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Conserved domains on  [gi|165377241|ref|NP_536684|]
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retinol dehydrogenase 16 precursor [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; ...
 30-306 1.55e-145

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: 410.90  E-value: 1.55e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE--KGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLW 107
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 108 GLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRMSFF-GGGYCISKYGVEAF 186
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 187 SDSLRRELSYFGVKVAIIEPGGFKTCVT-SSDRLSSNTKMIWDKASSEVKEIYGEKFLLFYLKNLNELDKRCNKDLSVVT 265
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITgNSELWEKQAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 165377241 266 DCMEHALTACHPRTRYSAGWDAKFLFLPLSYLPTFLVDALL 306
Cdd:cd09805  241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 30-306 1.55e-145

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: 410.90  E-value: 1.55e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE--KGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLW 107
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 108 GLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRMSFF-GGGYCISKYGVEAF 186
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 187 SDSLRRELSYFGVKVAIIEPGGFKTCVT-SSDRLSSNTKMIWDKASSEVKEIYGEKFLLFYLKNLNELDKRCNKDLSVVT 265
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITgNSELWEKQAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 165377241 266 DCMEHALTACHPRTRYSAGWDAKFLFLPLSYLPTFLVDALL 306
Cdd:cd09805  241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
27-306 1.21e-51

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 170.82  E-value: 1.21e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRN---KTSDRLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAelrAAGARVEVVALDVTDPDAVAALAEAVLARFG- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 rGLWGLVNNAGISTPsGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKA-RGRVVNVSSVMGRMSF-FGGGYCISKY 181
Cdd:COG0300   82 -PIDVLVNNAGVGGG-GPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARgRGRIVNVSSVAGLRGLpGMAAYAASKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 182 GVEAFSDSLRRELSYFGVKVAIIEPGGFKTcvtssdRLSSNTKMIWDKASSEVKEiygekfllfylknlneldkrcnkdl 261
Cdd:COG0300  160 ALEGFSESLRAELAPTGVRVTAVCPGPVDT------PFTARAGAPAGRPLLSPEE------------------------- 208

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 165377241 262 svVTDCMEHALTacHPRTRYSAGWDAKFLFLPLSYLPTfLVDALL 306
Cdd:COG0300  209 --VARAILRALE--RGRAEVYVGWDARLLARLLRLLPR-LFDRLL 248
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 30-211 1.38e-48

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 160.86  E-value: 1.38e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLT----EKGAEELRNkTSDRLETVILDVTKTESIVAATQWVKERVGnrG 105
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSeeklEAVAKELGA-LGGKALFIQGDVTDRAQVKALVEQAVERLG--R 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  106 LWGLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSFFGGG-YCISKYGV 183
Cdd:pfam00106  78 LDILVNNAGI-TGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPYPGGSaYSASKAAV 156

                         170       180
                  ....*....|....*....|....*...
gi 165377241  184 EAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:pfam00106 157 IGFTRSLALELAPHGIRVNAVAPGGVDT 184
PRK06182 PRK06182
short chain dehydrogenase; Validated
 28-312 1.16e-43

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 150.88  E-value: 1.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAAClteKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLw 107
Cdd:PRK06182   2 QKKVALVTGASSGIGKATARRLAAQGYTVYGAA---RRVDKMEDLASLGVHPLSLDVTDEASIKAAVDTIIAEEGRIDV- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 108 gLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRM-SFFGGGYCISKYGVEA 185
Cdd:PRK06182  78 -LVNNAGYGS-YGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIyTPLGAWYHATKFALEG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 186 FSDSLRRELSYFGVKVAIIEPGGFKT--CVTSSDRL---SSNT--KMIWDKASSEVKEIYGEKFLlfylknlneldkrcn 258
Cdd:PRK06182 156 FSDALRLEVAPFGIDVVVIEPGGIKTewGDIAADHLlktSGNGayAEQAQAVAASMRSTYGSGRL--------------- 220

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 165377241 259 KDLSVVTDCMEHALTACHPRTRYSAGWDAKFLFLPLSYLPTFLVDALLyWTSMK 312
Cdd:PRK06182 221 SDPSVIADAISKAVTARRPKTRYAVGFGAKPLIFLRRILPDRAFDRLI-MSATR 273
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 32-224 2.95e-26

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: 103.83  E-value: 2.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241   32 VFITGCDSGFGNLLARQLDRRGMRVLAACLT-EKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKERVGnrGLW 107
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSsEEGAEEVVEELKAlgvKALGVVLDVSDREDVKAVVEEIEEELG--TID 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  108 GLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFFG-GGYCISKYGVEA 185
Cdd:TIGR01830  79 ILVNNAGI-TRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRsGRIINISSVVGLMGNAGqANYAASKAGVIG 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 165377241  186 FSDSLRRELSYFGVKVAIIEPGGFKTCVTssDRLSSNTK 224
Cdd:TIGR01830 158 FTKSLAKELASRNITVNAVAPGFIDTDMT--DKLSEKVK 194
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 30-306 1.55e-145

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: 410.90  E-value: 1.55e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE--KGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLW 107
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 108 GLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRMSFF-GGGYCISKYGVEAF 186
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 187 SDSLRRELSYFGVKVAIIEPGGFKTCVT-SSDRLSSNTKMIWDKASSEVKEIYGEKFLLFYLKNLNELDKRCNKDLSVVT 265
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITgNSELWEKQAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 165377241 266 DCMEHALTACHPRTRYSAGWDAKFLFLPLSYLPTFLVDALL 306
Cdd:cd09805  241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 30-288 1.38e-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: 1.38e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGLWGL 109
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFG--RIDVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 110 VNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSF-FGGGYCISKYGVEAFS 187
Cdd:cd05374   79 VNNAGYGL-FGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGsGRIVNVSSVAGLVPTpFLGPYCASKAALEALS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 188 DSLRRELSYFGVKVAIIEPGGFKTcvtssdRLSSNTkMIWDKASSEVKEiygekfllfYLKNLNELDKRCNKDLSV---- 263
Cdd:cd05374  158 ESLRLELAPFGIKVTIIEPGPVRT------GFADNA-AGSALEDPEISP---------YAPERKEIKENAAGVGSNpgdp 221

                        250       260
                 ....*....|....*....|....*..
gi 165377241 264 --VTDCMEHALTACHPRTRYSAGWDAK 288
Cdd:cd05374  222 ekVADVIVKALTSESPPLRYFLGSDAL 248
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
27-306 1.21e-51

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 170.82  E-value: 1.21e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRN---KTSDRLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAelrAAGARVEVVALDVTDPDAVAALAEAVLARFG- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 rGLWGLVNNAGISTPsGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKA-RGRVVNVSSVMGRMSF-FGGGYCISKY 181
Cdd:COG0300   82 -PIDVLVNNAGVGGG-GPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARgRGRIVNVSSVAGLRGLpGMAAYAASKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 182 GVEAFSDSLRRELSYFGVKVAIIEPGGFKTcvtssdRLSSNTKMIWDKASSEVKEiygekfllfylknlneldkrcnkdl 261
Cdd:COG0300  160 ALEGFSESLRAELAPTGVRVTAVCPGPVDT------PFTARAGAPAGRPLLSPEE------------------------- 208

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 165377241 262 svVTDCMEHALTacHPRTRYSAGWDAKFLFLPLSYLPTfLVDALL 306
Cdd:COG0300  209 --VARAILRALE--RGRAEVYVGWDARLLARLLRLLPR-LFDRLL 248
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 28-211 1.07e-50

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: 168.05  E-value: 1.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGLW 107
Cdd:COG4221    4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFG--RLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 108 GLVNNAGISTPsGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSF-FGGGYCISKYGVEA 185
Cdd:COG4221   82 VLVNNAGVALL-GPLEELDPEDWDRMIDVNVKGVLYVTRAALPaMRARGSGHIVNISSIAGLRPYpGGAVYAATKAAVRG 160

                        170       180
                 ....*....|....*....|....*.
gi 165377241 186 FSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:COG4221  161 LSESLRAELRPTGIRVTVIEPGAVDT 186
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 30-211 1.38e-48

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 160.86  E-value: 1.38e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241   30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLT----EKGAEELRNkTSDRLETVILDVTKTESIVAATQWVKERVGnrG 105
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSeeklEAVAKELGA-LGGKALFIQGDVTDRAQVKALVEQAVERLG--R 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  106 LWGLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSFFGGG-YCISKYGV 183
Cdd:pfam00106  78 LDILVNNAGI-TGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPYPGGSaYSASKAAV 156

                         170       180
                  ....*....|....*....|....*...
gi 165377241  184 EAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:pfam00106 157 IGFTRSLALELAPHGIRVNAVAPGGVDT 184
PRK06182 PRK06182
short chain dehydrogenase; Validated
 28-312 1.16e-43

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 150.88  E-value: 1.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAAClteKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLw 107
Cdd:PRK06182   2 QKKVALVTGASSGIGKATARRLAAQGYTVYGAA---RRVDKMEDLASLGVHPLSLDVTDEASIKAAVDTIIAEEGRIDV- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 108 gLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRM-SFFGGGYCISKYGVEA 185
Cdd:PRK06182  78 -LVNNAGYGS-YGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIyTPLGAWYHATKFALEG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 186 FSDSLRRELSYFGVKVAIIEPGGFKT--CVTSSDRL---SSNT--KMIWDKASSEVKEIYGEKFLlfylknlneldkrcn 258
Cdd:PRK06182 156 FSDALRLEVAPFGIDVVVIEPGGIKTewGDIAADHLlktSGNGayAEQAQAVAASMRSTYGSGRL--------------- 220

