMARAFAPvLAANGGGAIVNVLSVLSWVNFPnLGT 145

                        170       180       190
                 ....*....|....*....|....*....|..
gi 8567342   175 YCISKYGVEAFSDSLRREISYFGVKVAIIEPG 206
Cdd:PRK08264 146 YSASKAAAWSLTQALRAELAPQGTRVLGVHPG 177
PRK08219 PRK08219
SDR family oxidoreductase;
34-211 4.11e-18

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 81.52  E-value: 4.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    34 ITGCDSGFGNLLARQLDRRgMRVLAACLTEKGAEQLRNkTSDRLETVILDVTKTESIVAATQWVkERVGNrglwgLVNNA 113
Cdd:PRK08219   8 ITGASRGIGAAIARELAPT-HTLLLGGRPAERLDELAA-ELPGATPFPVDLTDPEAIAAAVEQL-GRLDV-----LVHNA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   114 GICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISSSMGRVSLCGGG-YCISKYGVEAFSDSLRRE 192
Cdd:PRK08219  80 GVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRANPGWGsYAASKFALRALADALREE 159

                        170
                 ....*....|....*....
gi 8567342   193 iSYFGVKVAIIEPGgfRTN 211
Cdd:PRK08219 160 -EPGNVRVTSVHPG--RTD 175
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 30-212 8.42e-18

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


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 80.81  E-value: 8.42e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEK--GAEQL-RNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENpgAAAELqAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFG--RV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  107 WGLVNNAGIC--VFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR----GRVVNISSSMG-----RVSLcgggY 175
Cdd:cd05323  79 DILINNAGILdeKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKggkgGVIVNIGSVAGlypapQFPV----Y 154

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 8567342  176 CISKYGVEAFSDSLRREISY-FGVKVAIIEPGGFRTNV 212
Cdd:cd05323 155 SASKHGVVGFTRSLADLLEYkTGVRVNAICPGFTNTPL 192
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 32-206 1.03e-17

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 80.96  E-value: 1.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLwgLVN 111
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDV--LVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   112 NAGICVFAinEWLKK---EDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCGGG-YCISKYGVEAFS 186
Cdd:PRK10538  81 NAGLALGL--EPAHKasvEDWETMIDTNNKGLVYMTRAVLPgMVERNHGHIINIGSTAGSWPYAGGNvYGATKAFVRQFS 158

                        170       180
                 ....*....|....*....|
gi 8567342   187 DSLRREISYFGVKVAIIEPG 206
Cdd:PRK10538 159 LNLRTDLHGTAVRVTDIEPG 178
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 27-214 1.19e-17

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: 80.92  E-value: 1.19e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVlaaCLTEKGAEQL---------RNKTSDRLETVILDVTKTESIVAATQWV 97
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTAILFARLGARL---ALTGRDAERLeetrqsclqAGVSEKKILLVVADLTEEEGQDRIISTT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   98 KERVGNRGLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISSSMGRVSLCGG-GYC 176
Cdd:cd05364  78 LAKFGRLDI--LVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGRSFPGVlYYC 155

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 8567342  177 ISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVSN 214
Cdd:cd05364 156 ISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHR 193
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 29-219 1.71e-17

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: 79.95  E-value: 1.71e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE----KGAEQLRNKTSDRLETVILDVTKTESIVAAtqwVKERVGNR 104
Cdd:cd05356   1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQekldAVAKEIEEKYGVETKTIAADFSAGDDIYER---IEKELEGL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  105 GLWGLVNNAGICVFAINEWLKKED--FANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRV-SLCGGGYCISKY 180
Cdd:cd05356  78 DIGILVNNVGISHSIPEYFLETPEdeLQDIINVNVMATLKMTRLILPgMVKRKKGAIVNISSFAGLIpTPLLATYSASKA 157

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 8567342  181 GVEAFSDSLRREISYFGVKVAIIEPGGFRTNVSNYERLS 219
Cdd:cd05356 158 FLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSKIRKSS 196
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 27-206 2.20e-17

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 79.96  E-value: 2.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV-LAACLTEKgAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrG 105
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVgLHGTRVEK-LEALAAELGERVKIFPANLSDRDEVKALGQKAEADLE--G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   106 LWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSML-PLVRKARGRVVNISSSMGRVSLCG-GGYCISKYGVE 183
Cdd:PRK12936  81 VDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELThPMMRRRYGRIINITSVVGVTGNPGqANYCASKAGMI 160

                        170       180
                 ....*....|....*....|...
gi 8567342   184 AFSDSLRREISYFGVKVAIIEPG 206
Cdd:PRK12936 161 GFSKSLAQEIATRNVTVNCVAPG 183
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
27-206 4.40e-17

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 79.30  E-value: 4.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFG--GI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   107 WGLVNNAGICVFA-INEwLKKEDFANILDVNLLGMI----EVTLSMLPlvRKARGRVVNISSSMGR-----VSLcgggYC 176
Cdd:PRK07067  82 DILFNNAALFDMApILD-ISRDSYDRLFAVNVKGLFflmqAVARHMVE--QGRGGKIINMASQAGRrgealVSH----YC 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 8567342   177 ISKYGVEAFSDSLRREISYFGVKVAIIEPG 206
Cdd:PRK07067 155 ATKAAVISYTQSAALALIRHGINVNAIAPG 184
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 27-205 6.86e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 78.55  E-value: 6.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGL 106
Cdd:PRK06841  13 LSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRIDI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   107 wgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCGG-GYCISKYGVEA 184
Cdd:PRK06841  93 --LVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRhMIAAGGGKIVNLASQAGVVALERHvAYCASKAGVVG 170

                        170       180
                 ....*....|....*....|.
gi 8567342   185 FSDSLRREISYFGVKVAIIEP 205
Cdd:PRK06841 171 MTKVLALEWGPYGITVNAISP 191
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 26-210 8.27e-17

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 78.30  E-value: 8.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEQLRNKTSDRLETVI----LDVTKTESIVAATQWVKERV 101
Cdd:PRK12828   4 SLQGKVVAITGGFGGLGRATAAWLAARGARVA---LIGRGAAPLSQTLPGVPADALriggIDLVDPQAARRAVDEVNRQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   102 GnrGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCG-GGYCISK 179
Cdd:PRK12828  81 G--RLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPaLTASGGGRIVNIGAGAALKAGPGmGAYAAAK 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 8567342   180 YGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK12828 159 AGVARLTEALAAELLDRGITVNAVLPSIIDT 189
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 24-212 2.34e-16

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 76.97  E-value: 2.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    24 VSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEK-GAEQLRNKTSDRLETVIL---DVTKTESivaATQWVKE 99
Cdd:PRK12935   1 MVQLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKeAAENLVNELGKEGHDVYAvqaDVSKVED---ANRLVEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   100 RVGNRG-LWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCG-GGYC 176
Cdd:PRK12935  78 AVNHFGkVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEeGRIISISSIIGQAGGFGqTNYS 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 8567342   177 ISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNV 212
Cdd:PRK12935 158 AAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEM 193
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
27-212 5.05e-16

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 76.20  E-value: 5.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAC-----LTEKGAEQLRNKTSDRLETViLDVTKTESIVAATQWVKERV 101
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAGCgpnspRRVKWLEDQKALGFDFIASE-GNVGDWDSTKAAFDKVKAEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   102 GNRGLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCG-GGYCISK 179
Cdd:PRK12938  80 GEIDV--LVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDgMVERGWGRIINISSVNGQKGQFGqTNYSTAK 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 8567342   180 YGVEAFSDSLRREISYFGVKVAIIEPGGFRTNV 212
Cdd:PRK12938 158 AGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDM 190
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 32-215 5.94e-16

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: 75.83  E-value: 5.94e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSD---RLETVILDVTKTESIVAATQWVKERVGnrGLWG 108
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNpnpSVEVEILDVTDEERNQLVIAELEAELG--GLDL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  109 LVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCGG-GYCISKYGVEAFS 186
Cdd:cd05350  79 VIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPqFRAKGRGHLVLISSVAALRGLPGAaAYSASKAALSSLA 158

                       170       180
                ....*....|....*....|....*....
gi 8567342  187 DSLRREISYFGVKVAIIEPGGFRTNVSNY 215
Cdd:cd05350 159 ESLRYDVKKRGIRVTVINPGFIDTPLTAN 187
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 27-206 5.97e-16

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 76.15  E-value: 5.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE----KGAEQLRNkTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAerldEVAAEIDD-LGRRALAVPTDITDEDQCANLVALALERFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   103 nrGLWGLVNNAgicvFAINEW--LKKEDFANI---LDVNLLGMIEVTLSMLPLVRKARGRVVNISSSMGRVSLCG-GGYC 176
Cdd:PRK07890  82 --RVDALVNNA----FRVPSMkpLADADFAHWravIELNVLGTLRLTQAFTPALAESGGSIVMINSMVLRHSQPKyGAYK 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 8567342   177 ISKYGVEAFSDSLRREISYFGVKVAIIEPG 206
Cdd:PRK07890 156 MAKGALLAASQSLATELGPQGIRVNSVAPG 185
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 27-210 7.88e-16

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


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 75.57  E-value: 7.88e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVI-LDVTKTESIVAATQWVKERVGNrg 105
Cdd:cd05326   2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFVhCDVTVEADVRAAVDTAVARFGR-- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  106 LWGLVNNAGIC---VFAINEWlKKEDFANILDVNL----LGMIEVTLSMLPlvrKARGRVVNISSSMGRVSlcGGG---Y 175
Cdd:cd05326  80 LDIMFNNAGVLgapCYSILET-SLEEFERVLDVNVygafLGTKHAARVMIP---AKKGSIVSVASVAGVVG--GLGphaY 153

                       170       180       190
                ....*....|....*....|....*....|....*
gi 8567342  176 CISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd05326 154 TASKHAVLGLTRSAATELGEHGIRVNCVSPYGVAT 188
PRK07063 PRK07063
SDR family oxidoreductase;
27-206 8.52e-16

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 75.86  E-value: 8.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV----LAACLTEKGAEQLRNKTSD-RLETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK07063   5 LAGKVALVTGAAQGIGAAIARAFAREGAAValadLDAALAERAAAAIARDVAGaRVLAVPADVTDAASVAAAVAAAEEAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   102 GnrGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCGG-GYCISK 179
Cdd:PRK07063  85 G--PLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPgMVERGRGSIVNIASTHAFKIIPGCfPYPVAK 162

                        170       180
                 ....*....|....*....|....*..
gi 8567342   180 YGVEAFSDSLRREISYFGVKVAIIEPG 206
Cdd:PRK07063 163 HGLLGLTRALGIEYAARNVRVNAIAPG 189
FabG-like PRK07231
SDR family oxidoreductase;
27-210 8.90e-16

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 75.25  E-value: 8.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG----AEQLRnkTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAaervAAEIL--AGGRAIAVAADVSDEADVEAAVAAALERFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   103 nrGLWGLVNNAGIcvFAINEWLKK---EDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMG-RVSLCGGGYCI 177
Cdd:PRK07231  81 --SVDILVNNAGT--THRNGPLLDvdeAEFDRIFAVNVKSPYLWTQAAVPAMRGEGgGAIVNVASTAGlRPRPGLGWYNA 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 8567342   178 SKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK07231 157 SKGAVITLTKALAAELGPDKIRVNAVAPVVVET 189
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 30-210 1.00e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 75.14  E-value: 1.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDrlETVILDVTKTESIVAAtqwvkerVGNRGLW-G 108
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGC--EPLRLDVGDDAAIRAA-------LAAAGAFdG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   109 LVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKAR-GRVVNISSSMGRVS----LCgggYCISKYGV 182
Cdd:PRK07060  81 LVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARaMIAAGRgGSIVNVSSQAALVGlpdhLA---YCASKAAL 157

                        170       180
                 ....*....|....*....|....*...
gi 8567342   183 EAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK07060 158 DAITRVLCVELGPHGIRVNSVNPTVTLT 185
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 27-210 1.30e-15

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 74.92  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQ---LRNKTSDRLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAaaeALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   104 rGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCG-GGYCISKYG 181
Cdd:PRK12429  81 -GVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGgGRIINMASVHGLVGSAGkAAYVSAKHG 159

                        170       180
                 ....*....|....*....|....*....
gi 8567342   182 VEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK12429 160 LIGLTKVVALEGATHGVTVNAICPGYVDT 188
PRK08589 PRK08589
SDR family oxidoreductase;
27-210 1.81e-15

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 74.81  E-value: 1.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLR--NKTSDRLETVILDVTKTESIVAATQWVKERVGNR 104
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDkiKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   105 GLwgLVNNAGICVFA--INEWlKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISSSMGRVS-LCGGGYCISKYG 181
Cdd:PRK08589  84 DV--LFNNAGVDNAAgrIHEY-PVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAAdLYRSGYNAAKGA 160

                        170       180
                 ....*....|....*....|....*....
gi 8567342   182 VEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK08589 161 VINFTKSIAIEYGRDGIRANAIAPGTIET 189
PRK07454 PRK07454
SDR family oxidoreductase;
32-230 3.38e-15

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 73.45  E-value: 3.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    32 VFITGCDSGFGNLLARQLDRRGMRVL----AACLTEKGAEQLRNKTSdRLETVILDVTKTESIVAATQWVKERVGNRGLw 107
Cdd:PRK07454   9 ALITGASSGIGKATALAFAKAGWDLAlvarSQDALEALAAELRSTGV-KAAAYSIDLSNPEAIAPGIAELLEQFGCPDV- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   108 gLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCG-GGYCISKYGVEAF 185
Cdd:PRK07454  87 -LINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGgGLIINVSSIAARNAFPQwGAYCVSKAALAAF 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 8567342   186 SDSLRREISYFGVKVAIIEPGGFRTnvsnyerlshsieKLWDQTS 230
Cdd:PRK07454 166 TKCLAEEERSHGIRVCTITLGAVNT-------------PLWDTET 197
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 32-210 4.59e-15