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 165377241 259 KDLSVVTDCMEHALTACHPRTRYSAGWDAKFLFLPLSYLPTFLVDALLyWTSMK 312
Cdd:PRK06182 221 SDPSVIADAISKAVTARRPKTRYAVGFGAKPLIFLRRILPDRAFDRLI-MSATR 273
PRK08017 PRK08017
SDR family oxidoreductase;
30-308 1.09e-40

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 142.53  E-value: 1.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAAClteKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRgLWGL 109
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAAC---RKPDDVARMNSLGFTGILLDLDDPESVERAADEVIALTDNR-LYGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 110 VNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVR-KARGRVVNVSSVMGRMSFFG-GGYCISKYGVEAFS 187
Cdd:PRK08017  79 FNNAGFGV-YGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLpHGEGRIVMTSSVMGLISTPGrGAYAASKYALEAWS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 188 DSLRRELSYFGVKVAIIEPGGFKTcvtssdRLSSNtkmiwdkasseVKEIYGEKfllfYLKNLNeLDKRCNKDLSVVTDC 267
Cdd:PRK08017 158 DALRMELRHSGIKVSLIEPGPIRT------RFTDN-----------VNQTQSDK----PVENPG-IAARFTLGPEAVVPK 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 165377241 268 MEHALTACHPRTRYSAGWDAKFLFLPLSYLPTFLVDALLYW 308
Cdd:PRK08017 216 LRHALESPKPKLRYPVTLVTHAVMVLKRLLPGRMMDKILRG 256
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 33-211 9.76e-40

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 140.44  E-value: 9.76e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  33 FITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGLWGLVNN 112
Cdd:PRK06180   8 LITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFG--PIDVLVNN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 113 AGI----STPSGPNEWMKKQdfarvLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFFG-GGYCISKYGVEAF 186
Cdd:PRK06180  86 AGYghegAIEESPLAEMRRQ-----FEVNVFGAVAMTKAVLPGMRARRrGHIVNITSMGGLITMPGiGYYCGSKFALEGI 160

                        170       180
                 ....*....|....*....|....*
gi 165377241 187 SDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK06180 161 SESLAKEVAPFGIHVTAVEPGSFRT 185
PRK06914 PRK06914
SDR family oxidoreductase;
30-298 3.09e-39

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 139.39  E-value: 3.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKT-----SDRLETVILDVTKTESIVAATQWVKErVGNR 104
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQAtqlnlQQNIKVQQLDVTDQNSIHNFQLVLKE-IGRI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 105 GLwgLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFFG-GGYCISKYG 182
Cdd:PRK06914  83 DL--LVNNAGYAN-GGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGlSPYVSSKYA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 183 VEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSSdrlSSNTKMIWDKASSEVKEiYGEKFLLFYLKNLNELdkrcnKDLS 262
Cdd:PRK06914 160 LEGFSESLRLELKPFGIDVALIEPGSYNTNIWEV---GKQLAENQSETTSPYKE-YMKKIQKHINSGSDTF-----GNPI 230

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 165377241 263 VVTDCMEHALTACHPRTRYSAGWDAKFLFLPLSYLP 298
Cdd:PRK06914 231 DVANLIVEIAESKRPKLRYPIGKGVKLMILAKKILP 266
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 25-211 4.04e-39

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: 137.99  E-value: 4.04e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  25 SHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELR---NKTSDRLETVILDVTKTESIVAATQWVKERV 101
Cdd:COG1028    2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAaelRAAGGRALAVAADVTDEAAVEALVAAAVAAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 102 GnrGLWGLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFFG-GGYCIS 179
Cdd:COG1028   82 G--RLDILVNNAGI-TPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGgGRIVNISSIAGLRGSPGqAAYAAS 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 165377241 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:COG1028  159 KAAVVGLTRSLALELAPRGIRVNAVAPGPIDT 190
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 32-211 4.75e-39

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: 137.42  E-value: 4.75e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD--RLETVILDVTKTESIVAATQWVKERVGnrGLWGL 109
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEALggNAVAVQADVSDEEDVEALVEEALEEFG--RLDIL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 110 VNNAGISTPsGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFFG-GGYCISKYGVEAFS 187
Cdd:cd05233   79 VNNAGIARP-GPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGgGRIVNISSVAGLRPLPGqAAYAASKAALEGLT 157

                        170       180
                 ....*....|....*....|....
gi 165377241 188 DSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd05233  158 RSLALELAPYGIRVNAVAPGLVDT 181
PRK05993 PRK05993
SDR family oxidoreductase;
30-310 5.35e-39

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 138.62  E-value: 5.35e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNktsDRLETVILDVTKTESIVAATQWVKERVGNRgLWGL 109
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEA---EGLEAFQLDYAEPESIAALVAQVLELSGGR-LDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 110 VNNAGISTPSG----PNEWMKKQdfarvLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVMGRMSF-FGGGYCISKYGV 183
Cdd:PRK05993  81 FNNGAYGQPGAvedlPTEALRAQ-----FEANFFGWHDLTRRVIPVMRKqGQGRIVQCSSILGLVPMkYRGAYNASKFAI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 184 EAFSDSLRRELSYFGVKVAIIEPGGFKTCVTsSDRLSSNTKMIwDKASSEVKEiygekfllFYLKNLNELDKRCNKDLSV 263
Cdd:PRK05993 156 EGLSLTLRMELQGSGIHVSLIEPGPIETRFR-ANALAAFKRWI-DIENSVHRA--------AYQQQMARLEGGGSKSRFK 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 165377241 264 -----VTDCMEHALTACHPRTRYSAGWDAKFLFLPLSYLPTFLVDALLYWTS 310
Cdd:PRK05993 226 lgpeaVYAVLLHALTAPRPRPHYRVTTPAKQGALLKRLLPARWLYRLLRKAA 277
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 27-211 6.90e-36

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: 130.01  E-value: 6.90e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacLT-------EKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKE 99
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLV---LSarreerlEEVKSECLELGAPSPHVVPLDMSDLEDAEQVVEEALK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 100 RVGnrGLWGLVNNAGISTPSgpnEWMKK--QDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSF-FGGG 175
Cdd:cd05332   78 LFG--GLDILINNAGISMRS---LFHDTsiDVDRKIMEVNYFGPVALTKAALPhLIERSQGSIVVVSSIAGKIGVpFRTA 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 165377241 176 YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd05332  153 YAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDT 188
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 27-211 1.15e-35

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 129.16  E-value: 1.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLT-EKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASsEAGAEALVAEIGAlggKALAVQGDVSDAESVERAVDEAKAEFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 nrGLWGLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFFGGG-YCISK 180
Cdd:PRK05557  83 --GVDILVNNAGI-TRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRsGRIINISSVVGLMGNPGQAnYAASK 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 165377241 181 YGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK05557 160 AGVIGFTKSLARELASRGITVNAVAPGFIET 190
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 32-211 1.20e-34

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: 125.87  E-value: 1.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRG-MRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLWGLV 110
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSAATELAALGASHSRLHILELDVTDEIAESAEAVAERLGDAGLDVLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 111 NNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKA-RGRVVNVSSVMGRMSFFGGG----YCISKYGVEA 185
Cdd:cd05325   81 NNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGaRAKIINISSRVGSIGDNTSGgwysYRASKAALNM 160

                        170       180
                 ....*....|....*....|....*.
gi 165377241 186 FSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd05325  161 LTKSLAVELKRDGITVVSLHPGWVRT 186
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 33-211 3.34e-33

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 123.22  E-value: 3.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  33 FITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNrgLWGLVNN 112
Cdd:PRK08263   7 FITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGR--LDIVVNN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 113 AGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFFGGG-YCISKYGVEAFSDSL 190
Cdd:PRK08263  85 AGYGL-FGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRsGHIIQISSIGGISAFPMSGiYHASKWALEGMSEAL 163

                        170       180
                 ....*....|....*....|.
gi 165377241 191 RRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK08263 164 AQEVAEFGIKVTLVEPGGYST 184
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 28-306 8.86e-33

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 121.93  E-value: 8.86e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAAclTEKGAeelRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLw 107
Cdd:PRK06179   3 NSKVALVTGASSGIGRATAEKLARAGYRVFGT--SRNPA---RAAPIPGVELLELDVTDDASVQAAVDEVIARAGRIDV- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 108 gLVNNAGISTPSGPNEWMKKQDfARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGrmsF----FGGGYCISKYG 182
Cdd:PRK06179  77 -LVNNAGVGLAGAAEESSIAQA-QALFDTNVFGILRMTRAVLPHMRAQGsGRIINISSVLG---FlpapYMALYAASKHA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 183 VEAFSDSLRRELSYFGVKVAIIEPGGFKTcvtssdRLSSNTKmiwdKASSEVKEiygekfllfYLKNLNELDKRCNK--- 259
Cdd:PRK06179 152 VEGYSESLDHEVRQFGIRVSLVEPAYTKT------NFDANAP----EPDSPLAE---------YDRERAVVSKAVAKavk 212

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 165377241 260 ---DLSVVTDCMEHALTACHPRTRYSAGWDAKFLFLPLSYLPTFLVDALL 306
Cdd:PRK06179 213 kadAPEVVADTVVKAALGPWPKMRYTAGGQASLLSKLRRFMPAGAVDKSL 262
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 30-211 6.11e-32

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: 118.49  E-value: 6.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRG--MRVLAACLTEKG---AEELRNKTSDrLETVILDVTKTESIVAATQWVKERVGnr 104
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGpgTVILTARDVERGqaaVEKLRAEGLS-VRFHQLDVTDDASIEAAADFVEEKYG-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 105 GLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSffgGGYCISKYGV 183
Cdd:cd05324   78 GLDILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPaGRIVNVSSGLGSLT---SAYGVSKAAL 154

                        170       180
                 ....*....|....*....|....*...
gi 165377241 184 EAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd05324  155 NALTRILAKELKETGIKVNACCPGWVKT 182
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 27-211 1.03e-31

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


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 118.41  E-value: 1.03e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNK---TSDRLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:cd08934    1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADEleaEGGKALVLELDVTDEQQVDAAVERTVEALG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 rGLWGLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVR-KARGRVVNVSSVMGRMSFFG-GGYCISKY 181
Cdd:cd08934   80 -RLDILVNNAGIML-LGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLlRNKGTIVNISSVAGRVAVRNsAVYNATKF 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 165377241 182 GVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd08934  158 GVNAFSEGLRQEVTERGVRVVVIEPGTVDT 187
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
27-207 1.13e-31

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 118.34  E-value: 1.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTS---DRLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRaagGEARVLVFDVSDEAAVRALIEAAVEAFG- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 rGLWGLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFFGGG-YCISKY 181
Cdd:PRK05653  82 -ALDILVNNAGI-TRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARyGRIVNISSVSGVTGNPGQTnYSAAKA 159

                        170       180
                 ....*....|....*....|....*.
gi 165377241 182 GVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK05653 160 GVIGFTKALALELASRGITVNAVAPG 185
PRK12826 PRK12826
SDR family oxidoreductase;
27-211 1.26e-30

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 115.78  E-value: 1.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:PRK12826   4 LEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAaggKARARQVDVRDRAALKAAVAAGVEDFG- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 rGLWGLVNNAGIStPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSFFGG--GYCISK 180
Cdd:PRK12826  83 -RLDILVANAGIF-PLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPaLIRAGGGRIVLTSSVAGPRVGYPGlaHYAASK 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 165377241 181 YGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK12826 161 AGLVGFTRALALELAARNITVNSVHPGGVDT 191
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
30-207 1.75e-30

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 115.25  E-value: 1.75e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGA----EELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRG 105
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCakdwFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGPVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 106 LwgLVNNAGISTPSGPNEwMKKQDFARVLDVNLLGMIEVTLSMLPLVR-KARGRVVNVSSVMGRMSFFGG-GYCISKYGV 183
Cdd:PRK12824  83 I--LVNNAGITRDSVFKR-MSHQEWNDVINTNLNSVFNVTQPLFAAMCeQGYGRIINISSVNGLKGQFGQtNYSAAKAGM 159

                        170       180
                 ....*....|....*....|....
gi 165377241 184 EAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK12824 160 IGFTKALASEGARYGITVNCIAPG 183
PRK05693 PRK05693
SDR family oxidoreductase;
32-211 3.34e-30

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 115.27  E-value: 3.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGMRVLAaclTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGLWGLVN 111
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWA---TARKAEDVEALAAAGFTAVQLDVNDGAALARLAEELEAEHG--GLDVLIN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 112 NAGIST--P--SGPNEWMKKQdfarvLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRMSF-FGGGYCISKYGVEAF 186
Cdd:PRK05693  79 NAGYGAmgPllDGGVEAMRRQ-----FETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTpFAGAYCASKAAVHAL 153

                        170       180
                 ....*....|....*....|....*
gi 165377241 187 SDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK05693 154 SDALRLELAPFGVQVMEVQPGAIAS 178
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 27-203 3.34e-30

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 115.84  E-value: 3.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNK--TSDRLETVILDVTKTESIVAATQWVKERVGnr 104
Cdd:PRK05872   7 LAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAElgGDDRVLTVVADVTDLAAMQAAAEEAVERFG-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 105 GLWGLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMgrmSFFGGG----YCISK 180
Cdd:PRK05872  85 GIDVVVANAGI-ASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSLA---AFAAAPgmaaYCASK 160

                        170       180
                 ....*....|....*....|...
gi 165377241 181 YGVEAFSDSLRRELSYFGVKVAI 203
Cdd:PRK05872 161 AGVEAFANALRLEVAHHGVTVGS 183
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 29-211 3.79e-30

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: 114.27  E-value: 3.79e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE----KGAEELR---NKTSDRLETVILDVTKTESIVAATQWVKERV 101
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSEskleEAVEEIEaeaNASGQKVSYISADLSDYEEVEQAFAQAVEKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 102 GNRGLwgLVNNAGISTPsGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFFG-GGYCIS 179
Cdd:cd08939   81 GPPDL--VVNCAGISIP-GLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRpGHIVFVSSQAALVGIYGySAYCPS 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 165377241 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd08939  158 KFALRGLAESLRQELKPYNIRVSVVYPPDTDT 189
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 30-207 2.18e-29

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: 112.37  E-value: 2.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLaacLT-------EKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLI---LTgrraerlQELADELGAKFPVKVLPLQLDVSDRESIEAALENLPEEFR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 NrgLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSFFGGG-YCISK 180
Cdd:cd05346   78 D--IDILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPiMIARNQGHIINLGSIAGRYPYAGGNvYCATK 155

                        170       180
                 ....*....|....*....|....*..
gi 165377241 181 YGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:cd05346  156 AAVRQFSLNLRKDLIGTGIRVTNIEPG 182
PRK06482 PRK06482
SDR family oxidoreductase;
33-216 5.81e-29

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 112.13  E-value: 5.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  33 FITGCDSGFGNLLARQLDRRGMRVlAACLTEKGA-EELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLwgLVN 111
Cdd:PRK06482   6 FITGASSGFGRGMTERLLARGDRV-AATVRRPDAlDDLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAALGRIDV--VVS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 112 NAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFFGGG-YCISKYGVEAFSDS 189
Cdd:PRK06482  83 NAGYGL-FGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGgGRIVQVSSEGGQIAYPGFSlYHATKWGIEGFVEA 161

                        170       180
                 ....*....|....*....|....*..
gi 165377241 190 LRRELSYFGVKVAIIEPGGFKTCVTSS 216
Cdd:PRK06482 162 VAQEVAPFGIEFTIVEPGPARTNFGAG 188
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 30-211 8.02e-29

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: 110.72  E-value: 8.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGA---EELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAaetVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFG--PV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 WGLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFFG-GGYCISKYGVE 184
Cdd:cd05333   79 DILVNNAGI-TRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRsGRIINISSVVGLIGNPGqANYAASKAGVI 157

                        170       180
                 ....*....|....*....|....*..
gi 165377241 185 AFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd05333  158 GFTKSLAKELASRGITVNAVAPGFIDT 184
PRK09291 PRK09291
SDR family oxidoreductase;
30-235 1.10e-28

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 110.86  E-value: 1.10e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDR---LETVILDVTKTESIVAATQW---Vkervgn 103
Cdd:PRK09291   3 KTILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRglaLRVEKLDLTDAIDRAQAAEWdvdV------ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 rglwgLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSF-FGGGYCISKY 181
Cdd:PRK09291  77 -----LLNNAGIGE-AGAVVDIPVELVRELFETNVFGPLELTQGFVRkMVARGKGKVVFTSSMAGLITGpFTGAYCASKH 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 165377241 182 GVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVtsSDRLSSNTKMIWDKASSEVK 235
Cdd:PRK09291 151 ALEAIAEAMHAELKPFGIQVATVNPGPYLTGF--NDTMAETPKRWYDPARNFTD 202
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 27-233 1.37e-28

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: 110.19  E-value: 1.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGM-RVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKErvgnrg 105
Cdd:cd05354    1 IKDKTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAAQAKD------ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 106 LWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKA-RGRVVNVSSVMGRMSFFG-GGYCISKYGV 183
Cdd:cd05354   75 VDVVINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANgGGAIVNLNSVASLKNFPAmGTYSASKSAA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 165377241 184 EAFSDSLRRELSYFGVKVAIIEPGGFKTcvtssdRLSSNTKMiwDKASSE 233
Cdd:cd05354  155 YSLTQGLRAELAAQGTLVLSVHPGPIDT------RMAAGAGG--PKESPE 196
PRK05650 PRK05650
SDR family oxidoreductase;
32-218 5.16e-28