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: 73.27  E-value: 4.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   32 VFITGCDSGFGNLLARQLDRRGMRVLAACLtekgAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGLWGLVN 111
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVIALDL----PFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHG--PIDALVN 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  112 NAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMG---RVSLcgGGYCISKYGVEAFSD 187
Cdd:cd05331  75 CAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRtGAIVTVASNAAhvpRISM--AAYGASKAALASLSK 152

                       170       180
                ....*....|....*....|...
gi 8567342  188 SLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd05331 153 CLGLELAPYGVRCNVVSPGSTDT 175
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 26-210 5.18e-15

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 73.46  E-value: 5.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRvLAacLTEKGAEQLRNKTSD------RLETVILDVTKTESIVAATQWVKE 99
Cdd:PRK08217   2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAK-LA--LIDLNQEKLEEAVAEcgalgtEVRGYAANVTDEEDVEATFAQIAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   100 RVGnrGLWGLVNNAGIC-----VFA----INEWLKKEDFANILDVNLLGMI----EVTLSMLPLVRKarGRVVNISS--- 163
Cdd:PRK08217  79 DFG--QLNGLINNAGILrdgllVKAkdgkVTSKMSLEQFQSVIDVNLTGVFlcgrEAAAKMIESGSK--GVIINISSiar 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 8567342   164 --SMGRVSlcgggYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK08217 155 agNMGQTN-----YSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIET 198
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 27-216 6.06e-15

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 73.51  E-value: 6.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQlrnktsDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQH------ENYQFVPTDVSSAEEVNHTVAEIIEKFG--RI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   107 WGLVNNAGICV-------------FAINEwlkkEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMG-RVSLC 171
Cdd:PRK06171  79 DGLVNNAGINIprllvdekdpagkYELNE----AAFDKMFNINQKGVFLMSQAVARqMVKQHDGVIVNMSSEAGlEGSEG 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 8567342   172 GGGYCISKYGVEAFSDSLRREISYFGVKV-----AIIEPGGFRTnvSNYE 216
Cdd:PRK06171 155 QSCYAATKAALNSFTRSWAKELGKHNIRVvgvapGILEATGLRT--PEYE 202
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 33-235 8.34e-15

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: 72.96  E-value: 8.34e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   33 FITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEQLRnKTSDRLETVIL-------DVTKTESIVAATQWVKERVGNRG 105
Cdd:cd08945   7 LVTGATSGIGLAIARRLGKEGLRVF---VCARGEEGLA-TTVKELREAGVeadgrtcDVRSVPEIEALVAAAVARYGPID 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  106 LwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP---LVRKARGRVVNISSSMGRVSLCGGG-YCISKYG 181
Cdd:cd08945  83 V--LVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKaggMLERGTGRIINIASTGGKQGVVHAApYSASKHG 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 8567342  182 VEAFSDSLRREISYFGVKVAIIEPGGFRTNVSnyERLSHSIEKLWDQTSSEVKE 235
Cdd:cd08945 161 VVGFTKALGLELARTGITVNAVCPGFVETPMA--ASVREHYADIWEVSTEEAFD 212
PRK08267 PRK08267
SDR family oxidoreductase;
30-309 8.46e-15

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 72.66  E-value: 8.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNK-TSDRLETVILDVTKTESIVAATQWVKERVGNRgLWG 108
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAElGAGNAWTGALDVTDRAAWDAALADFAAATGGR-LDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   109 LVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKARG-RVVNISSS-----MGRVSLcgggYCISKYGV 182
Cdd:PRK08267  81 LFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGaRVINTSSAsaiygQPGLAV----YSATKFAV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   183 EAFSDSLRREISYFGVKVAIIEPGGFRTnvsnyerlshsieKLWDQTSSEVKevydknfldsyIKAIQSL--TDTCSDDL 260
Cdd:PRK08267 157 RGLTEALDLEWRRHGIRVADVMPLFVDT-------------AMLDGTSNEVD-----------AGSTKRLgvRLTPEDVA 212

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 8567342   261 SVVTDCMEHAltachPRTRYSAGWDAKLFYLPLSYMPTFLVDAMLYWSS 309
Cdd:PRK08267 213 EAVWAAVQHP-----TRLHWPVGKQAKLLAFLARLSPGFVRRLINKSLA 256
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 27-210 8.93e-15

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: 72.80  E-value: 8.93e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEK-GAEQL-RNKTSDRLETVIL--DVTKTESIVAATQWVKERVG 102
Cdd:cd05358   1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEdAAEEVvEEIKAVGGKAIAVqaDVSKEEDVVALFQSAIKEFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  103 NRGLWglVNNAGI-CVFAINEwLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR--GRVVNISSSMGRVSLCG-GGYCIS 178
Cdd:cd05358  81 TLDIL--VNNAGLqGDASSHE-MTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKikGKIINMSSVHEKIPWPGhVNYAAS 157

                       170       180       190
                ....*....|....*....|....*....|..
gi 8567342  179 KYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd05358 158 KGGVKMMTKTLAQEYAPKGIRVNAIAPGAINT 189
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 31-206 1.07e-14

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: 72.32  E-value: 1.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   31 YVFITGCDSGFGNLLARQLDRRGMRVLAACLTE------KGAEQLRNktSDRLETVILDVTKT---ESIVAATQWV-KER 100
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARseeplqELKEELRP--GLRVTTVKADLSDAagvEQLLEAIRKLdGER 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  101 VgnrglwGLVNNAG-------ICVFAINEWlkKEDFanilDVNLLGMIEVTLSMLPLVRKAR--GRVVNISSSMGRVSLC 171
Cdd:cd05367  79 D------LLINNAGslgpvskIEFIDLDEL--QKYF----DLNLTSPVCLTSTLLRAFKKRGlkKTVVNVSSGAAVNPFK 146

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 8567342  172 G-GGYCISKYGVEAFSDSLRREisYFGVKVAIIEPG 206
Cdd:cd05367 147 GwGLYCSSKAARDMFFRVLAAE--EPDVRVLSYAPG 180
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 23-210 1.71e-14

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 72.24  E-value: 1.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    23 VVSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAE---QLRNKTSDRLETVILDVTKTESIVAATQWVKE 99
Cdd:PRK13394   1 MMSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANavaDEINKAGGKAIGVAMDVTNEDAVNAGIDKVAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   100 RVGNRGLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR--GRVVNISSSMGRVSLCG-GGYC 176
Cdd:PRK13394  81 RFGSVDI--LVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHSHEASPLkSAYV 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 8567342   177 ISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK13394 159 TAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRT 192
PRK09242 PRK09242
SDR family oxidoreductase;
27-224 2.72e-14

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 71.32  E-value: 2.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSD-----RLETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK09242   7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEefperEVHGLAADVSDDEDRRAILDWVEDHW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   102 GnrGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRK-ARGRVVNISSSMGRVSL-CGGGYCISK 179
Cdd:PRK09242  87 D--GLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQhASSAIVNIGSVSGLTHVrSGAPYGMTK 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 8567342   180 YGVEAFSDSLRREISYFGVKVAIIEPGGFRTN-----VSNYERLSHSIEK 224
Cdd:PRK09242 165 AALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPltsgpLSDPDYYEQVIER 214
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 34-210 3.57e-14

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 70.78  E-value: 3.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   34 ITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRnKTSDRLETVILDVTKTESIVAATQWVKERVGNrgLWGLVNNA 113
Cdd:cd05371   7 VTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVA-KLGDNCRFVPVDVTSEKDVKAALALAKAKFGR--LDIVVNCA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  114 GICVFAINEWLKK------EDFANILDVNLLGmievTLSMLPLVRKA-----------RGRVVNISSSMGRVSLCG-GGY 175
Cdd:cd05371  84 GIAVAAKTYNKKGqqphslELFQRVINVNLIG----TFNVIRLAAGAmgknepdqggeRGVIINTASVAAFEGQIGqAAY 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 8567342  176 CISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd05371 160 SASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDT 194
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 30-215 3.79e-14

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


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 71.34  E-value: 3.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACL----TEKGAEQLRNKTSDRLETVI-LDVTKTESIVA-ATQWVKERvgn 103
Cdd:cd09807   2 KTVIITGANTGIGKETARELARRGARVIMACRdmakCEEAAAEIRRDTLNHEVIVRhLDLASLKSIRAfAAEFLAEE--- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  104 RGLWGLVNNAGicVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRK-ARGRVVNISS---SMGRVSL--------- 170
Cdd:cd09807  79 DRLDVLINNAG--VMRCPYSKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKsAPSRIVNVSSlahKAGKINFddlnseksy 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 8567342  171 -CGGGYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVSNY 215
Cdd:cd09807 157 nTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELGRH 202
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 27-210 4.14e-14

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


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 71.01  E-value: 4.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSD-----RLETVILDVTKTESIVAATQWVKERV 101
Cdd:cd05330   1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEiapdaEVLLIKADVSDEAQVEAYVDATVEQF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  102 GNrgLWGLVNNAGI-CVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMG-RVSLCGGGYCIS 178
Cdd:cd05330  81 GR--IDGFFNNAGIeGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGsGMIVNTASVGGiRGVGNQSGYAAA 158

                       170       180       190
                ....*....|....*....|....*....|..
gi 8567342  179 KYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd05330 159 KHGVVGLTRNSAVEYGQYGIRINAIAPGAILT 190
PRK06114 PRK06114
SDR family oxidoreductase;
27-229 4.57e-14

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 70.58  E-value: 4.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVlaACLTEKGAEQLRnKTSDRLET-------VILDVTKTESIVAATQWVKE 99
Cdd:PRK06114   6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADV--ALFDLRTDDGLA-ETAEHIEAagrraiqIAADVTSKADLRAAVARTEA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   100 RVGNRGLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGmieVTLS-------MLPlvrKARGRVVNISSSMGRVS--- 169
Cdd:PRK06114  83 ELGALTL--AVNAAGIANANPAEEMEEEQWQTVMDINLTG---VFLScqaearaMLE---NGGGSIVNIASMSGIIVnrg 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   170 LCGGGYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVSNYERLSHSIEKLWDQT 229
Cdd:PRK06114 155 LLQAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTRPEMVHQTKLFEEQT 214
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 34-218 5.97e-14

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 70.76  E-value: 5.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    34 ITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQ----LRNKTSDrLETVILDVTKTESIVAATQWVKERVGNRGLwgL 109
Cdd:PRK05876  11 ITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQavnhLRAEGFD-VHGVMCDVRHREEVTHLADEAFRLLGHVDV--V 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   110 VNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP--LVRKARGRVVNISSSMGRVSLCG-GGYCISKYGVEAFS 186
Cdd:PRK05876  88 FSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPrlLEQGTGGHVVFTASFAGLVPNAGlGAYGVAKYGVVGLA 167

                        170       180       190
                 ....*....|....*....|....*....|...
gi 8567342   187 DSLRREISYFGVKVAIIEPGGFRTN-VSNYERL 218
Cdd:PRK05876 168 ETLAREVTADGIGVSVLCPMVVETNlVANSERI 200
PRK07774 PRK07774
SDR family oxidoreductase;
27-206 7.82e-14

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 69.77  E-value: 7.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVI---LDVTKTESIVAATQWVKERVGn 103
Cdd:PRK07774   4 FDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIavqVDVSDPDSAKAMADATVSAFG- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   104 rGLWGLVNNAGICV-----FAIN-EWlkkEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGrvSLCGGGYC 176
Cdd:PRK07774  83 -GIDYLVNNAAIYGgmkldLLITvPW---DYYKKFMSVNLDGALVCTRAVYKHMAKRGgGAIVNQSSTAA--WLYSNFYG 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 8567342   177 ISKYGVEAFSDSLRREISYFGVKVAIIEPG 206
Cdd:PRK07774 157 LAKVGLNGLTQQLARELGGMNIRVNAIAPG 186
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 27-210 8.42e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 69.78  E-value: 8.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSD---RLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQegiKAHAAPFNVTHKQEVEAAIEHIEKDIG- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   104 rGLWGLVNNAGI------CVFAINEWlkkedfANILDVNLLGMIEVTLSMLP-LVRKARGRVVNI---SSSMGRVSLCgg 173
Cdd:PRK08085  86 -PIDVLINNAGIqrrhpfTEFPEQEW------NDVIAVNQTAVFLVSQAVARyMVKRQAGKIINIcsmQSELGRDTIT-- 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 8567342   174 GYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK08085 157 PYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKT 193
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 27-210 8.53e-14

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: 69.61  E-value: 8.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEK-GAEQLR---NKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:cd05362   1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNYASSKaAAEEVVaeiEAAGGKAIAVQADVSDPSQVARLFDAAEKAFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  103 nrGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRkARGRVVNISSSMGRVSLCG-GGYCISKYG 181
Cdd:cd05362  81 --GVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLR-DGGRIINISSSLTAAYTPNyGAYAGSKAA 157

                       170       180
                ....*....|....*....|....*....
gi 8567342  182 VEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd05362 158 VEAFTRVLAKELGGRGITVNAVAPGPVDT 186
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 29-239 1.55e-13

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 69.29  E-value: 1.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTS-----DRLETVILDVTKTESIVAATQWVKERVGN 103
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINaeygeGMAYGFGADATSEQSVLALSRGVDEIFGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   104 RGLwgLVNNAGICVFA-INEwLKKEDFANILDVNLLGMI----EVTLSMLPlvRKARGRVVNISSSMGRV-SLCGGGYCI 177
Cdd:PRK12384  82 VDL--LVYNAGIAKAAfITD-FQLGDFDRSLQVNLVGYFlcarEFSRLMIR--DGIQGRIIQINSKSGKVgSKHNSGYSA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   178 SKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTnvsnyerlSHSIEKLWDQ-------TSSEVKEVY-DK 239
Cdd:PRK12384 157 AKFGGVGLTQSLALDLAEYGITVHSLMLGNLLK--------SPMFQSLLPQyakklgiKPDEVEQYYiDK 218
PRK05855 PRK05855
SDR family oxidoreductase;
29-212 1.82e-13