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 109.36  E-value: 5.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKERVGnrGLWG 108
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREaggDGFYQRCDVRDYSQLTALAQACEEKWG--GIDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 109 LVNNAGISTPSGPNEwMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSF-FGGGYCISKYGVEAF 186
Cdd:PRK05650  81 IVNNAGVASGGFFEE-LSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKsGRIVNIASMAGLMQGpAMSSYNVAKAGVVAL 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 165377241 187 SDSLRRELSYFGVKVAIIEPGGFKTCVTSSDR 218
Cdd:PRK05650 160 SETLLVELADDEIGVHVVCPSFFQTNLLDSFR 191
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 32-211 1.62e-26

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


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 104.39  E-value: 1.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG----AEELRNKTSDRLeTVILDVTKTESIVAATQWVKERVGNRGLW 107
Cdd:cd05360    3 VVITGASSGIGRATALAFAERGAKVVLAARSAEAlhelAREVRELGGEAI-AVVADVADAAQVERAADTAVERFGRIDTW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 108 glVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSF-FGGGYCISKYGVEA 185
Cdd:cd05360   82 --VNNAGVAV-FGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPhLRRRGGGALINVGSLLGYRSApLQAAYSASKHAVRG 158

                        170       180
                 ....*....|....*....|....*...
gi 165377241 186 FSDSLRRELSYFGVKVAI--IEPGGFKT 211
Cdd:cd05360  159 FTESLRAELAHDGAPISVtlVQPTAMNT 186
PRK09072 PRK09072
SDR family oxidoreductase;
26-206 2.25e-26

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 104.64  E-value: 2.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTS--DRLETVILDVTKTESIVAATQWVKErvgN 103
Cdd:PRK09072   2 DLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPypGRHRWVVADLTSEAGREAVLARARE---M 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 RGLWGLVNNAGISTPSgpneWMKKQD---FARVLDVNLLGMIEVTLSMLPLVRKA-RGRVVNVSSVMGRMSFFG-GGYCI 178
Cdd:PRK09072  79 GGINVLINNAGVNHFA----LLEDQDpeaIERLLALNLTAPMQLTRALLPLLRAQpSAMVVNVGSTFGSIGYPGyASYCA 154

                        170       180
                 ....*....|....*....|....*...
gi 165377241 179 SKYGVEAFSDSLRRELSYFGVKVAIIEP 206
Cdd:PRK09072 155 SKFALRGFSEALRRELADTGVRVLYLAP 182
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 32-224 2.95e-26

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: 103.83  E-value: 2.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241   32 VFITGCDSGFGNLLARQLDRRGMRVLAACLT-EKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKERVGnrGLW 107
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSsEEGAEEVVEELKAlgvKALGVVLDVSDREDVKAVVEEIEEELG--TID 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  108 GLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFFG-GGYCISKYGVEA 185
Cdd:TIGR01830  79 ILVNNAGI-TRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRsGRIINISSVVGLMGNAGqANYAASKAGVIG 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 165377241  186 FSDSLRRELSYFGVKVAIIEPGGFKTCVTssDRLSSNTK 224
Cdd:TIGR01830 158 FTKSLAKELASRNITVNAVAPGFIDTDMT--DKLSEKVK 194
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 30-211 5.77e-26

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: 102.97  E-value: 5.77e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGLWGL 109
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFG--GLDAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 110 VNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTL-SMLPLVRKARGRVVNVSSVMGRMSFFGG-GYCISKYGVEAFS 187
Cdd:cd08929   79 VNNAGVGV-MKPVEELTPEEWRLVLDTNLTGAFYCIHkAAPALLRRGGGTIVNVGSLAGKNAFKGGaAYNASKFGLLGLS 157

                        170       180
                 ....*....|....*....|....
gi 165377241 188 DSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd08929  158 EAAMLDLREANIRVVNVMPGSVDT 181
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 20-207 1.39e-25

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 102.83  E-value: 1.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  20 ERQVVSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLET-VILDVTKTESIVAATQWVK 98
Cdd:PRK12829   2 AIDLLKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPGAKVTaTVADVADPAQVERVFDTAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  99 ERVGnrGLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKA-RGRVV-NVSSVMGRMSF-FGGG 175
Cdd:PRK12829  82 ERFG--GLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASgHGGVIiALSSVAGRLGYpGRTP 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 165377241 176 YCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK12829 160 YAASKWAVVGLVKSLAIELGPLGIRVNAILPG 191
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 30-207 1.71e-25

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: 102.54  E-value: 1.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDR---RGMRVLAAC--LTEKG--AEELRNKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLASdpsKRFKVYATMrdLKKKGrlWEAAGALAGGTLETLQLDVCDSKSVAAAVERVTERHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 NRglwgLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSF-FGGGYCISK 180
Cdd:cd09806   81 DV----LVCNAGVGL-LGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGsGRILVTSSVGGLQGLpFNDVYCASK 155

                        170       180
                 ....*....|....*....|....*..
gi 165377241 181 YGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:cd09806  156 FALEGLCESLAVQLLPFNVHLSLIECG 182
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-207 2.35e-25

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 101.87  E-value: 2.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACL-TEKGAEELRNK---TSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK12825   4 LMGRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEAveaLGRRAQAVQADVTDKAALEAAVAAAVERFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 nrGLWGLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFFG-GGYCISK 180
Cdd:PRK12825  84 --RIDILVNNAGI-FEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRgGRIVNISSVAGLPGWPGrSNYAAAK 160

                        170       180
                 ....*....|....*....|....*..
gi 165377241 181 YGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK12825 161 AGLVGLTKALARELAEYGITVNMVAPG 187
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 38-211 3.04e-25

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: 100.97  E-value: 3.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241   38 DSGFGNLLARQLDRRGMRVLAACLTEKGAEELRnKTSDRLETVIL--DVTKTESIVAATQWVKERVGnrGLWGLVNNAGI 115
Cdd:pfam13561   5 ESGIGWAIARALAEEGAEVVLTDLNEALAKRVE-ELAEELGAAVLpcDVTDEEQVEALVAAAVEKFG--RLDILVNNAGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  116 STP-SGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLvRKARGRVVNVSSVMGRMSFFGGG-YCISKYGVEAFSDSLRRE 193
Cdd:pfam13561  82 APKlKGPFLDTSREDFDRALDVNLYSLFLLAKAALPL-MKEGGSIVNLSSIGAERVVPNYNaYGAAKAALEALTRYLAVE 160

                         170
                  ....*....|....*...
gi 165377241  194 LSYFGVKVAIIEPGGFKT 211
Cdd:pfam13561 161 LGPRGIRVNAISPGPIKT 178
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 30-224 4.77e-25

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: 100.13  E-value: 4.77e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRnKTSDRLETVILDVTKTESIVAATQWVKERVGnrGLWGL 109
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALS-ASGGDVEAVPYDARDPEDARALVDALRDRFG--RIDVL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 110 VNNAGISTPSGPNEWMKKQDfARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSF-FGGGYCISKYGVEAFS 187
Cdd:cd08932   78 VHNAGIGRPTTLREGSDAEL-EAHFSINVIAPAELTRALLPaLREAGSGRVVFLNSLSGKRVLaGNAGYSASKFALRALA 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 165377241 188 DSLRRELSYFGVKVAIIEPGGFKTCVTSSDRLSSNTK 224
Cdd:cd08932  157 HALRQEGWDHGVRVSAVCPGFVDTPMAQGLTLVGAFP 193
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 32-219 4.95e-25

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: 100.78  E-value: 4.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRN---KTSDRLETVILDVTKTESIVAATQWVKERVGNRGLwg 108
Cdd:cd05339    2 VLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANnvrKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTI-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 109 LVNNAGISTPSGPNEwMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSFFGGG-YCISKYGVEAF 186
Cdd:cd05339   80 LINNAGVVSGKKLLE-LPDEEIEKTFEVNTLAHFWTTKAFLPdMLERNHGHIVTIASVAGLISPAGLAdYCASKAAAVGF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 165377241 187 SDSLRRELSYF---GVKVAIIEP-----GGFKTCVTSSDRL 219
Cdd:cd05339  159 HESLRLELKAYgkpGIKTTLVCPyfintGMFQGVKTPRPLL 199
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 27-211 1.72e-24

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 101.15  E-value: 1.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG----AEELRNKTSDRLeTVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK07109   6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGlealAAEIRAAGGEAL-AVVADVADAEAVQAAADRAEEELG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 NRGLWglVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSF-FGGGYCISK 180
Cdd:PRK07109  85 PIDTW--VNNAMVTV-FGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRhMRPRDRGAIIQVGSALAYRSIpLQSAYCAAK 161

                        170       180       190
                 ....*....|....*....|....*....|...
gi 165377241 181 YGVEAFSDSLRRELSYFG--VKVAIIEPGGFKT 211
Cdd:PRK07109 162 HAIRGFTDSLRCELLHDGspVSVTMVQPPAVNT 194
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 27-227 5.78e-24

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 98.47  E-value: 5.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEElrnkTSDRLETVI---LDVTKTESIVAATQWVkervgn 103
Cdd:PRK07825   3 LRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKE----TAAELGLVVggpLDVTDPASFAAFLDAV------ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 RGLWG----LVNNAGIsTPSGPnewMKKQDFA---RVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSFFGGG 175
Cdd:PRK07825  73 EADLGpidvLVNNAGV-MPVGP---FLDEPDAvtrRILDVNVYGVILGSKLAAPrMVPRGRGHVVNVASLAGKIPVPGMA 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 165377241 176 -YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTcvtssdRLSSNTKMIW 227
Cdd:PRK07825 149 tYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNT------ELIAGTGGAK 195
PRK07326 PRK07326
SDR family oxidoreductase;
27-211 7.52e-24

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 97.39  E-value: 7.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVIL--DVTKTESIVAATQWVKERVGnr 104
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGNVLGLaaDVRDEADVQRAVDAIVAAFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 105 GLWGLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRMSFFGG-GYCISKYGV 183
Cdd:PRK07326  82 GLDVLIANAGVGH-FAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGTNFFAGGaAYNASKFGL 160

                        170       180
                 ....*....|....*....|....*...
gi 165377241 184 EAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK07326 161 VGFSEAAMLDLRQYGIKVSTIMPGSVAT 188
PRK08264 PRK08264
SDR family oxidoreductase;
26-207 9.07e-24

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 97.27  E-value: 9.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  26 HLQDKYVFITGCDSGFGNLLARQLDRRG-MRVLAACltekgaeelRNKTS-----DRLETVILDVTKTESIVAATqwvkE 99
Cdd:PRK08264   3 DIKGKVVLVTGANRGIGRAFVEQLLARGaAKVYAAA---------RDPESvtdlgPRVVPLQLDVTDPASVAAAA----E 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 100 RVGNRGLwgLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSF-FGGGYC 177
Cdd:PRK08264  70 AASDVTI--LVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPvLAANGGGAIVNVLSVLSWVNFpNLGTYS 147

                        170       180       190
                 ....*....|....*....|....*....|
gi 165377241 178 ISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK08264 148 ASKAAAWSLTQALRAELAPQGTRVLGVHPG 177
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 27-237 9.94e-24

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: 96.99  E-value: 9.94e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDrLETVILDVTKTESIVAATQWVKERvgNRGL 106
Cdd:cd05370    3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN-IHTIVLDVGDAESVEALAEALLSE--YPNL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 WGLVNNAGISTP---SGPNEWMkkQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSFFGGG-YCISKY 181
Cdd:cd05370   80 DILINNAGIQRPidlRDPASDL--DKADTEIDTNLIGPIRLIKAFLPhLKKQPEATIVNVSSGLAFVPMAANPvYCATKA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 165377241 182 GVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSSDR---LSSNTKM--------IWDKASSEVKEI 237
Cdd:cd05370  158 ALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRnpdGGTPRKMpldefvdeVVAGLERGREEI 224
PRK06181 PRK06181
SDR family oxidoreductase;
29-211 1.13e-23

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 97.36  E-value: 1.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG----AEELRNKTSDRLeTVILDVTKTESIVAATQWVKERVGnr 104
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRlaslAQELADHGGEAL-VVPTDVSDAEACERLIEAAVARFG-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 105 GLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRMSFFG-GGYCISKYGV 183
Cdd:PRK06181  78 GIDILVNNAGITMWSRFDELTDLSVFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTrSGYAASKHAL 157

                        170       180
                 ....*....|....*....|....*...
gi 165377241 184 EAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK06181 158 HGFFDSLRIELADDGVAVTVVCPGFVAT 185
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 30-233 4.67e-23

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: 95.45  E-value: 4.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEK--GAEEL-RNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENpgAAAELqAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFG--RV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 WGLVNNAGISTPSGPNEWMK-KQDFARVLDVNLLGMIEVTLSMLPLVRKAR----GRVVNVSSVMGRMSF-FGGGYCISK 180
Cdd:cd05323   79 DILINNAGILDEKSYLFAGKlPPPWEKTIDVNLTGVINTTYLALHYMDKNKggkgGVIVNIGSVAGLYPApQFPVYSASK 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 165377241 181 YGVEAFSDSLRRELSY-FGVKVAIIEPGgfktcVTSSDRLSSNTKMIWDKASSE 233
Cdd:cd05323  159 HGVVGFTRSLADLLEYkTGVRVNAICPG-----FTNTPLLPDLVAKEAEMLPSA 207
PRK07832 PRK07832
SDR family oxidoreductase;
30-211 6.74e-23

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 95.49  E-value: 6.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEELRNKTSD---RLETVI----LDVTKTESIVAATQWVKERVG 102
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELF---LTDRDADGLAQTVADaraLGGTVPehraLDISDYDAVAAFAADIHAAHG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 NRGLwgLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGR-VVNVSSVMGRMSF-FGGGYCIS 179
Cdd:PRK07832  78 SMDV--VMNIAGISA-WGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPpMVAAGRGGhLVNVSSAAGLVALpWHAAYSAS 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 165377241 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK07832 155 KFGLRGLSEVLRFDLARHGIGVSVVVPGAVKT 186
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 24-207 2.62e-22

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 93.50  E-value: 2.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  24 VSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKER 100
Cdd:PRK12939   2 ASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAaggRAHAIAADLADPASVQRFFDAAAAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 101 VGnrGLWGLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVR-KARGRVVNVSSVMGRMSFFGGG-YCI 178
Cdd:PRK12939  82 LG--GLDGLVNNAGI-TNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRdSGRGRIVNLASDTALWGAPKLGaYVA 158

                        170       180
                 ....*....|....*....|....*....
gi 165377241 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK12939 159 SKGAVIGMTRSLARELGGRGITVNAIAPG 187
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 27-211 2.85e-22

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


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 93.22  E-value: 2.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:cd05341    3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFG--RL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 WGLVNNAGISTPsGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKA-RGRVVNVSSVMGRMSFFG-GGYCISKYGVE 184
Cdd:cd05341   81 DVLVNNAGILTG-GTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAgGGSIINMSSIEGLVGDPAlAAYNASKGAVR 159

                        170       180
                 ....*....|....*....|....*....
gi 165377241 185 AFSDSLRREL--SYFGVKVAIIEPGGFKT 211
Cdd:cd05341  160 GLTKSAALECatQGYGIRVNSVHPGYIYT 188
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 27-205 3.01e-22

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: 93.30  E-value: 3.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAcltekG--AEELRNKTSDR--LETVILDVTKTESIVAATQWVKERVG 102
Cdd:COG3967    3 LTGNTILITGGTSGIGLALAKRLHARGNTVIIT-----GrrEEKLEEAAAANpgLHTIVLDVADPASIAALAEQVTAEFP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 nrGLWGLVNNAGISTP----SGPNEWmkkQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSFFG-GGY 176
Cdd:COG3967   78 --DLNVLINNAGIMRAedllDEAEDL---ADAEREITTNLLGPIRLTAAFLPhLKAQPEAAIVNVSSGLAFVPLAVtPTY 152

                        170       180
                 ....*....|....*....|....*....
gi 165377241 177 CISKYGVEAFSDSLRRELSYFGVKVaiIE 205
Cdd:COG3967  153 SATKAALHSYTQSLRHQLKDTSVKV--IE 179
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 27-214 7.09e-22

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: 92.42  E-value: 7.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKERVGN 103
Cdd:cd05347    3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKegvEATAFTCDVSDEEAIKAAVEAIEEDFGK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 RGLwgLVNNAGISTPSgPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMgrmSFFGG----GYCI 178
Cdd:cd05347   83 IDI--LVNNAGIIRRH-PAEEFPEAEWRDVIDVNLNGVFFVSQAVARhMIKQGHGKIINICSLL---SELGGppvpAYAA 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 165377241 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVT 214
Cdd:cd05347  157 SKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMT 192
FabG-like PRK07231
SDR family oxidoreductase;
27-211 9.99e-22

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 91.82  E-value: 9.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG----AEELRnkTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAaervAAEIL--AGGRAIAVAADVSDEADVEAAVAAALERFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 nrGLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMG-RMSFFGGGYCISK 180
Cdd:PRK07231  81 --SVDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGgGAIVNVASTAGlRPRPGLGWYNASK 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 165377241 181 YGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK07231 159 GAVITLTKALAAELGPDKIRVNAVAPVVVET 189
PRK06484 PRK06484
short chain dehydrogenase; Validated
 32-212 1.86e-21

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 94.53  E-value: 1.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLwgLVN 111
Cdd:PRK06484 272 VAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRLDV--LVN 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 112 NAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKArGRVVNVSSVMGRMSFFG-GGYCISKYGVEAFSDSL 190
Cdd:PRK06484 350 NAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG-GVIVNLGSIASLLALPPrNAYCASKAAVTMLSRSL 428

                        170       180
                 ....*....|....*....|..
gi 165377241 191 RRELSYFGVKVAIIEPGGFKTC 212
Cdd:PRK06484 429 ACEWAPAGIRVNTVAPGYIETP 450
PRK07024 PRK07024
SDR family oxidoreductase;
32-214 5.77e-21

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 89.99  E-value: 5.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGMRV-LAACLTE---KGAEELRNktSDRLETVILDVTKTESIVAATQWVKERVGNRGLw 107
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLgLVARRTDalqAFAARLPK--AARVSVYAADVRDADALAAAAADFIAAHGLPDV- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 108 gLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSML-PLVRKARGRVVNVSSVMGRMSFFGGG-YCISKYGVEA 185
Cdd:PRK07024  82 -VIANAGISVGTLTEEREDLAVFREVMDTNYFGMVATFQPFIaPMRAARRGTLVGIASVAGVRGLPGAGaYSASKAAAIK 160