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 70.78  E-value: 1.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQlrnkTSDRLE-------TVILDVTKTESIVAATQWVKERV 101
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAER----TAELIRaagavahAYRVDVSDADAMEAFAEWVRAEH 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   102 GNRGLwgLVNNAGICV---FainewLK--KEDFANILDVNLLG-----------MIEvtlsmlplvRKARGRVVNISS-- 163
Cdd:PRK05855 391 GVPDI--VVNNAGIGMaggF-----LDtsAEDWDRVLDVNLWGvihgcrlfgrqMVE---------RGTGGHIVNVASaa 454

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 8567342   164 ------SMGrvslcggGYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNV 212
Cdd:PRK05855 455 ayapsrSLP-------AYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNI 502
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 27-210 1.86e-13

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 68.76  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEqlrnktSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQE------DYPFATFVLDVSDAAAVAQVCQRLLAETG--PL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   107 WGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCG-GGYCISKYGVEA 184
Cdd:PRK08220  78 DVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPqFRRQRSGAIVTVGSNAAHVPRIGmAAYGASKAALTS 157

                        170       180
                 ....*....|....*....|....*.
gi 8567342   185 FSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK08220 158 LAKCVGLELAPYGVRCNVVSPGSTDT 183
PRK06484 PRK06484
short chain dehydrogenase; Validated
 28-212 2.06e-13

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 70.65  E-value: 2.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLw 107
Cdd:PRK06484   4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDV- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   108 gLVNNAGICVFAINEWLKK--EDFANILDVNLLGMIEVTLSMLPLVRKAR--GRVVNISSSMGRVSLCG-GGYCISKYGV 182
Cdd:PRK06484  83 -LVNNAGVTDPTMTATLDTtlEEFARLQAINLTGAYLVAREALRLMIEQGhgAAIVNVASGAGLVALPKrTAYSASKAAV 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 8567342   183 EAFSDSLRREISYFGVKVAIIEPGGFRTNV 212
Cdd:PRK06484 162 ISLTRSLACEWAAKGIRVNAVLPGYVRTQM 191
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 27-206 2.39e-13

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: 68.69  E-value: 2.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAC----LTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:cd05343   4 WRGRVALVTGASVGIGAAVARALVQHGMKVVGCArrvdKIEALAAECQSAGYPTLFPYQCDLSNEEQILSMFSAIRTQHQ 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  103 nrGLWGLVNNAGIcvfAINEWL---KKEDFANILDVNLLGMIEVT---LSMLPLVRKARGRVVNISSSMGRVSLCG---G 173
Cdd:cd05343  84 --GVDVCINNAGL---ARPEPLlsgKTEGWKEMFDVNVLALSICTreaYQSMKERNVDDGHIININSMSGHRVPPVsvfH 158

                       170       180       190
                ....*....|....*....|....*....|....*
gi 8567342  174 GYCISKYGVEAFSDSLRREISYF--GVKVAIIEPG 206
Cdd:cd05343 159 FYAATKHAVTALTEGLRQELREAktHIRATSISPG 193
PRK08628 PRK08628
SDR family oxidoreductase;
26-203 5.42e-13

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 67.68  E-value: 5.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    26 HLQDKYVFITGCDSGFGNLLARQLDRRG-MRVLAACLTEKG--AEQLRNKTSdRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK08628   4 NLKDKVVIVTGGASGIGAAISLRLAEEGaIPVIFGRSAPDDefAEELRALQP-RAEFVQVDLTDDAQCRDAVEQTVAKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   103 nrGLWGLVNNAGIcvfaiNEWL----KKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISSsmgRVSLCG----GG 174
Cdd:PRK08628  83 --RIDGLVNNAGV-----NDGVgleaGREAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISS---KTALTGqggtSG 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 8567342   175 YCISKYGVEAFSDSLRREISYFGVKV-AII 203
Cdd:PRK08628 153 YAAAKGAQLALTREWAVALAKDGVRVnAVI 182
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 29-210 6.59e-13

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


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 67.30  E-value: 6.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG----AEQLRnKTSDRLETVILDVTKTESIVAATQWVKERVGnr 104
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENleraASELR-AGGAGVLAVVADLTDPEDIDRLVEKAGDAFG-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  105 GLWGLVNNAG--ICVFAINewLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCGGGYC-ISKY 180
Cdd:cd05344  78 RVDILVNNAGgpPPGPFAE--LTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLTVKEPEPNLVLSnVARA 155

                       170       180       190
                ....*....|....*....|....*....|
gi 8567342  181 GVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd05344 156 GLIGLVKTLSRELAPDGVTVNSVLPGYIDT 185
PRK06949 PRK06949
SDR family oxidoreductase;
27-215 8.80e-13

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 67.09  E-value: 8.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV-LAACLTEKGAEqLRNKTSDR---LETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVvLASRRVERLKE-LRAEIEAEggaAHVVSLDVTDYQSIKAAVAHAETEAG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   103 NRGLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMI----EVTLSMLPLVR-----KARGRVVNISSSMG-RVSLCG 172
Cdd:PRK06949  86 TIDI--LVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFfvaqEVAKRMIARAKgagntKPGGRIINIASVAGlRVLPQI 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 8567342   173 GGYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVSNY 215
Cdd:PRK06949 164 GLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHH 206
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 27-206 1.02e-12

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 66.69  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVL-----AACLTEKGAEQLRnKTSDRLETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK12937   3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAvnyagSAAAADELVAEIE-AAGGRAIAVQADVADAAAVTRLFDAAETAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   102 GnrGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKArGRVVNISSSMGRVSLCGGG-YCISKY 180
Cdd:PRK12937  82 G--RIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQG-GRIINLSTSVIALPLPGYGpYAASKA 158

                        170       180
                 ....*....|....*....|....*.
gi 8567342   181 GVEAFSDSLRREISYFGVKVAIIEPG 206
Cdd:PRK12937 159 AVEGLVHVLANELRGRGITVNAVAPG 184
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 30-240 1.22e-12

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: 66.63  E-value: 1.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACL----TEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrG 105
Cdd:cd05366   3 KVAIITGAAQGIGRAIAERLAADGFNIVLADLnleeAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFG--S 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  106 LWGLVNNAGICVFAINEWLKKEDFANILDVN----LLGMIEVTLSMLPLVRKarGRVVNISSSMGRVSLCG-GGYCISKY 180
Cdd:cd05366  81 FDVMVNNAGIAPITPLLTITEEDLKKVYAVNvfgvLFGIQAAARQFKKLGHG--GKIINASSIAGVQGFPNlGAYSASKF 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  181 GVEAFSDSLRREISYFGVKVAIIEPGGFRTNVsnYERLSHSIEKLWDQTSSEVKEVYDKN 240
Cdd:cd05366 159 AVRGLTQTAAQELAPKGITVNAYAPGIVKTEM--WDYIDEEVGEIAGKPEGEGFAEFSSS 216
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 30-210 1.37e-12

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: 66.32  E-value: 1.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRGMRVL------AACLtEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:cd08940   3 KVALVTGSTSGIGLGIARALAAAGANIVlngfgdAAEI-EAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFG- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  104 rGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCG-GGYCISKYG 181
Cdd:cd08940  81 -GVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGwGRIINIASVHGLVASANkSAYVAAKHG 159

                       170       180
                ....*....|....*....|....*....
gi 8567342  182 VEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd08940 160 VVGLTKVVALETAGTGVTCNAICPGWVLT 188
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 28-210 2.49e-12

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: 65.63  E-value: 2.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNK--TSDRLETVIL--DVTKTESIVAATQWVKERVGN 103
Cdd:cd08933   8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESElnRAGPGSCKFVpcDVTKEEDIKTLISVTVERFGR 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  104 rgLWGLVNNAGIcvFAINEWLKK---EDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISS---SMGRVSLCggGYCI 177
Cdd:cd08933  88 --IDCLVNNAGW--HPPHQTTDEtsaQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSlvgSIGQKQAA--PYVA 161

                       170       180       190
                ....*....|....*....|....*....|...
gi 8567342  178 SKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd08933 162 TKGAITAMTKALAVDESRYGVRVNCISPGNIWT 194
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 27-211 2.82e-12

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 65.28  E-value: 2.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacltekgaeqLRNKTSDRLETV---------------ILD---VTKTE 88
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVI-----------LLGRTEEKLEAVydeieaaggpqpaiiPLDlltATPQN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    89 SI-VAATqwVKERVGNrgLWGLVNNAGI----CVFainEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNIS 162
Cdd:PRK08945  79 YQqLADT--IEEQFGR--LDGVLHNAGLlgelGPM---EQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPaASLVFTS 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 8567342   163 SSMGRVSLCG-GGYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTN 211
Cdd:PRK08945 152 SSVGRQGRANwGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTA 201
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 27-206 3.49e-12

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: 65.20  E-value: 3.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFG--GL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  107 WGLVNNAGICVFAIN-EWLKKEDFANILDVNLLGMIEVTLSMLPLVR-KARGRVVNISSSMGRVSLCG-GGYCISKYGVE 183
Cdd:cd08944  79 DLLVNNAGAMHLTPAiIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIaRGGGSIVNLSSIAGQSGDPGyGAYGASKAAIR 158

                       170       180
                ....*....|....*....|...
gi 8567342  184 AFSDSLRREISYFGVKVAIIEPG 206
Cdd:cd08944 159 NLTRTLAAELRHAGIRCNALAPG 181
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 27-205 5.17e-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: 64.80  E-value: 5.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDrLETVILDVtktesivAATQWVKERVGNRGL 106
Cdd:cd05351   5 FAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPG-IEPVCVDL-------SDWDATEEALGSVGP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  107 W-GLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP--LVRKARGRVVNISSSMGRVSLCG-GGYCISKYGV 182
Cdd:cd05351  77 VdLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARgmIARGVPGSIVNVSSQASQRALTNhTVYCSTKAAL 156

                       170       180
                ....*....|....*....|...
gi 8567342  183 EAFSDSLRREISYFGVKVAIIEP 205
Cdd:cd05351 157 DMLTKVMALELGPHKIRVNSVNP 179
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 27-210 7.34e-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: 64.15  E-value: 7.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAC----LTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:cd05369   1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGrkpeVLEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLKEFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  103 NrgLWGLVNNAG---ICVFainEWLKKEDFANILDVNLLGMIEVTLSMLP--LVRKARGRVVNISSSMGRvslCGGGYCI 177
Cdd:cd05369  81 K--IDILINNAAgnfLAPA---ESLSPNGFKTVIDIDLNGTFNTTKAVGKrlIEAKHGGSILNISATYAY---TGSPFQV 152

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 8567342  178 ----SKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd05369 153 hsaaAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPT 189
PRK06138 PRK06138
SDR family oxidoreductase;
26-211 8.15e-12

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 64.02  E-value: 8.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSD--RLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:PRK06138   2 RLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAggRAFARQGDVGSAEAVEALVDFVAARWG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   104 rGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCG-GGYCISKYG 181
Cdd:PRK06138  81 -RLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGgGSIVNTASQLALAGGRGrAAYVASKGA 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 8567342   182 VEAFSDSLRREISYFGVKVAIIEPGGFRTN 211
Cdd:PRK06138 160 IASLTRAMALDHATDGIRVNAVAPGTIDTP 189
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 27-228 1.01e-11

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: 63.89  E-value: 1.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV----LAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:cd05352   6 LKGKVAIVTGGSRGIGLAIARALAEAGADVaiiyNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  103 NrgLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRK-ARGRVVNISSSMGRV---SLCGGGYCIS 178
Cdd:cd05352  86 K--IDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKqGKGSLIITASMSGTIvnrPQPQAAYNAS 163

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 8567342  179 KYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVSNYerLSHSIEKLWDQ 228
Cdd:cd05352 164 KAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDF--VDKELRKKWES 211
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 30-210 1.43e-11

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: 63.26  E-value: 1.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKgAEQLRNKTSdRLETVILDVTKTESIVAATQWVkERVGNrglwgL 109
Cdd:cd05368   3 KVALITAAAQGIGRAIALAFAREGANVIATDINEE-KLKELERGP-GITTRVLDVTDKEQVAALAKEE-GRIDV-----L 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  110 VNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSLCGG--GYCISKYGVEAFS 186
Cdd:cd05368  75 FNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPkMLARKDGSIINMSSVASSIKGVPNrfVYSTTKAAVIGLT 154

                       170       180
                ....*....|....*....|....
gi 8567342  187 DSLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd05368 155 KSVAADFAQQGIRCNAICPGTVDT 178
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 27-210 1.48e-11

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 63.20  E-value: 1.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLET-------VILDVTKTESIVAATQWVKE 99
Cdd:PRK12827   4 LDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAVAAGIEAaggkalgLAFDVRDFAATRAALDAGVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   100 RVGnrGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR--GRVVNISS-SMGRVSLCGGGYC 176
Cdd:PRK12827  84 EFG--RLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARrgGRIVNIASvAGVRGNRGQVNYA 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 8567342   177 ISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK12827 162 ASKAGLIGLTKTLANELAPRGITVNAVAPGAINT 195
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 27-205 1.49e-11

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: 63.18  E-value: 1.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:cd05345   3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFG--RL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  107 WGLVNNAGICVFAIN-EWLKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRV-VNISSSMG---RVSLCggGYCISKYG 181
Cdd:cd05345  81 DILVNNAGITHRNKPmLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGViINIASTAGlrpRPGLT--WYNASKGW 158

                       170       180
                ....*....|....*....|....
gi 8567342  182 VEAFSDSLRREISYFGVKVAIIEP 205
Cdd:cd05345 159 VVTATKAMAVELAPRNIRVNCLCP 182
PRK07775 PRK07775
SDR family oxidoreductase;
25-212 2.17e-11