                        170       180
                 ....*....|....*....|....*....
gi 165377241 186 FSDSLRRELSYFGVKVAIIEPGGFKTCVT 214
Cdd:PRK07024 161 YLESLRVELRPAGVRVVTIAPGYIRTPMT 189
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 29-211 7.39e-21

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: 89.98  E-value: 7.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNK-----TSDRLETVILDVTKTESIVAATQWVKERVgn 103
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEikketGNAKVEVIQLDLSSLASVRQFAEEFLARF-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 RGLWGLVNNAGISTPSgpnEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFFGGG------- 175
Cdd:cd05327   79 PRLDILINNAGIMAPP---RRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASApSRIVNVSSIAHRAGPIDFNdldlenn 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 165377241 176 --------YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd05327  156 keyspykaYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRT 199
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 27-236 7.57e-21

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: 89.78  E-value: 7.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVlaaCLTEKGAEEL---------RNKTSDRLETVILDVTKTESIVAATQWV 97
Cdd:cd05364    1 LSGKVAIITGSSSGIGAGTAILFARLGARL---ALTGRDAERLeetrqsclqAGVSEKKILLVVADLTEEEGQDRIISTT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  98 KERVGNRGLwgLVNNAGISTPsGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRMSFFGG-GY 176
Cdd:cd05364   78 LAKFGRLDI--LVNNAGILAK-GGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGRSFPGVlYY 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSSDRLSSNTkmiWDKASSEVKE 236
Cdd:cd05364  155 CISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRMGMPEEQ---YIKFLSRAKE 211
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 30-224 1.40e-20

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: 88.28  E-value: 1.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKT-SDRLETVILDVTKTESIVAATQWVKERVGNRgLWG 108
Cdd:cd08931    1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELgAENVVAGALDVTDRAAWAAALADFAAATGGR-LDA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 109 LVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARG-RVVNVSSVMGrmsFFG----GGYCISKYGV 183
Cdd:cd08931   80 LFNNAGVGR-GGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGaRVINTASSSA---IYGqpdlAVYSATKFAV 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 165377241 184 EAFSDSLRRELSYFGVKVAIIEPGGFKT-CVTSSDRLSSNTK 224
Cdd:cd08931  156 RGLTEALDVEWARHGIRVADVWPWFVDTpILTKGETGAAPKK 197
PRK08219 PRK08219
SDR family oxidoreductase;
34-215 2.13e-20

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 87.68  E-value: 2.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  34 ITGCDSGFGNLLARQLDRRgMRVLAACLTEKGAEELRNkTSDRLETVILDVTKTESIVAATQWVkERVGNrglwgLVNNA 113
Cdd:PRK08219   8 ITGASRGIGAAIARELAPT-HTLLLGGRPAERLDELAA-ELPGATPFPVDLTDPEAIAAAVEQL-GRLDV-----LVHNA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 114 GISTPsGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRMSFFGGG-YCISKYGVEAFSDSLRR 192
Cdd:PRK08219  80 GVADL-GPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRANPGWGsYAASKFALRALADALRE 158

                        170       180
                 ....*....|....*....|...
gi 165377241 193 ElsyfgvkvaiiEPGgfKTCVTS 215
Cdd:PRK08219 159 E-----------EPG--NVRVTS 168
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-211 2.79e-20

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 87.98  E-value: 2.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAC-LTEKGAEELRNKTSDRLETVIL---DVTKTESIVAATQWVKERVG 102
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYdINEEAAQELLEEIKEEGGDAIAvkaDVSSEEDVENLVEQIVEKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 nrGLWGLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSF-FGGGYCISK 180
Cdd:PRK05565  83 --KIDILVNNAGISN-FGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPyMIKRKSGVIVNISSIWGLIGAsCEVLYSASK 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 165377241 181 YGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK05565 160 GAVNAFTKALAKELAPSGIRVNAVAPGAIDT 190
PRK07454 PRK07454
SDR family oxidoreductase;
32-228 4.10e-20

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 87.32  E-value: 4.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGMRVL----AACLTEKGAEELRNKTSdRLETVILDVTKTESIVAATQWVKERVGNRGLw 107
Cdd:PRK07454   9 ALITGASSGIGKATALAFAKAGWDLAlvarSQDALEALAAELRSTGV-KAAAYSIDLSNPEAIAPGIAELLEQFGCPDV- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 108 gLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFFG-GGYCISKYGVEA 185
Cdd:PRK07454  87 -LINNAGMAY-TGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGgGLIINVSSIAARNAFPQwGAYCVSKAALAA 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 165377241 186 FSDSLRRELSYFGVKVAIIEPGgfktcvtssdrlSSNTKmIWD 228
Cdd:PRK07454 165 FTKCLAEEERSHGIRVCTITLG------------AVNTP-LWD 194
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 32-207 9.09e-20

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 86.73  E-value: 9.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLwgLVN 111
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDV--LVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 112 NAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSFFGGG-YCISKYGVEAFSDS 189
Cdd:PRK10538  81 NAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPgMVERNHGHIINIGSTAGSWPYAGGNvYGATKAFVRQFSLN 160

                        170
                 ....*....|....*...
gi 165377241 190 LRRELSYFGVKVAIIEPG 207
Cdd:PRK10538 161 LRTDLHGTAVRVTDIEPG 178
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 27-211 1.36e-19

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: 86.28  E-value: 1.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEK-GAEEL-RNKTSDRLETVIL--DVTKTESIVAATQWVKERVG 102
Cdd:cd05358    1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEdAAEEVvEEIKAVGGKAIAVqaDVSKEEDVVALFQSAIKEFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 NRGLWglVNNAGISTPSGPNEwMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR--GRVVNVSSVMGRMSFFG-GGYCIS 179
Cdd:cd05358   81 TLDIL--VNNAGLQGDASSHE-MTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKikGKIINMSSVHEKIPWPGhVNYAAS 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 165377241 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd05358  158 KGGVKMMTKTLAQEYAPKGIRVNAIAPGAINT 189
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 27-211 7.07e-19

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: 84.04  E-value: 7.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVI-LDVTKTESIVAATQWVKERVGNrg 105
Cdd:cd05326    2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFVhCDVTVEADVRAAVDTAVARFGR-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 106 LWGLVNNAGI-STPSGPNEWMKKQDFARVLDVNL----LGMIEVTLSMLPlvrKARGRVVNVSSVMGRMSFFGG-GYCIS 179
Cdd:cd05326   80 LDIMFNNAGVlGAPCYSILETSLEEFERVLDVNVygafLGTKHAARVMIP---AKKGSIVSVASVAGVVGGLGPhAYTAS 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 165377241 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd05326  157 KHAVLGLTRSAATELGEHGIRVNCVSPYGVAT 188
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 25-226 7.64e-19

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 84.06  E-value: 7.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  25 SHLQDKYVFITGCDSGFGNLLARQLDRRGMRVlaACL---TEKGAEELRNKTSdrlETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK06463   3 MRFKGKVALITGGTRGIGRAIAEAFLREGAKV--AVLynsAENEAKELREKGV---FTIKCDVGNRDQVKKSKEVVEKEF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 102 GNRGLwgLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMG-----RMSFFggg 175
Cdd:PRK06463  78 GRVDV--LVNNAGIMY-LMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKnGAIVNIASNAGigtaaEGTTF--- 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 165377241 176 YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSSDRLSSNTKMI 226
Cdd:PRK06463 152 YAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLSGKSQEEAEKL 202
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 24-211 1.42e-18

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 83.13  E-value: 1.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  24 VSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEK-GAEELRNKTSDRLETVIL---DVTKTESivaATQWVKE 99
Cdd:PRK12935   1 MVQLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKeAAENLVNELGKEGHDVYAvqaDVSKVED---ANRLVEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 100 RVGNRG-LWGLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFFG-GGY 176
Cdd:PRK12935  78 AVNHFGkVDILVNNAGI-TRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEeGRIISISSIIGQAGGFGqTNY 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 165377241 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK12935 157 SAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDT 191
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 27-211 1.44e-18

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: 83.34  E-value: 1.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD-----RLETVILDVTKTESIVAATQWVKERV 101
Cdd:cd05330    1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEiapdaEVLLIKADVSDEAQVEAYVDATVEQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 102 GNrgLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMG-RMSFFGGGYCIS 179
Cdd:cd05330   81 GR--IDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGsGMIVNTASVGGiRGVGNQSGYAAA 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 165377241 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd05330  159 KHGVVGLTRNSAVEYGQYGIRINAIAPGAILT 190
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 30-207 2.48e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 82.46  E-value: 2.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDrlETVILDVTKTESIVAAtqwvkerVGNRGLW-G 108
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGC--EPLRLDVGDDAAIRAA-------LAAAGAFdG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 109 LVNNAGISTPSGPNEwMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKAR-GRVVNVSSVMGRMSF-FGGGYCISKYGVEA 185
Cdd:PRK07060  81 LVNCAGIASLESALD-MTAEGFDRVMAVNARGAALVARHVARaMIAAGRgGSIVNVSSQAALVGLpDHLAYCASKAALDA 159

                        170       180
                 ....*....|....*....|..
gi 165377241 186 FSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK07060 160 ITRVLCVELGPHGIRVNSVNPT 181
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 29-234 2.79e-18

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


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 82.27  E-value: 2.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE----KGAEELRNKTSDRLETVILDVTKTESIVAAtqwVKERVGNR 104
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQekldAVAKEIEEKYGVETKTIAADFSAGDDIYER---IEKELEGL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 105 GLWGLVNNAGISTP-SGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSF-FGGGYCISKY 181
Cdd:cd05356   78 DIGILVNNVGISHSiPEYFLETPEDELQDIINVNVMATLKMTRLILPgMVKRKKGAIVNISSFAGLIPTpLLATYSASKA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 165377241 182 GVEAFSDSLRRELSYFGVKVAIIEPGGfktcVTSsdRLSSNTKMIWDKASSEV 234
Cdd:cd05356  158 FLDFFSRALYEEYKSQGIDVQSLLPYL----VAT--KMSKIRKSSLFVPSPEQ 204
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 31-207 3.08e-18

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: 82.33  E-value: 3.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  31 YVFITGCDSGFGNLLARQLDRRGMRVLAACLTE------KGAEELRNktSDRLETVILDVTKT---ESIVAATQWV-KER 100
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARseeplqELKEELRP--GLRVTTVKADLSDAagvEQLLEAIRKLdGER 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 101 VGnrglwgLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR--GRVVNVSSVMGRMSFFG-GGYC 177
Cdd:cd05367   79 DL------LINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGlkKTVVNVSSGAAVNPFKGwGLYC 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 165377241 178 ISKYGVEAFSDSLRRELSyfGVKVAIIEPG 207
Cdd:cd05367  153 SSKAARDMFFRVLAAEEP--DVRVLSYAPG 180
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-206 3.17e-18

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 82.04  E-value: 3.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG----AEELrNKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK07666   5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENlkavAEEV-EAYGVKVVIATADVSDYEEVTAAIEQLKNELG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 NRGLwgLVNNAGISTPSGPNEwMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSFFGG-GYCISK 180
Cdd:PRK07666  84 SIDI--LINNAGISKFGKFLE-LDPAEWEKIIQVNLMGVYYATRAVLPsMIERQSGDIINISSTAGQKGAAVTsAYSASK 160

                        170       180
                 ....*....|....*....|....*.
gi 165377241 181 YGVEAFSDSLRRELSYFGVKVAIIEP 206
Cdd:PRK07666 161 FGVLGLTESLMQEVRKHNIRVTALTP 186
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 32-214 3.78e-18

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: 81.99  E-value: 3.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKERVGnrGLWG 108
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNpnpSVEVEILDVTDEERNQLVIAELEAELG--GLDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 109 LVNNAGISTPSgPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSFFGG-GYCISKYGVEAF 186
Cdd:cd05350   79 VIINAGVGKGT-SLGDLSFKAFRETIDTNLLGAAAILEAALPqFRAKGRGHLVLISSVAALRGLPGAaAYSASKAALSSL 157

                        170       180
                 ....*....|....*....|....*...
gi 165377241 187 SDSLRRELSYFGVKVAIIEPGGFKTCVT 214
Cdd:cd05350  158 AESLRYDVKKRGIRVTVINPGFIDTPLT 185
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 27-224 3.97e-18

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 81.89  E-value: 3.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV-LAACLTEKgAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrG 105
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVgLHGTRVEK-LEALAAELGERVKIFPANLSDRDEVKALGQKAEADLE--G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 106 LWGLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSML-PLVRKARGRVVNVSSVMGRMSFFG-GGYCISKYGV 183
Cdd:PRK12936  81 VDILVNNAGI-TKDGLFVRMSDEDWDSVLEVNLTATFRLTRELThPMMRRRYGRIINITSVVGVTGNPGqANYCASKAGM 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 165377241 184 EAFSDSLRRELSYFGVKVAIIEPGGFKTCVTssDRLSSNTK 224
Cdd:PRK12936 160 IGFSKSLAQEIATRNVTVNCVAPGFIESAMT--GKLNDKQK 198
PRK05855 PRK05855
SDR family oxidoreductase;
29-218 8.95e-18

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 83.49  E-value: 8.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEElrnkTSDRLE-------TVILDVTKTESIVAATQWVKERV 101
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAER----TAELIRaagavahAYRVDVSDADAMEAFAEWVRAEH 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 102 GNRGLwgLVNNAGISTpSGPNEWMKKQDFARVLDVNLLG-----------MIEvtlsmlplvRKARGRVVNVSSvmgrMS 170
Cdd:PRK05855 391 GVPDI--VVNNAGIGM-AGGFLDTSAEDWDRVLDVNLWGvihgcrlfgrqMVE---------RGTGGHIVNVAS----AA 454

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 165377241 171 FFG-----GGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSSDR 218
Cdd:PRK05855 455 AYApsrslPAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVATTR 507
PRK08589 PRK08589
SDR family oxidoreductase;
27-211 3.76e-17

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 79.82  E-value: 3.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELR--NKTSDRLETVILDVTKTESIVAATQWVKERVGNR 104
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDkiKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 105 GLwgLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRMS-FFGGGYCISKYGV 183
Cdd:PRK08589  84 DV--LFNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAAdLYRSGYNAAKGAV 161

                        170       180
                 ....*....|....*....|....*...
gi 165377241 184 EAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK08589 162 INFTKSIAIEYGRDGIRANAIAPGTIET 189
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 27-207 4.02e-17

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 79.23  E-value: 4.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDlgrRALAVPTDITDEDQCANLVALALERFG- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 rGLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRMSFFG-GGYCISKYG 182
Cdd:PRK07890  82 -RVDALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMINSMVLRHSQPKyGAYKMAKGA 160

                        170       180
                 ....*....|....*....|....*
gi 165377241 183 VEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK07890 161 LLAASQSLATELGPQGIRVNSVAPG 185
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 26-211 6.60e-17

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 78.30  E-value: 6.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEELRNKTSDRLETVI----LDVTKTESIVAATQWVKERV 101
Cdd:PRK12828   4 SLQGKVVAITGGFGGLGRATAAWLAARGARVA---LIGRGAAPLSQTLPGVPADALriggIDLVDPQAARRAVDEVNRQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 102 GnrGLWGLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSFFG-GGYCIS 179
Cdd:PRK12828  81 G--RLDALVNIAGA-FVWGTIADGDADTWDRMYGVNVKTTLNASKAALPaLTASGGGRIVNIGAGAALKAGPGmGAYAAA 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 165377241 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK12828 158 KAGVARLTEALAAELLDRGITVNAVLPSIIDT 189
PRK08267 PRK08267
SDR family oxidoreductase;
30-211 6.68e-17

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 78.83  E-value: 6.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNK-TSDRLETVILDVTKTESIVAATQWVKERVGNRgLWG 108
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAElGAGNAWTGALDVTDRAAWDAALADFAAATGGR-LDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 109 LVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARG-RVVNVSSVMGrmsFFGGG----YCISKYGV 183
Cdd:PRK08267  81 LFNNAGILR-GGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGaRVINTSSASA---IYGQPglavYSATKFAV 156

                        170       180
                 ....*....|....*....|....*...
gi 165377241 184 EAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK08267 157 RGLTEALDLEWRRHGIRVADVMPLFVDT 184
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
27-207 7.39e-17

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 78.53  E-value: 7.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFG--GI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 WGLVNNAGISTPSGPNEwMKKQDFARVLDVNLLGMI----EVTLSMLPlvRKARGRVVNVSSVMGRMsffGGG----YCI 178
Cdd:PRK07067  82 DILFNNAALFDMAPILD-ISRDSYDRLFAVNVKGLFflmqAVARHMVE--QGRGGKIINMASQAGRR---GEAlvshYCA 155

                        170       180
                 ....*....|....*....|....*....
gi 165377241 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK07067 156 TKAAVISYTQSAALALIRHGINVNAIAPG 184
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 26-237 9.32e-17

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 78.08  E-value: 9.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRvLAacLTEKGAEELRNKTSD------RLETVILDVTKTESIVAATQWVKE 99
Cdd:PRK08217   2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAK-LA--LIDLNQEKLEEAVAEcgalgtEVRGYAANVTDEEDVEATFAQIAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 100 RVGnrGLWGLVNNAGI-------STPSGP-NEWMKKQDFARVLDVNLLGMI----EVTLSMLPLVRKarGRVVNVSSV-- 165
Cdd:PRK08217  79 DFG--QLNGLINNAGIlrdgllvKAKDGKvTSKMSLEQFQSVIDVNLTGVFlcgrEAAAKMIESGSK--GVIINISSIar 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 166 ---MGRMSffgggYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSS------DRLssnTKMIWDKASSEVKE 236
Cdd:PRK08217 155 agnMGQTN-----YSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAmkpealERL---EKMIPVGRLGEPEE 226


                 .
gi 165377241 237 I 237
Cdd:PRK08217 227 I 227
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
27-226 1.19e-16