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 63.23  E-value: 2.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    25 SHLQDKYVFITGCDSGFGNLLARQLDRRGMRV-LAACLTEKGAEQLRNKTSDRLETVI--LDVTKTESIVAATQWVKERV 101
Cdd:PRK07775   6 PHPDRRPALVAGASSGIGAATAIELAAAGFPVaLGARRVEKCEELVDKIRADGGEAVAfpLDVTDPDSVKSFVAQAEEAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   102 GNRGLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMG-RVSLCGGGYCISK 179
Cdd:PRK07775  86 GEIEV--LVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPgMIERRRGDLIFVGSDVAlRQRPHMGAYGAAK 163

                        170       180       190
                 ....*....|....*....|....*....|...
gi 8567342   180 YGVEAFSDSLRREISYFGVKVAIIEPGGFRTNV 212
Cdd:PRK07775 164 AGLEAMVTNLQMELEGTGVRASIVHPGPTLTGM 196
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 27-211 8.06e-11

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: 61.32  E-value: 8.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLT-EKGAEQLRNKTS--DRLETVILDVTKTESIVAATQWVKERVGN 103
Cdd:cd08935   3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNqEKGDKVAKEITAlgGRAIALAADVLDRASLERAREEIVAQFGT 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  104 RGLwgLVNNAG-------ICVFAINEW-------LKKEDFANILDVNLLGmiEVTLSML---PLVRKARGRVVNISS--- 163
Cdd:cd08935  83 VDI--LINGAGgnhpdatTDPEHYEPEteqnffdLDEEGWEFVFDLNLNG--SFLPSQVfgkDMLEQKGGSIINISSmna 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 8567342  164 --SMGRVSlcggGYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTN 211
Cdd:cd08935 159 fsPLTKVP----AYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTP 204
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 27-210 1.37e-10

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


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 60.28  E-value: 1.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSD--RLETVI----LDVTKTESIVAATQWVKER 100
Cdd:cd05340   2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEegGRQPQWfildLLTCTSENCQQLAQRIAVN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  101 VGNrgLWGLVNNAGIcVFAIN--EWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCG-GGYC 176
Cdd:cd05340  82 YPR--LDGVLHNAGL-LGDVCplSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQGRANwGAYA 158

                       170       180       190
                ....*....|....*....|....*....|....
gi 8567342  177 ISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd05340 159 VSKFATEGL*QVLADEYQQRNLRVNCINPGGTRT 192
PRK12746 PRK12746
SDR family oxidoreductase;
24-213 1.37e-10

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 60.82  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    24 VSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGA--EQLRNKTSDRLETVIL--DVTKTESIVAATQWVKE 99
Cdd:PRK12746   1 MKNLDGKVALVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAadETIREIESNGGKAFLIeaDLNSIDGVKKLVEQLKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   100 ----RVGNRGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRkARGRVVNISSSMGRVSLCGG-G 174
Cdd:PRK12746  81 elqiRVGTSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLR-AEGRVINISSAEVRLGFTGSiA 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 8567342   175 YCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVS 213
Cdd:PRK12746 160 YGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDIN 198
PRK06139 PRK06139
SDR family oxidoreductase;
27-209 1.92e-10

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 60.89  E-value: 1.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMR-VLAA------------ClTEKGAEQLrnktsdrleTVILDVTKTESIVAA 93
Cdd:PRK06139   5 LHGAVVVITGASSGIGQATAEAFARRGARlVLAArdeealqavaeeC-RALGAEVL---------VVPTDVTDADQVKAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    94 TQWVKERVGNRGLWglVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRK-ARGRVVNISSSMGRVSL-C 171
Cdd:PRK06139  75 ATQAASFGGRIDVW--VNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKqGHGIFINMISLGGFAAQpY 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 8567342   172 GGGYCISKYGVEAFSDSLRREISYF-GVKVAIIEPG-----GFR 209
Cdd:PRK06139 153 AAAYSASKFGLRGFSEALRGELADHpDIHVCDVYPAfmdtpGFR 196
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-211 2.71e-10

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 59.75  E-value: 2.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAE--QLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNR 104
Cdd:PRK06935  13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWDEtrRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   105 GLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMgrvSLCGG----GYCISK 179
Cdd:PRK06935  93 DI--LVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKvMAKQGSGKIINIASML---SFQGGkfvpAYTASK 167

                        170       180       190
                 ....*....|....*....|....*....|..
gi 8567342   180 YGVEAFSDSLRREISYFGVKVAIIEPGGFRTN 211
Cdd:PRK06935 168 HGVAGLTKAFANELAAYNIQVNAIAPGYIKTA 199
PRK07201 PRK07201
SDR family oxidoreductase;
18-203 2.98e-10

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 61.12  E-value: 2.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    18 FRERQVVSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVIL---DVTKTESIVAAT 94
Cdd:PRK07201 360 ARRRDLRGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAytcDLTDSAAVDHTV 439

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    95 QWVKERVGNRGLwgLVNNAG--ICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNIsSSMG----- 166
Cdd:PRK07201 440 KDILAEHGHVDY--LVNNAGrsIRRSVENSTDRFHDYERTMAVNYFGAVRLILGLLPHMRERRfGHVVNV-SSIGvqtna 516

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 8567342   167 -RVSlcggGYCISKYGVEAFSDSLRREISYFGVKVAII 203
Cdd:PRK07201 517 pRFS----AYVASKAALDAFSDVAASETLSDGITFTTI 550
PRK06194 PRK06194
hypothetical protein; Provisional
 27-217 2.98e-10

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 60.03  E-value: 2.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMR-VLA-----------ACLTEKGAEQLrnktsdrleTVILDVTKTESIVAAT 94
Cdd:PRK06194   4 FAGKVAVITGAASGFGLAFARIGAALGMKlVLAdvqqdaldravAELRAQGAEVL---------GVRTDVSDAAQVEALA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    95 QWVKERVGNRGLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKA-------RGRVVNISSSMGR 167
Cdd:PRK06194  75 DAALERFGAVHL--LFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAaekdpayEGHIVNTASMAGL 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 8567342   168 VSLCGGG-YCISKYGVEAFSDSLRREISYFG--VKVAIIEPGGFRTNVSNYER 217
Cdd:PRK06194 153 LAPPAMGiYNVSKHAVVSLTETLYQDLSLVTdqVGASVLCPYFVPTGIWQSER 205
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 27-206 3.24e-10

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: 59.55  E-value: 3.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWG--SI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  107 WGLVNNAGICVFAINEWLKKEDFANILDVNLLGMievtLSMLPLVRKAR------GRVVNISSSMGRV-SLCGGGYCISK 179
Cdd:cd05363  79 DILVNNAALFDLAPIVDITRESYDRLFAINVSGT----LFMMQAVARAMiaqgrgGKIINMASQAGRRgEALVGVYCATK 154

                       170       180
                ....*....|....*....|....*..
gi 8567342  180 YGVEAFSDSLRREISYFGVKVAIIEPG 206
Cdd:cd05363 155 AAVISLTQSAGLNLIRHGINVNAIAPG 181
PRK05866 PRK05866
SDR family oxidoreductase;
27-200 3.33e-10

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 59.76  E-value: 3.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDR---LETVILDVTKTESIVAATQWVKERVGn 103
Cdd:PRK05866  38 LTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAggdAMAVPCDLSDLDAVDALVADVEKRIG- 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   104 rGLWGLVNNAGICVF-----AINEWlkkEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISS--SMGRVSLCGGGY 175
Cdd:PRK05866 117 -GVDILINNAGRSIRrplaeSLDRW---HDVERTMVLNYYAPLRLIRGLAPgMLERGDGHIINVATwgVLSEASPLFSVY 192

                        170       180
                 ....*....|....*....|....*
gi 8567342   176 CISKYGVEAFSDSLRREISYFGVKV 200
Cdd:PRK05866 193 NASKAALSAVSRVIETEWGDRGVHS 217
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 29-210 3.42e-10

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 59.21  E-value: 3.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGaeqlrnKTSDRLETVILDVTKTESivAATQWVKErvgnrgLWG 108
Cdd:PRK06550   5 TKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDKP------DLSGNFHFLQLDLSDDLE--PLFDWVPS------VDI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   109 LVNNAGIC-----VFAINEwlkkEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRVSlcGGG---YCISK 179
Cdd:PRK06550  71 LCNTAGILddykpLLDTSL----EEWQHIFDTNLTSTFLLTRAYLPqMLERKSGIIINMCSIASFVA--GGGgaaYTASK 144

                        170       180       190
                 ....*....|....*....|....*....|.
gi 8567342   180 YGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK06550 145 HALAGFTKQLALDYAKDGIQVFGIAPGAVKT 175
PRK07074 PRK07074
SDR family oxidoreductase;
29-210 4.32e-10

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 59.01  E-value: 4.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSD-RLETVILDVTKTESIVAAtqwVKERVGNRGLW 107
Cdd:PRK07074   2 KRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDaRFVPVACDLTDAASLAAA---LANAAAERGPV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   108 G-LVNNAGIcvfAINEWLKKEDFANI---LDVNLLGMIEVTLSMLPLVRKA-RGRVVNISSSMGRVSLCGGGYCISKYGV 182
Cdd:PRK07074  79 DvLVANAGA---ARAASLHDTTPASWradNALNLEAAYLCVEAVLEGMLKRsRGAVVNIGSVNGMAALGHPAYSAAKAGL 155

                        170       180
                 ....*....|....*....|....*...
gi 8567342   183 EAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK07074 156 IHYTKLLAVEYGRFGIRANAVAPGTVKT 183
PRK06398 PRK06398
aldose dehydrogenase; Validated
 27-163 4.42e-10

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 59.08  E-value: 4.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKgaeqlRNKTSDRLEtviLDVTKTESIVAATQWVKERVGNRGL 106
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEP-----SYNDVDYFK---VDVSNKEQVIKGIDYVISKYGRIDI 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 8567342   107 wgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISS 163
Cdd:PRK06398  76 --LVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDkGVIINIAS 131
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 27-224 4.70e-10

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: 59.00  E-value: 4.70e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDR---LETVILDVTKTESIVAATQWVKERVGN 103
Cdd:cd05329   4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKgfkVEGSVCDVSSRSERQELMDTVASHFGG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  104 RgLWGLVNNAGICVF--AINewLKKEDFANILDVNLLGMIEVTLSMLPLV-RKARGRVVNISSSMGRVSL-CGGGYCISK 179
Cdd:cd05329  84 K-LNILVNNAGTNIRkeAKD--YTEEDYSLIMSTNFEAAYHLSRLAHPLLkASGNGNIVFISSVAGVIAVpSGAPYGATK 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 8567342  180 YGVEAFSDSLRREISYFGVKVAIIEPGGFRTN-----VSNYERLSHSIEK 224
Cdd:cd05329 161 GALNQLTRSLACEWAKDNIRVNAVAPWVIATPlvepvIQQKENLDKVIER 210
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 27-206 5.92e-10

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 58.87  E-value: 5.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:PRK08265   4 LAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFG--RV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   107 WGLVNNAgiCVFAIN-------EWLKKedfaniLDVNLLGMIEVTLSMLPLVRKARGRVVNISSSMGRVSLCGGG-YCIS 178
Cdd:PRK08265  82 DILVNLA--CTYLDDglassraDWLAA------LDVNLVSAAMLAQAAHPHLARGGGAIVNFTSISAKFAQTGRWlYPAS 153

                        170       180
                 ....*....|....*....|....*...
gi 8567342   179 KYGVEAFSDSLRREISYFGVKVAIIEPG 206
Cdd:PRK08265 154 KAAIRQLTRSMAMDLAPDGIRVNSVSPG 181
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 32-213 8.17e-10

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


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 58.13  E-value: 8.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   32 VFITGCDSGFGNLLARQLDRRGMRV-------------LAACLTEKGAeqlrnktsdRLETVILDVTKTESIVAATQWVK 98
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVvinyrkskdaaaeVAAEIEELGG---------KAVVVRADVSQPQDVEEMFAAVK 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   99 ERVGnrGLWGLVNNAGICVFA-INEwLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISS-SMGRVSLCGGGY 175
Cdd:cd05359  72 ERFG--RLDVLVSNAAAGAFRpLSE-LTPAHWDAKMNTNLKALVHCAQQAAKLMRERGgGRIVAISSlGSIRALPNYLAV 148

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 8567342  176 CISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVS 213
Cdd:cd05359 149 GTAKAALEALVRYLAVELGPRGIRVNAVSPGVIDTDAL 186
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
30-210 9.71e-10

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 58.20  E-value: 9.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLE---TVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:PRK08643   3 KVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGkaiAVKADVSDRDQVFAAVRQVVDTFG--DL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   107 WGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR--GRVVNISSSMGRVSLCG-GGYCISKYGVE 183
Cdd:PRK08643  81 NVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGhgGKIINATSQAGVVGNPElAVYSSTKFAVR 160

                        170       180
                 ....*....|....*....|....*..
gi 8567342   184 AFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK08643 161 GLTQTAARDLASEGITVNAYAPGIVKT 187
PRK07069 PRK07069
short chain dehydrogenase; Validated
 33-189 9.92e-10

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 58.18  E-value: 9.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    33 FITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEQLRNKTSDRLET---------VILDVTKTESIVAATQWVKERVGn 103
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVF---LTDINDAAGLDAFAAEINAahgegvafaAVQDVTDEAQWQALLAQAADAMG- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   104 rGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMG-RVSLCGGGYCISKYG 181
Cdd:PRK07069  79 -GLSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQpASIVNISSVAAfKAEPDYTAYNASKAA 157


                 ....*...
gi 8567342   182 VEAFSDSL 189
Cdd:PRK07069 158 VASLTKSI 165
PLN02253 PLN02253
xanthoxin dehydrogenase
 27-213 1.82e-09

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 57.53  E-value: 1.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVIL--DVTKTESIVAATQWVKERVGNR 104
Cdd:PLN02253  16 LLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNVCFFhcDVTVEDDVSRAVDFTVDKFGTL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   105 GLwgLVNNAGICVFAINEWLKKE--DFANILDVNL----LGMIEVTLSMLPLvrkARGRVVNISSSMGRVSLCG-GGYCI 177
Cdd:PLN02253  96 DI--MVNNAGLTGPPCPDIRNVElsEFEKVFDVNVkgvfLGMKHAARIMIPL---KKGSIVSLCSVASAIGGLGpHAYTG 170

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 8567342   178 SKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVS 213
Cdd:PLN02253 171 SKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALA 206
PRK06124 PRK06124
SDR family oxidoreductase;
27-210 2.00e-09

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 57.03  E-value: 2.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEQLRNKTSD------RLETVILDVTKTESIVAATQWVKER 100
Cdd:PRK06124   9 LAGQVALVTGSARGLGFEIARALAGAGAHVL---VNGRNAATLEAAVAAlraaggAAEALAFDIADEEAVAAAFARIDAE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   101 VGnrGLWGLVNNAGicvfAINEW----LKKEDFANILDVNLLGMIevTLSMLPLVRKAR---GRVVNISSSMGRVSLCGG 173
Cdd:PRK06124  86 HG--RLDILVNNVG----ARDRRplaeLDDAAIRALLETDLVAPI--LLSRLAAQRMKRqgyGRIIAITSIAGQVARAGD 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 8567342   174 G-YCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK06124 158 AvYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFAT 195
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 27-210 3.03e-09

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 56.66  E-value: 3.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLT-EKGAEQLRN---KTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK08936   5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSdEEEANDVAEeikKAGGEAIAVKGDVTVESDVVNLIQTAVKEFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   103 NRGLWglVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRK--ARGRVVNISSSMGRVSL-CGGGYCISK 179
Cdd:PRK08936  85 TLDVM--INNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEhdIKGNIINMSSVHEQIPWpLFVHYAASK 162

                        170       180       190
                 ....*....|....*....|....*....|.
gi 8567342   180 YGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK08936 163 GGVKLMTETLAMEYAPKGIRVNNIGPGAINT 193
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 27-208 3.46e-09

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: 56.34  E-value: 3.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVL------AACltEKGAEQLrnKTSDRLETVILDVTKTESIVAATQWVKER 100
Cdd:cd08942   4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIisarkaEAC--ADAAEEL--SAYGECIAIPADLSSEEGIEALVARVAER 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  101 vgNRGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-----GRVVNISSSMGRV--SLCGG 173
Cdd:cd08942  80 --SDRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAAtaenpARVINIGSIAGIVvsGLENY 157

                       170       180       190
                ....*....|....*....|....*....|....*
gi 8567342  174 GYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGF 208
Cdd:cd08942 158 SYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRF 192
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 27-206 4.01e-09

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


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 56.25  E-value: 4.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEQLRNKTSDRLETVI------------------LDVTKTE 88
Cdd:cd05338   1 LSGKVAFVTGASRGIGRAIALRLAKAGATVV---VAAKTASEGDNGSAKSLPGTIeetaeeieaaggqalpivVDVRDED 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   89 SIVAATQWVKERVGnrGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKA-RGRVVNISSSMGR 167
Cdd:cd05338  78 QVRALVEATVDQFG--RLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAgQGHILNISPPLSL 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 8567342  168 VSLCGG-GYCISKYGVEAFSDSLRREISYFGVKVAIIEPG 206
Cdd:cd05338 156 RPARGDvAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPS 195
PRK08251 PRK08251
SDR family oxidoreductase;
30-210 4.32e-09

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 56.10  E-value: 4.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    30 KYVFITGCDSGFGNLLARQLDRRGmRVLAAC------LTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKG-RDLALCarrtdrLEELKAELLARYPGIKVAVAALDVNDHDQVFEVFAEFRDELG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   104 rGLWGLVNNAGICV--------FAINEWLKKEDFanildVNLLGMIEVTLSMLplvRKA-RGRVVNISSSMGRVSLCG-- 172
Cdd:PRK08251  81 -GLDRVIVNAGIGKgarlgtgkFWANKATAETNF-----VAALAQCEAAMEIF---REQgSGHLVLISSVSAVRGLPGvk 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 8567342   173 GGYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK08251 152 AAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRS 189
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 27-210 5.98e-09

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 55.84  E-value: 5.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV----LAACLTEKGAEQLRNKTSDrLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIvfndINQELVDKGLAAYRELGIE-AHGYVCDVTDEDGVQAMVSQIEKEVG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   103 NRGLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSM---GRVSLcgGGYCIS 178
Cdd:PRK07097  87 VIDI--LVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPsMIKKGHGKIINICSMMselGRETV--SAYAAA 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 8567342   179 KYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK07097 163 KGGLKMLTKNIASEYGEANIQCNGIGPGYIAT 194
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
32-208 6.65e-09

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 56.14  E-value: 6.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   32 VFITGCdSGF-GNLLARQLDRRGMRVLAACLTEKGAEQLRNktSDRLETVILDVTKTESIVAATQWVkERVgnrglwglV 110
Cdd:COG0451   2 ILVTGG-AGFiGSHLARRLLARGHEVVGLDRSPPGAANLAA--LPGVEFVRGDLRDPEALAAALAGV-DAV--------V 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  111 NNAGICVFAInewlkkEDFANILDVNLLGmievTLSMLPLVRKAR-GRVVNISSS--MGRVSLC---------GGGYCIS 178
Cdd:COG0451  70 HLAAPAGVGE------EDPDETLEVNVEG----TLNLLEAARAAGvKRFVYASSSsvYGDGEGPidedtplrpVSPYGAS 139

                       170       180       190
                ....*....|....*....|....*....|
gi 8567342  179 KYGVEAFSDSLRREisyFGVKVAIIEPGGF 208
Cdd:COG0451 140 KLAAELLARAYARR---YGLPVTILRPGNV 166
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 109-210 8.75e-09

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: 54.44  E-value: 8.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  109 LVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGRVSLCG-GGYCISKYGVEAFS 186
Cdd:cd02266  35 VVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRlGRFILISSVAGLFGAPGlGGYAASKAALDGLA 114

                        90       100
                ....*....|....*....|....
gi 8567342  187 DSLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd02266 115 QQWASEGWGNGLPATAVACGTWAG 138
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 32-166 8.82e-09

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: 55.19  E-value: 8.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEkgAEqlrnktsdrletVILDVTKTESIVAATQWVKERVGnRGLWGLVN 111
Cdd:cd05328   2 IVITGAASGIGAATAELLEDAGHTVIGIDLRE--AD------------VIADLSTPEGRAAAIADVLARCS-GVLDGLVN 66

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 8567342  112 NAGICVFAINEwlkkedfaNILDVNLLGMIEVTLSMLPLVRKARG-RVVNISSSMG 166
Cdd:cd05328  67 CAGVGGTTVAG--------LVLKVNYFGLRALMEALLPRLRKGHGpAAVVVSSIAG 114
PRK12743 PRK12743
SDR family oxidoreductase;
28-210 1.06e-08

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 55.04  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    28 QDKYVFITGCDSGFGNLLARQLDRRGMRVlaaCLT----EKGAEqlrnKTSD-------RLETVILDVTKTESIVAATQW 96
Cdd:PRK12743   1 MAQVAIVTASDSGIGKACALLLAQQGFDI---GITwhsdEEGAK----ETAEevrshgvRAEIRQLDLSDLPEGAQALDK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    97 VKERVGnrGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGmievtlSMLPLVRKAR--------GRVVNISSSMGRV 168
Cdd:PRK12743  74 LIQRLG--RIDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDG------AFLCSQIAARhmvkqgqgGRIINITSVHEHT 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 8567342   169 SLCGGG-YCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK12743 146 PLPGASaYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIAT 188
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 28-211 1.06e-08

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


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 55.03  E-value: 1.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQ----LRNKTSDRLETVILDVTKTESIVAATQWVKERVGN 103
Cdd:cd08930   1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQlkeeLTNLYKNRVIALELDITSKESIKELIESYLEKFGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  104 rgLWGLVNNAGICVFAIN---EWLKKEDFANILDVNLLGMIEVTLSMLPLVRK-ARGRVVNISSSMGRVS----LCGGG- 174
Cdd:cd08930  81 --IDILINNAYPSPKVWGsrfEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKqGKGSIINIASIYGVIApdfrIYENTq 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 8567342  175 ------YCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTN 211
Cdd:cd08930 159 myspveYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNN 201
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 27-210 1.09e-08

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 54.96  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAFG--KL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   107 WGLVNNAGICVFAINewLKKED-------FANILDVNLLGMIEVTLSMLPLVRKARGRVVNISSSMGRVSlcGGG---YC 176
Cdd:PRK06200  82 DCFVGNAGIWDYNTS--LVDIPaetldtaFDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLSNSSFYP--GGGgplYT 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 8567342   177 ISKYGVEAfsdsLRREISYF---GVKVAIIEPGGFRT 210
Cdd:PRK06200 158 ASKHAVVG----LVRQLAYElapKIRVNGVAPGGTVT 190
PRK06953 PRK06953
SDR family oxidoreductase;
30-169 1.26e-08

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 54.31  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSdrlETVILDVTKTESiVAATQWV--KERVG----N 103
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQALGA---EALALDVADPAS-VAGLAWKldGEALDaavyV 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8567342   104 RGLWGlVNNAGIcvfainEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISSSMGRVS 169
Cdd:PRK06953  78 AGVYG-PRTEGV------EPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSRMGSIG 136
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 30-209 1.52e-08

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: 54.71  E-value: 1.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTS--DRLETVILDVTKTESIVAATQWVKERVGnrGLW 107
Cdd:cd08943   2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQggPRALGVQCDVTSEAQVQSAFEQAVLEFG--GLD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  108 GLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR--GRVV-NISSSMGRVSLCGGGYCISKygveA 184
Cdd:cd08943  80 IVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGigGNIVfNASKNAVAPGPNAAAYSAAK----A 155

                       170       180
                ....*....|....*....|....*....
gi 8567342  185 FSDSLRR----EISYFGVKVAIIEPGGFR 209
Cdd:cd08943 156 AEAHLARclalEGGEDGIRVNTVNPDAVF 184
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 27-211 1.72e-08

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 54.52  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVIL---DVTKTESIVAATQWVKERVGN 103
Cdd:PRK08277   8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAvkaDVLDKESLEQARQQILEDFGP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   104 RGLwgLVNNAG---------ICVFAINEW------LKKEDFANILDVNLLGmievtlSMLP-------LVRKARGRVVNI 161
Cdd:PRK08277  88 CDI--LINGAGgnhpkattdNEFHELIEPtktffdLDEEGFEFVFDLNLLG------TLLPtqvfakdMVGRKGGNIINI 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 8567342   162 SS-----SMGRVSlcggGYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTN 211
Cdd:PRK08277 160 SSmnaftPLTKVP----AYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTE 210
PRK06500 PRK06500
SDR family oxidoreductase;
25-234 2.07e-08

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 54.19  E-value: 2.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    25 SHLQDKYVFITGCDSGFGNLLARQLDRRGMRV---------LAACLTEKGAEQL--RNKTSDrletvildvtktesiVAA 93
Cdd:PRK06500   2 SRLQGKTALITGGTSGIGLETARQFLAEGARVaitgrdpasLEAARAELGESALviRADAGD---------------VAA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    94 TQWVKERVGNRG--LWGLVNNAGICVFA-INEWlKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISSS----MG 166
Cdd:PRK06500  67 QKALAQALAEAFgrLDAVFINAGVAKFApLEDW-DEAMFDRSFNTNVKGPYFLIQALLPLLANPASIVLNGSINahigMP 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8567342   167 RVSLcgggYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVsnYERLSHSIEKLwDQTSSEVK 234
Cdd:PRK06500 146 NSSV----YAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPL--YGKLGLPEATL-DAVAAQIQ 206
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 27-264 2.15e-08

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


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 54.07  E-value: 2.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQL--RNKTSDRLETVILDVTKTESIVAATQWVKERVGNR 104
Cdd:cd08937   2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLaeILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  105 GLwgLVNNAGICVFA--INEWLKKEDFANIlDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMGRvslcgGG----YCI 177
Cdd:cd08937  82 DV--LINNVGGTIWAkpYEHYEEEQIEAEI-RRSLFPTLWCCRAVLPhMLERQQGVIVNVSSIATR-----GIyripYSA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  178 SKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVSNYERLSHSI---EKLW-----DQT--SSEVKEVydkNFLDSYIK 247
Cdd:cd08937 154 AKGGVNALTASLAFEHARDGIRVNAVAPGGTEAPPRKIPRNAAPMseqEKVWyqrivDQTldSSLMGRY---GTIDEQVR 230

                       250
                ....*....|....*..
gi 8567342  248 AIQSLTdtcSDDLSVVT 264
Cdd:cd08937 231 AILFLA---SDEASYIT 244
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
30-211 2.15e-08

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 53.92  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE-KGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLWG 108
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTEnKELTKLAEQYNSNLTFHSLDLQDVHELETNFNEILSSIQEDNVSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   109 --LVNNAGIcVFAIN--EWLKKEDFANILDVNLLgmIEVTLSMLPLVR----KARGRVVNISSSMGRVSLCG-GGYCISK 179
Cdd:PRK06924  82 ihLINNAGM-VAPIKpiEKAESEELITNVHLNLL--APMILTSTFMKHtkdwKVDKRVINISSGAAKNPYFGwSAYCSSK 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 8567342   180 YGVEAFSDS--LRREISYFGVKVAIIEPGGFRTN 211
Cdd:PRK06924 159 AGLDMFTQTvaTEQEEEEYPVKIVAFSPGVMDTN 192
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 28-239 2.65e-08

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: 54.01  E-value: 2.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAACL----TEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGN 103
Cdd:cd05322   1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADInsenAEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  104 RGLwgLVNNAGICVFAINEWLKKEDFANILDVNLLG--MIEVTLSMLPLVRKARGRVVNISSSMGRV-SLCGGGYCISKY 180
Cdd:cd05322  81 VDL--LVYSAGIAKSAKITDFELGDFDRSLQVNLVGyfLCAREFSKLMIRDGIQGRIIQINSKSGKVgSKHNSGYSAAKF 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  181 GVEAFSDSLRREISYFGVKVAIIEPGGFRTNvSNYERLSHSIEKLWDQTSSEVKEVY-DK 239
Cdd:cd05322 159 GGVGLTQSLALDLAEHGITVNSLMLGNLLKS-PMFQSLLPQYAKKLGIKESEVEQYYiDK 217
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 27-207 2.77e-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: 53.89  E-value: 2.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNrgL 106
Cdd:cd05348   2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGK--L 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  107 WGLVNNAGI-----CVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISSSMGRVSlcGGG---YCIS 178
Cdd:cd05348  80 DCFIGNAGIwdystSLVDIPEEKLDEAFDELFHINVKGYILGAKAALPALYATEGSVIFTVSNAGFYP--GGGgplYTAS 157

                       170       180       190
                ....*....|....*....|....*....|..
gi 8567342  179 KYGVEAfsdsLRREISY-FG--VKVAIIEPGG 207
Cdd:cd05348 158 KHAVVG----LVKQLAYeLAphIRVNGVAPGG 185
PRK06947 PRK06947
SDR family oxidoreductase;
30-212 4.42e-08

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 53.27  E-value: 4.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    30 KYVFITGCDSGFGNLLARQLDRRGMRV--------LAACLTEKGAEQlrnkTSDRLETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVginyardaAAAEETADAVRA----AGGRACVVAGDVANEADVIAMFDAVQSAF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   102 GnrGLWGLVNNAGICvfAINEWLKKEDFAN---ILDVNLLGMIEVTLSMLPLVRKARG----RVVNISSSMGRVslcgGG 174
Cdd:PRK06947  79 G--RLDALVNNAGIV--APSMPLADMDAARlrrMFDTNVLGAYLCAREAARRLSTDRGgrggAIVNVSSIASRL----GS 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 8567342   175 ------YCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNV 212
Cdd:PRK06947 151 pneyvdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEI 194
PRK07577 PRK07577
SDR family oxidoreductase;
27-210 4.76e-08

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 52.81  E-value: 4.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACltekgaeqlRNKTSD---RLETVIL-DVTKTESIVAATqwvkerVG 102
Cdd:PRK07577   1 MSSRTVLVTGATKGIGLALSLRLANLGHQVIGIA---------RSAIDDfpgELFACDLaDIEQTAATLAQI------NE 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   103 NRGLWGLVNNAGIcvfAINEWLKKEDFA---NILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISS-----SMGRVSlcgg 173
Cdd:PRK07577  66 IHPVDAIVNNVGI---ALPQPLGKIDLAalqDVYDLNVRAAVQVTQAFLEGMKLREqGRIVNICSraifgALDRTS---- 138

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 8567342   174 gYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK07577 139 -YSAAKSALVGCTRTWALELAEYGITVNAVAPGPIET 174
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 32-210 6.33e-08

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


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 52.14  E-value: 6.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   32 VFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEQLRNKTSDRLE-TVILDVTKTESIVAATQwvkeRVGNRGLWglV 110
Cdd:cd11730   1 ALILGATGGIGRALARALAGRGWRLL---LSGRDAGALAGLAAEVGAlARPADVAAELEVWALAQ----ELGPLDLL--V 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  111 NNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVrKARGRVVNISSSMGRVSLCG-GGYCISKYGVEAFSDSL 189
Cdd:cd11730  72 YAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHALALL-AAGARLVFLGAYPELVMLPGlSAYAAAKAALEAYVEVA 150

                       170       180
                ....*....|....*....|.
gi 8567342  190 RREISyfGVKVAIIEPGGFRT 210
Cdd:cd11730 151 RKEVR--GLRLTLVRPPAVDT 169
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
27-205 7.82e-08

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 53.70  E-value: 7.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNK--TSDRLETVILDVTKTESIVAATQWVKERVGnr 104
Cdd:PRK08324 420 LAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAElgGPDRALGVACDVTDEAAVQAAFEEAALAFG-- 497

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   105 GLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKA--RGRVVNISSSMGRVSLCG-GGYCISKyg 181
Cdd:PRK08324 498 GVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQglGGSIVFIASKNAVNPGPNfGAYGAAK-- 575

                        170       180
                 ....*....|....*....|....*...
gi 8567342   182 veAFSDSLRR----EISYFGVKVAIIEP 205
Cdd:PRK08324 576 --AAELHLVRqlalELGPDGIRVNGVNP 601
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 30-213 7.91e-08

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 52.77  E-value: 7.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFG-----NLLARQLDRRGMRVLAACLTEKGAEQLRNKTSD-------RLETVILDVTKTESIVAATQWV 97
Cdd:cd08941   2 KVVLVTGANSGLGlaiceRLLAEDDENPELTLILACRNLQRAEAACRALLAshpdarvVFDYVLVDLSNMVSVFAAAKEL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   98 KERVgnRGLWGLVNNAGICVFAINEWLK--KEDFAN-------------------------------ILDVNLLGMIEVT 144
Cdd:cd08941  82 KKRY--PRLDYLYLNAGIMPNPGIDWIGaiKEVLTNplfavtnptykiqaegllsqgdkatedglgeVFQTNVFGHYYLI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  145 LSMLPLVRKAR--GRVVNISSSMGRVSL-------CGGG---YCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNV 212
Cdd:cd08941 160 RELEPLLCRSDggSQIIWTSSLNASPKYfslediqHLKGpapYSSSKYLVDLLSLALNRKFNKLGVYSYVVHPGICTTNL 239


                .
gi 8567342  213 S 213
Cdd:cd08941 240 T 240
PRK07023 PRK07023
SDR family oxidoreductase;
34-192 8.16e-08

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 52.32  E-value: 8.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    34 ITGCDSGFGNLLARQLDRRGMRVLaaCLTEKGAEQLRNKTSDRLETVILDVTKTEsivAATQWVKERVGNRGLWG----- 108
Cdd:PRK07023   6 VTGHSRGLGAALAEQLLQPGIAVL--GVARSRHPSLAAAAGERLAEVELDLSDAA---AAAAWLAGDLLAAFVDGasrvl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   109 LVNNAGIcVFAINEwLKKEDFANI---LDVNLLGMIEVTLSMLPLVRK-ARGRVVNISSSMGRVSLCG-GGYCISKYGVE 183
Cdd:PRK07023  81 LINNAGT-VEPIGP-LATLDAAAIaraVGLNVAAPLMLTAALAQAASDaAERRILHISSGAARNAYAGwSVYCATKAALD 158


                 ....*....
gi 8567342   184 AFSDSLRRE 192
Cdd:PRK07023 159 HHARAVALD 167
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 30-210 8.74e-08

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: 52.07  E-value: 8.74e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACL-TEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLwg 108
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYrSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDT-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  109 LVNNAGI---------CVFAINEWlkkEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSM---GRVSLcgGGY 175
Cdd:cd05349  79 IVNNALIdfpfdpdqrKTFDTIDW---EDYQQQLEGAVKGALNLLQAVLPDFKERGsGRVINIGTNLfqnPVVPY--HDY 153

                       170       180       190
                ....*....|....*....|....*....|....*
gi 8567342  176 CISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd05349 154 TTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKV 188
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-165 1.31e-07

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 51.63  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACL-TEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnRG 105
Cdd:PRK08642   3 ISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHqSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEHFG-KP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8567342   106 LWGLVNNAgICVFAIN-------EWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSM 165
Cdd:PRK08642  82 ITTVVNNA-LADFSFDgdarkkaDDITWEDFQQQLEGSVKGALNTIQAALPGMREQGfGRIINIGTNL 148
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 30-206 1.46e-07

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: 51.43  E-value: 1.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGLWGL 109
Cdd:cd09761   2 KVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLG--RIDVL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  110 VNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISSSMGRVSLCGG-GYCISKYGVEAFSDS 188
Cdd:cd09761  80 VNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAFQSEPDSeAYAASKGGLVALTHA 159

                       170
                ....*....|....*...
gi 8567342  189 LRREISYFgVKVAIIEPG 206
Cdd:cd09761 160 LAMSLGPD-IRVNCISPG 176
PRK07831 PRK07831
SDR family oxidoreductase;
27-205 1.54e-07

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 51.57  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGC-DSGFGNLLARQLDRRGMRVLAACLTEK----GAEQLRNKT-SDRLETVILDVTKTESIVAATQWVKER 100
Cdd:PRK07831  15 LAGKVVLVTAAaGTGIGSATARRALEEGARVVISDIHERrlgeTADELAAELgLGRVEAVVCDVTSEAQVDALIDAAVER 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   101 VGnrGLWGLVNNAG------ICVFAINEWLKkedfanILDVNLLGMIEVTLSMLP--LVRKARGRVVNISSSMG-RVSLC 171
Cdd:PRK07831  95 LG--RLDVLVNNAGlggqtpVVDMTDDEWSR------VLDVTLTGTFRATRAALRymRARGHGGVIVNNASVLGwRAQHG 166

                        170       180       190
                 ....*....|....*....|....*....|....
gi 8567342   172 GGGYCISKYGVEAFSDSLRREISYFGVKVAIIEP 205
Cdd:PRK07831 167 QAHYAAAKAGVMALTRCSALEAAEYGVRINAVAP 200
PRK06101 PRK06101
SDR family oxidoreductase;
32-214 1.57e-07

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 51.41  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    32 VFITGCDSGFGNLLARQLDRRGMRVLaACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNrglWglVN 111
Cdd:PRK06101   4 VLITGATSGIGKQLALDYAKQGWQVI-ACGRNQSVLDELHTQSANIFTLAFDVTDHPGTKAALSQLPFIPEL---W--IF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   112 NAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKARgRVVNISSSMGRVSLC-GGGYCISKYGVEAFSDSLR 190
Cdd:PRK06101  78 NAGDCEYMDDGKVDATLMARVFNVNVLGVANCIEGIQPHLSCGH-RVVIVGSIASELALPrAEAYGASKAAVAYFARTLQ 156

                        170       180
                 ....*....|....*....|....
gi 8567342   191 REISYFGVKVAIIEPGGFRTNVSN 214
Cdd:PRK06101 157 LDLRPKGIEVVTVFPGFVATPLTD 180
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 25-183 2.01e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 51.16  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    25 SHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAC--LTEKGAEQLRNKTSDRLETVIL--DVTKTESIVAATQWVKER 100
Cdd:PRK06198   2 GRLDGKVALVTGGTQGLGAAIARAFAERGAAGLVICgrNAEKGEAQAAELEALGAKAVFVqaDLSDVEDCRRVVAAADEA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   101 VGnrGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLG----MIEVTLSMLPlvRKARGRVVNISSSMgrvSLCG---- 172
Cdd:PRK06198  82 FG--RLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRApfflMQEAIKLMRR--RKAEGTIVNIGSMS---AHGGqpfl 154

                        170
                 ....*....|.
gi 8567342   173 GGYCISKYGVE 183
Cdd:PRK06198 155 AAYCASKGALA 165
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 34-238 2.01e-07

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


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 51.31  E-value: 2.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   34 ITGCDSGFGNLLARQLDRRGMRVL------AACLTEKGAEQLR-NKTSDRLETVILDVTKTESIVAATQwvkERVGnrGL 106
Cdd:cd05337   6 VTGASRGIGRAIATELAARGFDIAindlpdDDQATEVVAEVLAaGRRAIYFQADIGELSDHEALLDQAW---EDFG--RL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  107 WGLVNNAGICVFAINEWLK--KEDFANILDVNLLGMI----EVTLSML--PLVRKA-RGRVVNISS-SMGRVSLCGGGYC 176
Cdd:cd05337  81 DCLVNNAGIAVRPRGDLLDltEDSFDRLIAINLRGPFfltqAVARRMVeqPDRFDGpHRSIIFVTSiNAYLVSPNRGEYC 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8567342  177 ISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTnvsnyerlshsieklwDQTSSeVKEVYD 238
Cdd:cd05337 161 ISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHT----------------DMTAP-VKEKYD 205
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 27-238 3.46e-07

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 50.46  E-value: 3.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVlaacltekgAEQLRNKTSDRLETV----------------ILDVTKTESI 90
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALV---------AIHYGNRKEEAEETVyeiqsnggsafsiganLESLHGVEAL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    91 VAA-TQWVKERVGNRGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKaRGRVVNISSSMGRVS 169
Cdd:PRK12747  73 YSSlDNELQNRTGSTKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRD-NSRIINISSAATRIS 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8567342   170 LCGG-GYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVsNYERLSHSIEKLWDQTSS------EVKEVYD 238
Cdd:PRK12747 152 LPDFiAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDM-NAELLSDPMMKQYATTISafnrlgEVEDIAD 226
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 33-210 5.17e-07

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 49.96  E-value: 5.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    33 FITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEQLRNKTSDRLET-------VILDVTKTESIVAATQWVKERVGnrG 105
Cdd:PRK12745   6 LVTGGRRGIGLGIARALAAAGFDLA---INDRPDDEELAATQQELRAlgvevifFPADVADLSAHEAMLDAAQAAWG--R 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   106 LWGLVNNAGICVFAINEWL--KKEDFANILDVNLLGMIEVT-------LSMLPLVRKARGRVVNISS-SMGRVSLCGGGY 175
Cdd:PRK12745  81 IDCLVNNAGVGVKVRGDLLdlTPESFDRVLAINLRGPFFLTqavakrmLAQPEPEELPHRSIVFVSSvNAIMVSPNRGEY 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 8567342   176 CISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK12745 161 CISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKT 195
PRK05867 PRK05867
SDR family oxidoreductase;
27-227 1.28e-06

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 48.88  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAClteKGAEQLRnKTSDRLE-------TVILDVTKTESIVAATQWVKE 99
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAA---RHLDALE-KLADEIGtsggkvvPVCCDVSQHQQVTSMLDQVTA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   100 RVGnrGLWGLVNNAGICVFAINEWLKKEDFANILDVNLLGM-IEVTLSMLPLVRKARGRVVNISSSMG----RVSLCGGG 174
Cdd:PRK05867  83 ELG--GIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVfLTAQAAAKAMVKQGQGGVIINTASMSghiiNVPQQVSH 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 8567342   175 YCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVsnYERLsHSIEKLWD 227
Cdd:PRK05867 161 YCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTEL--VEPY-TEYQPLWE 210
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 27-206 1.79e-06

(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: 48.47  E-value: 1.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLtekGAEQLRNKTSDRLETVILD---------VTKTESIVAATQWV 97
Cdd:cd05353   3 FDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDL---GGDRKGSGKSSSAADKVVDeikaaggkaVANYDSVEDGEKIV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   98 KERVGNRG-LWGLVNNAGIC---VFAInewLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISSSMGrvsLCG 172
Cdd:cd05353  80 KTAIDAFGrVDILVNNAGILrdrSFAK---MSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKfGRIINTSSAAG---LYG 153

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 8567342  173 ----GGYCISKYGVEAFSDSLRREISYFGVKVAIIEPG 206
Cdd:cd05353 154 nfgqANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA 191
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 27-210 1.98e-06

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 48.23  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVL-----AACLtEKGAEQLRNKTSDrLETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVIlngrdPAKL-AAAAESLKGQGLS-AHALAFDVTDHDAVRAAIDAFEAEI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   102 GNRGLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSML-PLVRKARGRVVNISS---SMGRVSLcgGGYCI 177
Cdd:PRK07523  86 GPIDI--LVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVArHMIARGAGKIINIASvqsALARPGI--APYTA 161

                        170       180       190
                 ....*....|....*....|....*....|...
gi 8567342   178 SKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK07523 162 TKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDT 194
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 32-211 4.91e-06

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


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 46.99  E-value: 4.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVIL----DVTKTESIVAATQWVKERVGNRGLw 107
Cdd:cd05373   2 AAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKavptDARDEDEVIALFDLIEEEIGPLEV- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  108 gLVNNAGICV-FAINEwLKKEDFANILDVNLLGMI----EVTLSMLPlvrKARGRVV--NISSSM-GRVSLcgGGYCISK 179
Cdd:cd05373  81 -LVYNAGANVwFPILE-TTPRVFEKVWEMAAFGGFlaarEAAKRMLA---RGRGTIIftGATASLrGRAGF--AAFAGAK 153

                       170       180       190
                ....*....|....*....|....*....|...
gi 8567342  180 YGVEAFSDSLRREISYFGVKVA-IIEPGGFRTN 211
Cdd:cd05373 154 FALRALAQSMARELGPKGIHVAhVIIDGGIDTD 186
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-211 8.80e-06

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 46.41  E-value: 8.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE-KGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRG 105
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEpTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEFGHID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   106 LwgLVNNAGICVF--AINewLKKEDFANILDVNllgmIEVTLSMLPLVRKA------RGRVVNISSSMgrvSLCGG---- 173
Cdd:PRK08993  88 I--LVNNAGLIRRedAIE--FSEKDWDDVMNLN----IKSVFFMSQAAAKHfiaqgnGGKIINIASML---SFQGGirvp 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 8567342   174 GYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTN 211
Cdd:PRK08993 157 SYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATN 194
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 30-206 1.17e-05

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 45.95  E-value: 1.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKtesiVAATQWVKERVGNRGLW-G 108
Cdd:cd08951   8 KRIFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSS----LAETRKLADQVNAIGRFdA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  109 LVNNAGIcVFAINEWLKKEDFANILDVNLLGMIEVTlsmlPLVRKARgRVVNISSSM---GRVSLCG-----------GG 174
Cdd:cd08951  84 VIHNAGI-LSGPNRKTPDTGIPAMVAVNVLAPYVLT----ALIRRPK-RLIYLSSGMhrgGNASLDDidwfnrgendsPA 157

                       170       180       190
                ....*....|....*....|....*....|..
gi 8567342  175 YCISKYGVEAFSDSLRReiSYFGVKVAIIEPG 206
Cdd:cd08951 158 YSDSKLHVLTLAAAVAR--RWKDVSSNAVHPG 187
PRK07814 PRK07814
SDR family oxidoreductase;
27-179 1.72e-05

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 45.54  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG----AEQLRnKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQldevAEQIR-AAGRRAHVVAADLAHPEATAGLAGQAVEAFG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   103 NRGLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRK--ARGRVVNISSSMGRVSLCG-GGYCISK 179
Cdd:PRK07814  87 RLDI--VVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEhsGGGSVINISSTMGRLAGRGfAAYGTAK 164
PRK06123 PRK06123
SDR family oxidoreductase;
29-212 1.77e-05

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 45.15  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEK-GAEQLRNKTSDRLETVIL---DVTKTESIVAATQWVKERVGNr 104
Cdd:PRK06123   2 RKVMIITGASRGIGAATALLAAERGYAVCLNYLRNRdAAEAVVQAIRRQGGEALAvaaDVADEADVLRLFEAVDRELGR- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   105 gLWGLVNNAGICVFAIN-EWLKKEDFANILDVNLLGMI----EVTLSMLPLVRKARGRVVNISSSMGRVSLCGG--GYCI 177
Cdd:PRK06123  81 -LDALVNNAGILEAQMRlEQMDAARLTRIFATNVVGSFlcarEAVKRMSTRHGGRGGAIVNVSSMAARLGSPGEyiDYAA 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 8567342   178 SKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNV 212
Cdd:PRK06123 160 SKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEI 194
PRK12742 PRK12742
SDR family oxidoreductase;
25-206 2.15e-05

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 45.13  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    25 SHLQDKYVFITGCDSGFGNLLARQLDRRGMRVL----------AACLTEKGAEQLRNKTSDRLETVildvtktesivaat 94
Cdd:PRK12742   2 GAFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRftyagskdaaERLAQETGATAVQTDSADRDAVI-------------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    95 qwvkERVGNRG-LWGLVNNAGICVFAINEWLKKEDFANILDVNllgmieVTLSMLPLVRKAR-----GRVVNISSSMG-R 167
Cdd:PRK12742  68 ----DVVRKSGaLDILVVNAGIAVFGDALELDADDIDRLFKIN------IHAPYHASVEAARqmpegGRIIIIGSVNGdR 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 8567342   168 VSLCGG-GYCISKYGVEAFSDSLRREISYFGVKVAIIEPG 206
Cdd:PRK12742 138 MPVAGMaAYAASKSALQGMARGLARDFGPRGITINVVQPG 177
PRK07985 PRK07985
SDR family oxidoreductase;
27-206 2.25e-05

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 45.37  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACL--TEKGAEQLRNKTSDRLETVIL---DVTKTESIVAATQWVKERV 101
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISYLpvEEEDAQDVKKIIEECGRKAVLlpgDLSDEKFARSLVHEAHKAL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   102 GNRGLWGLVNNAGICVFAINEwLKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISSSMGRVSLCGGGYCISKYG 181
Cdd:PRK07985 127 GGLDIMALVAGKQVAIPDIAD-LTSEQFQKTFAINVFALFWLTQEAIPLLPKGASIITTSSIQAYQPSPHLLDYAATKAA 205

                        170       180
                 ....*....|....*....|....*
gi 8567342   182 VEAFSDSLRREISYFGVKVAIIEPG 206
Cdd:PRK07985 206 ILNYSRGLAKQVAEKGIRVNIVAPG 230
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 32-210 2.28e-05

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: 44.87  E-value: 2.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRN---KTSDRLETVILDVTKTESIVAATQWVKERVGnrGLWG 108
Cdd:cd05365   2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAaiqQAGGQAIGLECNVTSEQDLEAVVKATVSQFG--GITI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  109 LVNNAGicvfaineW---------LKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISSSMGRV--SLCGGGYCI 177
Cdd:cd05365  80 LVNNAG--------GggpkpfdmpMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSEnkNVRIAAYGS 151

                       170       180       190
                ....*....|....*....|....*....|...
gi 8567342  178 SKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd05365 152 SKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKT 184
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-211 2.53e-05

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 44.90  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG-AEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRG 105
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEAPeTQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGHID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   106 LwgLVNNAGIcvfainewLKKEDFANILDVNLLGMIEVTLSMLPLVRKA----------RGRVVNISSSMgrvSLCGG-- 173
Cdd:PRK12481  86 I--LINNAGI--------IRRQDLLEFGNKDWDDVININQKTVFFLSQAvakqfvkqgnGGKIINIASML---SFQGGir 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 8567342   174 --GYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTN 211
Cdd:PRK12481 153 vpSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATD 192
PRK09186 PRK09186
flagellin modification protein A; Provisional
 27-166 2.59e-05

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 44.98  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQL-----RNKTSDRLETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELleslgKEFKSKKLSLVELDITDQESLEEFLSKSAEKY 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8567342   102 GNrgLWGLVNNA-------GICVFAInewlKKEDFANILDVNLLGMIEVTLSMLP-LVRKARGRVVNISSSMG 166
Cdd:PRK09186  82 GK--IDGAVNCAyprnkdyGKKFFDV----SLDDFNENLSLHLGSSFLFSQQFAKyFKKQGGGNLVNISSIYG 148
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 27-225 2.61e-05

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: 44.84  E-value: 2.61e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQlrnkTSDRLETVILDVTKT----------ESIVAATQw 96
Cdd:cd08936   8 LANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDR----AVATLQGEGLSVTGTvchvgkaedrERLVATAV- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   97 vkERVGnrGLWGLVNNAGICVFAINEWLKKED-FANILDVNLLGMIEVTLSMLPLVRK-ARGRVVNISSSMGRVSLCG-G 173
Cdd:cd08936  83 --NLHG--GVDILVSNAAVNPFFGNILDSTEEvWDKILDVNVKATALMTKAVVPEMEKrGGGSVVIVSSVAAFHPFPGlG 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 8567342  174 GYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVS-----NYERLSHSIEKL 225
Cdd:cd08936 159 PYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSsalwmDKAVEESMKETL 215
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 26-211 2.62e-05

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 44.84  E-value: 2.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVI---LDVTKTESIVAATQWVKERVG 102
Cdd:PRK06113   8 RLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFacrCDITSEQELSALADFALSKLG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   103 nrGLWGLVNNA---GICVFAinewLKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVV-NISSSMGR-VSLCGGGYCI 177
Cdd:PRK06113  88 --KVDILVNNAgggGPKPFD----MPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVIlTITSMAAEnKNINMTSYAS 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 8567342   178 SKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTN 211
Cdd:PRK06113 162 SKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTD 195
PRK07062 PRK07062
SDR family oxidoreductase;
27-163 3.11e-05

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 44.65  E-value: 3.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVlAACLTE----KGAE-QLRNKTSD-RLETVILDVTKTESIVAATQWVKER 100
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASV-AICGRDeerlASAEaRLREKFPGaRLLAARCDVLDEADVAAFAAAVEAR 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8567342   101 VGnrGLWGLVNNAG---ICVFAINEwlkKEDFANILDVNLLGMIEVTLSMLPLVRKA-RGRVVNISS 163
Cdd:PRK07062  85 FG--GVDMLVNNAGqgrVSTFADTT---DDAWRDELELKYFSVINPTRAFLPLLRASaAASIVCVNS 146
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 1-219 6.68e-05

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 44.09  E-value: 6.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342     1 MWLYLVALVGLWTLLRFFRE--RQV-VSHLQ-----DKY---VFITGCDSGFGNLLARQLDRRGMR-VLAACLTEK---G 65
Cdd:PLN02780  14 LWLLVLFVLGSLSILKFFFTilNWVyVYFLRpaknlKKYgswALVTGPTDGIGKGFAFQLARKGLNlVLVARNPDKlkdV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    66 AEQLRNKTSD-RLETVILDVTKteSIVAATQWVKERVGNRGLWGLVNNAGI---CVFAINEwLKKEDFANILDVNLLGMI 141
Cdd:PLN02780  94 SDSIQSKYSKtQIKTVVVDFSG--DIDEGVKRIKETIEGLDVGVLINNVGVsypYARFFHE-VDEELLKNLIKVNVEGTT 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   142 EVTLSMLP-LVRKARGRVVNISSSMGRVSLCGGGYCI---SKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNVSNYER 217
Cdd:PLN02780 171 KVTQAVLPgMLKRKKGAIINIGSGAAIVIPSDPLYAVyaaTKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMASIRR 250


                 ..
gi 8567342   218 LS 219
Cdd:PLN02780 251 SS 252
PRK07856 PRK07856
SDR family oxidoreductase;
27-210 7.69e-05

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 43.38  E-value: 7.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNktsdrLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETVDGRP-----AEFHAADVRDPDQVAALVDAIVERHG--RL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   107 WGLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRK--ARGRVVNISS-SMGRVSLCGGGYCISKYGVE 183
Cdd:PRK07856  77 DVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQqpGGGSIVNIGSvSGRRPSPGTAAYGAAKAGLL 156

                        170       180
                 ....*....|....*....|....*....
gi 8567342   184 AFSDSLRREisyFG--VKVAIIEPGGFRT 210
Cdd:PRK07856 157 NLTRSLAVE---WApkVRVNAVVVGLVRT 182
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-205 8.31e-05

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 43.62  E-value: 8.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVL-----AACLTEKGAEQLRNKTSdRLETVILDVTKTESivaATQWVKERV 101
Cdd:PRK07792  10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVvndvaSALDASDVLDEIRAAGA-KAVAVAGDISQRAT---ADELVATAV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   102 GNRGLWGLVNNAGIC----VFAINEwlkkEDFANILDVNLLGMIEVTLSMLPLVR-KAR-------GRVVNISSSMGRVS 169
Cdd:PRK07792  86 GLGGLDIVVNNAGITrdrmLFNMSD----EEWDAVIAVHLRGHFLLTRNAAAYWRaKAKaaggpvyGRIVNTSSEAGLVG 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 8567342   170 LCG-GGYCISKYGVEAFSDSLRREISYFGVKVAIIEP 205
Cdd:PRK07792 162 PVGqANYGAAKAGITALTLSAARALGRYGVRANAICP 198
PRK08177 PRK08177
SDR family oxidoreductase;
30-210 1.34e-04

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 42.32  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETviLDVTKTESIVAATQWVKERVGNRglwgL 109
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIEK--LDMNDPASLDQLLQRLQGQRFDL----L 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   110 VNNAGICVFAiNEWLKKEDFANILDV---NLLGMIEVTLSMLPLVRKARGRVVNISSSMGRVSLCGGG----YCISKYGV 182
Cdd:PRK08177  76 FVNAGISGPA-HQSAADATAAEIGQLfltNAIAPIRLARRLLGQVRPGQGVLAFMSSQLGSVELPDGGemplYKASKAAL 154

                        170       180
                 ....*....|....*....|....*...
gi 8567342   183 EAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK08177 155 NSMTRSFVAELGEPTLTVLSMHPGWVKT 182
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 34-163 1.35e-04

human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like SDRs; Classical SDR-like subgroup containing human DHRS-12/FLJ13639, the 36K protein of zebrafish CNS myelin, and related proteins. DHRS-12/FLJ13639 is expressed in neurons and oligodendrocytes in the human cerebral cortex. Proteins in this subgroup share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 42.58  E-value: 1.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   34 ITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRN---KTSDRLETV--ILDVTKTESIVAATQWVKERvgNRGLWG 108
Cdd:cd09808   6 ITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKeieTESGNQNIFlhIVDMSDPKQVWEFVEEFKEE--GKKLHV 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 8567342  109 LVNNAGiCVFAINEwLKKEDFANILDVNLLGMIEVTLSMLPLVRKARG-RVVNISS 163
Cdd:cd09808  84 LINNAG-CMVNKRE-LTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDpRVITVSS 137
PRK07035 PRK07035
SDR family oxidoreductase;
27-210 1.59e-04

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 42.31  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV------LAACltEKGAEQLRNKtSDRLETVILDVTKTESIVAATQWVKER 100
Cdd:PRK07035   6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVivssrkLDGC--QAVADAIVAA-GGKAEALACHIGEMEQIDALFAHIRER 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   101 VGNrgLWGLVNNAgicvfAINEWlkkedFANILD-----------VNLLGMIEVTLSMLPLVRK-ARGRVVNISSSMGRV 168
Cdd:PRK07035  83 HGR--LDILVNNA-----AANPY-----FGHILDtdlgafqktvdVNIRGYFFMSVEAGKLMKEqGGGSIVNVASVNGVS 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 8567342   169 SLCGGG-YCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:PRK07035 151 PGDFQGiYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDT 193
PRK08278 PRK08278
SDR family oxidoreductase;
27-181 1.72e-04

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 42.58  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMR-VLAACLTEK----------GAEQLRNKTSDRLeTVILDVTKTESIVAATQ 95
Cdd:PRK08278   4 LSGKTLFITGASRGIGLAIALRAARDGANiVIAAKTAEPhpklpgtihtAAEEIEAAGGQAL-PLVGDVRDEDQVAAAVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    96 WVKERVGnrGLWGLVNNAGicvfAIN----EWLKKEDFANILDVNLLGMIEVTLSMLPLVRKAR-GRVVNISS--SMGRV 168
Cdd:PRK08278  83 KAVERFG--GIDICVNNAS----AINltgtEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSEnPHILTLSPplNLDPK 156

                        170
                 ....*....|....
gi 8567342   169 SLCG-GGYCISKYG 181
Cdd:PRK08278 157 WFAPhTAYTMAKYG 170
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 29-167 1.90e-04

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 42.58  E-value: 1.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQ-----LRNKTSDRLETVILDVTKTESIVAATQWVKERvgN 103
Cdd:cd09809   1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAavsriLEEWHKARVEAMTLDLASLRSVQRFAEAFKAK--N 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8567342  104 RGLWGLVNNAGicVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRK-ARGRVVNISSSMGR 167
Cdd:cd09809  79 SPLHVLVCNAA--VFALPWTLTEDGLETTFQVNHLGHFYLVQLLEDVLRRsAPARVIVVSSESHR 141
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 27-212 1.96e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 42.48  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV---------LAACLTEKGAeqLRNKTSDRLETVilDVTKTESIVAATQWV 97
Cdd:PRK05875   5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVmivgrnpdkLAAAAEEIEA--LKGAGAVRYEPA--DVTDEDQVARAVDAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    98 KERVGnrGLWGLVNNAG--ICVFAINEwLKKEDFANILDVNLLG-MIEVTLSMLPLVRKARGRVVNISS-SMGRVSLCGG 173
Cdd:PRK05875  81 TAWHG--RLHGVVHCAGgsETIGPITQ-IDSDAWRRTVDLNVNGtMYVLKHAARELVRGGGGSFVGISSiAASNTHRWFG 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 8567342   174 GYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRTNV 212
Cdd:PRK05875 158 AYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDL 196
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 27-210 2.35e-04

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: 42.05  E-value: 2.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVL----AACLTEKG-AEQLRnKTSDRLETVILDVTKTESIVAATQWVKERV 101
Cdd:cd09763   1 LSGKIALVTGASRGIGRGIALQLGEAGATVYitgrTILPQLPGtAEEIE-ARGGKCIPVRCDHSDDDEVEALFERVAREQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  102 GNRgLWGLVNNA----GICVFAINE---WLKKEDFANILDVNLLGMIEVTLSMLPLVRKA-RGRVVNISSSMGRVSLCGG 173
Cdd:cd09763  80 QGR-LDILVNNAyaavQLILVGVAKpfwEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAgKGLIVIISSTGGLEYLFNV 158

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 8567342  174 GYCISKYGVEAFSDSLRREISYFGVKVAIIEPGGFRT 210
Cdd:cd09763 159 AYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRT 195
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 27-206 4.77e-04

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: 41.12  E-value: 4.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKgaEQLRNKTSDRLET-----VIL--DVTKTESIVAATQWVKE 99
Cdd:cd05355  24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEE--EDDAEETKKLIEEegrkcLLIpgDLGDESFCRDLVKEVVK 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342  100 RVGnrGLWGLVNNAG--ICVFAINEwLKKEDFANILDVNLLGMIEVTLSMLPLVRKArGRVVNISSSM---GRVSLCggG 174
Cdd:cd05355 102 EFG--KLDILVNNAAyqHPQESIED-ITTEQLEKTFRTNIFSMFYLTKAALPHLKKG-SSIINTTSVTaykGSPHLL--D 175

                       170       180       190
                ....*....|....*....|....*....|..
gi 8567342  175 YCISKYGVEAFSDSLRREISYFGVKVAIIEPG 206
Cdd:cd05355 176 YAATKGAIVAFTRGLSLQLAEKGIRVNAVAPG 207
PRK09730 PRK09730
SDR family oxidoreductase;
34-206 9.43e-04

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 40.22  E-value: 9.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    34 ITGCDSGFGNLLARQLDRRGMRVLAACL-TEKGAEQLRNK---TSDRLETVILDVTKTESIVAATQWVKERVGNrgLWGL 109
Cdd:PRK09730   6 VTGGSRGIGRATALLLAQEGYTVAVNYQqNLHAAQEVVNLitqAGGKAFVLQADISDENQVVAMFTAIDQHDEP--LAAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   110 VNNAGIcVF--AINEWLKKEDFANILDVNLLGMI----EVTLSMLPLVRKARGRVVNISSSMGRVSLCGG--GYCISKYG 181
Cdd:PRK09730  84 VNNAGI-LFtqCTVENLTAERINRVLSTNVTGYFlccrEAVKRMALKHGGSGGAIVNVSSAASRLGAPGEyvDYAASKGA 162

                        170       180
                 ....*....|....*....|....*
gi 8567342   182 VEAFSDSLRREISYFGVKVAIIEPG 206
Cdd:PRK09730 163 IDTLTTGLSLEVAAQGIRVNCVRPG 187
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 30-206 9.74e-04

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 40.05  E-value: 9.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    30 KYVFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEQLRNKTSD------RLETVILDVTKTESIVAATQWVKERVGN 103
Cdd:PRK07677   2 KVVIITGGSSGMGKAMAKRFAEEGANVV---ITGRTKEKLEEAKLEieqfpgQVLTVQMDVRNPEDVQKMVEQIDEKFGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   104 rgLWGLVNNAG---ICV---FAINEWlkkedfANILDVNLLGMIEVT--LSMLPLVRKARGRVVNISSSMGRVSlcGGGY 175
Cdd:PRK07677  79 --IDALINNAAgnfICPaedLSVNGW------NSVIDIVLNGTFYCSqaVGKYWIEKGIKGNIINMVATYAWDA--GPGV 148

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 8567342   176 CIS---KYGVEAFSDSLRREISY-FGVKVAIIEPG 206
Cdd:PRK07677 149 IHSaaaKAGVLAMTRTLAVEWGRkYGIRVNAIAPG 183
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 76-206 1.78e-03

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 39.38  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    76 RLETVILDVTKTESIVAATQWVKERVGNRGLwgLVNNAGICVfainewlkKEDFANI----LD----VNLLGMIEVTLSM 147
Cdd:PRK12859  69 KVSSMELDLTQNDAPKELLNKVTEQLGYPHI--LVNNAAYST--------NNDFSNLtaeeLDkhymVNVRATTLLSSQF 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8567342   148 LPLVRKARG-RVVNISSSMGRVSLCGG-GYCISKYGVEAFSDSLRREISYFGVKVAIIEPG 206
Cdd:PRK12859 139 ARGFDKKSGgRIINMTSGQFQGPMVGElAYAATKGAIDALTSSLAAEVAHLGITVNAINPG 199
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 32-173 1.82e-03

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 39.42  E-value: 1.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   32 VFITGCDSGFGNLLARQLDRRGM-RVLAACLTEKGAEQLRNKT---SDRLETVILDVTKTESIvaaTQWVKE-RVGNRGL 106
Cdd:cd09810   4 VVITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQEVgmpKDSYSVLHCDLASLDSV---RQFVDNfRRTGRPL 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8567342  107 WGLVNNAGICVFAINEWLKKED-FANILDVNLLGMIEVTLSMLPLVRKARG---RVVNISSSMGRVSLCGG 173
Cdd:cd09810  81 DALVCNAAVYLPTAKEPRFTADgFELTVGVNHLGHFLLTNLLLEDLQRSENaspRIVIVGSITHNPNTLAG 151
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 27-206 3.70e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 38.40  E-value: 3.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFgNL-LARQLDRRGMRV------------LAACLTEKGAEQLrnktsdrleTVILDVTKTESIVAA 93
Cdd:PRK07576   7 FAGKNVVVVGGTSGI-NLgIAQAFARAGANVavasrsqekvdaAVAQLQQAGPEGL---------GVSADVRDYAAVEAA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    94 TQWVKERVGNRGLwgLVNNAGICVFAINEWLKKEDFANILDVNLLGMIEVTLSMLPLVRKARGRVVNISSSMGRVSLCGG 173
Cdd:PRK07576  77 FAQIADEFGPIDV--LVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPGASIIQISAPQAFVPMPMQ 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 8567342   174 GY-CISKYGVEAFSDSLRREISYFGVKVAIIEPG 206
Cdd:PRK07576 155 AHvCAAKAGVDMLTRTLALEWGPEGIRVNSIVPG 188
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-237 4.03e-03

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 38.16  E-value: 4.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVL--AACLTEKGAEQLRNKTSDRLETVIL--DVTKTEsivAATQWVKERVG 102
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVvnAKKRAEEMNETLKMVKENGGEGIGVlaDVSTRE---GCETLAKATID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342   103 N-RGLWGLVNNAGICVFAIneWLKKED--FANILDVNLLGMIEVTLSMLPLVRKArGRVVNISSSMGRVSLCG-GGYCIS 178
Cdd:PRK06077  81 RyGVADILVNNAGLGLFSP--FLNVDDklIDKHISTDFKSVIYCSQELAKEMREG-GAIVNIASVAGIRPAYGlSIYGAM 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 8567342   179 KYGVEAFSDSLRREISYfGVKVAIIEPGGFRTnvsnyeRLSHSIEKLWDQTSSEVKEVY 237
Cdd:PRK06077 158 KAAVINLTKYLALELAP-KIRVNAIAPGFVKT------KLGESLFKVLGMSEKEFAEKF 209
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-163 4.21e-03

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 38.66  E-value: 4.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567342    27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLaaCLTEKGAEQLRNKTSDRL--ETVILDVTKTESIVAATQWVKERVGnr 104
Cdd:PRK08261 208 LAGKVALVTGAARGIGAAIAEVLARDGAHVV--CLDVPAAGEALAAVANRVggTALALDITAPDAPARIAEHLAERHG-- 283

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8567342   105 GLWGLVNNAGIcvfainewLKKEDFAN--------ILDVNLLGMIEVTLSML-PLVRKARGRVVNISS 163
Cdd:PRK08261 284 GLDIVVHNAGI--------TRDKTLANmdearwdsVLAVNLLAPLRITEALLaAGALGDGGRIVGVSS 343
 
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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