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 77.75  E-value: 1.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAC-----LTEKGAEELRNKTSDRLETViLDVTKTESIVAATQWVKERV 101
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAGCgpnspRRVKWLEDQKALGFDFIASE-GNVGDWDSTKAAFDKVKAEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 102 GNRGLwgLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSFFG-GGYCIS 179
Cdd:PRK12938  80 GEIDV--LVNNAGI-TRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDgMVERGWGRIINISSVNGQKGQFGqTNYSTA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 165377241 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSSDRLSSNTKMI 226
Cdd:PRK12938 157 KAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPDVLEKIV 203
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 29-237 4.73e-16

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: 76.16  E-value: 4.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG----AEELRnKTSDRLETVILDVTKTESIVAATQWVKERVGnr 104
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENleraASELR-AGGAGVLAVVADLTDPEDIDRLVEKAGDAFG-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 105 GLWGLVNNAGiSTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGR-----MSFFGggycI 178
Cdd:cd05344   78 RVDILVNNAG-GPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLTVKepepnLVLSN----V 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 165377241 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTcvtssDRLSSNTKMIWDKASSEVKEI 237
Cdd:cd05344  153 ARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDT-----ERVRRLLEARAEKEGISVEEA 206
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 27-207 1.35e-15

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 75.05  E-value: 1.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEElrnktsDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQH------ENYQFVPTDVSSAEEVNHTVAEIIEKFG--RI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 WGLVNNAGISTP---------SGPNEwMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSFFGGG- 175
Cdd:PRK06171  79 DGLVNNAGINIPrllvdekdpAGKYE-LNEAAFDKMFNINQKGVFLMSQAVARqMVKQHDGVIVNMSSEAGLEGSEGQSc 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 165377241 176 YCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK06171 158 YAATKAALNSFTRSWAKELGKHNIRVVGVAPG 189
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 27-216 1.54e-15

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


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 74.83  E-value: 1.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:cd08944    1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFG--GL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 WGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVR-KARGRVVNVSSVMGRMSFFG-GGYCISKYGVE 184
Cdd:cd08944   79 DLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIaRGGGSIVNLSSIAGQSGDPGyGAYGASKAAIR 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 165377241 185 AFSDSLRRELSYFGVKVAIIEPGGFKTCVTSS 216
Cdd:cd08944  159 NLTRTLAAELRHAGIRCNALAPGLIDTPLLLA 190
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 34-211 2.07e-15

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: 74.63  E-value: 2.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  34 ITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRnKTSDRLETVILDVTKTESIVAATQWVKERVGNrgLWGLVNNA 113
Cdd:cd05371    7 VTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVA-KLGDNCRFVPVDVTSEKDVKAALALAKAKFGR--LDIVVNCA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 114 GIS----TPSGPNEWMKK-QDFARVLDVNLLGmievTLSMLPLVRKA-----------RGRVVNVSSVMGrmsfFGG--- 174
Cdd:cd05371   84 GIAvaakTYNKKGQQPHSlELFQRVINVNLIG----TFNVIRLAAGAmgknepdqggeRGVIINTASVAA----FEGqig 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 165377241 175 --GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd05371  156 qaAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDT 194
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 27-207 2.16e-15

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 74.54  E-value: 2.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGA---EELRNKTSDRLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAaaaAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 rGLWGLVNNAGISTPSgPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFFG-GGYCISKY 181
Cdd:PRK12429  81 -GVDILVNNAGIQHVA-PIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGgGRIINMASVHGLVGSAGkAAYVSAKH 158

                        170       180
                 ....*....|....*....|....*.
gi 165377241 182 GVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK12429 159 GLIGLTKVVALEGATHGVTVNAICPG 184
PRK07063 PRK07063
SDR family oxidoreductase;
27-207 2.23e-15

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 74.70  E-value: 2.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV----LAACLTEKGAEELRNKTSD-RLETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK07063   5 LAGKVALVTGAAQGIGAAIARAFAREGAAValadLDAALAERAAAAIARDVAGaRVLAVPADVTDAASVAAAVAAAEEAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 102 GnrGLWGLVNNAGISTPSGPNEwMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGrMSFFGGG--YCI 178
Cdd:PRK07063  85 G--PLDVLVNNAGINVFADPLA-MTDEDWRRCFAVDLDGAWNGCRAVLPgMVERGRGSIVNIASTHA-FKIIPGCfpYPV 160

                        170       180
                 ....*....|....*....|....*....
gi 165377241 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK07063 161 AKHGLLGLTRALGIEYAARNVRVNAIAPG 189
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 28-211 2.95e-15

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: 74.11  E-value: 2.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNK--TSDRLETVIL--DVTKTESIVAATQWVKERVGN 103
Cdd:cd08933    8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESElnRAGPGSCKFVpcDVTKEEDIKTLISVTVERFGR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 rgLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRM-SFFGGGYCISKYG 182
Cdd:cd08933   88 --IDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIgQKQAAPYVATKGA 165

                        170       180
                 ....*....|....*....|....*....
gi 165377241 183 VEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd08933  166 ITAMTKALAVDESRYGVRVNCISPGNIWT 194
PRK06114 PRK06114
SDR family oxidoreductase;
27-207 2.97e-15

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 74.05  E-value: 2.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVlaACLTEKGAEELRnKTSDRLET-------VILDVTKTESIVAATQWVKE 99
Cdd:PRK06114   6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADV--ALFDLRTDDGLA-ETAEHIEAagrraiqIAADVTSKADLRAAVARTEA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 100 RVGNRGLwgLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGmieVTLS-------MLPlvrKARGRVVNVSSVMGRMSFF 172
Cdd:PRK06114  83 ELGALTL--AVNAAGIAN-ANPAEEMEEEQWQTVMDINLTG---VFLScqaearaMLE---NGGGSIVNIASMSGIIVNR 153

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 165377241 173 G---GGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK06114 154 GllqAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPG 191
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 27-206 4.62e-15

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: 73.58  E-value: 4.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:cd05345    3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFG--RL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 WGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRV-VNVSSVMG-----RMSFfgggYCISK 180
Cdd:cd05345   81 DILVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGViINIASTAGlrprpGLTW----YNASK 156

                        170       180
                 ....*....|....*....|....*.
gi 165377241 181 YGVEAFSDSLRRELSYFGVKVAIIEP 206
Cdd:cd05345  157 GWVVTATKAMAVELAPRNIRVNCLCP 182
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 33-241 4.74e-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: 73.73  E-value: 4.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  33 FITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEELRnKTSDRLETVIL-------DVTKTESIVAATQWVKERVGNRG 105
Cdd:cd08945    7 LVTGATSGIGLAIARRLGKEGLRVF---VCARGEEGLA-TTVKELREAGVeadgrtcDVRSVPEIEALVAAAVARYGPID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 106 LwgLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP---LVRKARGRVVNVSSVMGRMS-FFGGGYCISKY 181
Cdd:cd08945   83 V--LVNNAGRSG-GGATAELADELWLDVVETNLTGVFRVTKEVLKaggMLERGTGRIINIASTGGKQGvVHAAPYSASKH 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 182 GVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSSDRlsSNTKMIWDKASSEVKEIYGEK 241
Cdd:cd08945  160 GVVGFTKALGLELARTGITVNAVCPGFVETPMAASVR--EHYADIWEVSTEEAFDRITAR 217
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 27-211 5.24e-15

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: 73.08  E-value: 5.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEK-GAEELR---NKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:cd05362    1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNYASSKaAAEEVVaeiEAAGGKAIAVQADVSDPSQVARLFDAAEKAFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 nrGLWGLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRkARGRVVNVSSVMGRMSF-FGGGYCISKY 181
Cdd:cd05362   81 --GVDILVNNAGV-MLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLR-DGGRIINISSSLTAAYTpNYGAYAGSKA 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 165377241 182 GVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd05362  157 AVEAFTRVLAKELGGRGITVNAVAPGPVDT 186
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 30-211 5.72e-15

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


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 73.18  E-value: 5.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACL----TEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrG 105
Cdd:cd05366    3 KVAIITGAAQGIGRAIAERLAADGFNIVLADLnleeAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFG--S 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 106 LWGLVNNAGIStPSGPNEWMKKQDFARVLDVN----LLGMIEVTLSMLPLVRKarGRVVNVSSVMGRMSFFG-GGYCISK 180
Cdd:cd05366   81 FDVMVNNAGIA-PITPLLTITEEDLKKVYAVNvfgvLFGIQAAARQFKKLGHG--GKIINASSIAGVQGFPNlGAYSASK 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 165377241 181 YGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd05366  158 FAVRGLTQTAAQELAPKGITVNAYAPGIVKT 188
PRK07774 PRK07774
SDR family oxidoreductase;
27-207 7.01e-15

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 72.86  E-value: 7.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVI---LDVTKTESIVAATQWVKERVGn 103
Cdd:PRK07774   4 FDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIavqVDVSDPDSAKAMADATVSAFG- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 rGLWGLVNNAGISTPSGPNEWMKK--QDFARVLDVNLLGMIEVTLSMLPLVRKARG-RVVNVSSVMGRMsfFGGGYCISK 180
Cdd:PRK07774  83 -GIDYLVNNAAIYGGMKLDLLITVpwDYYKKFMSVNLDGALVCTRAVYKHMAKRGGgAIVNQSSTAAWL--YSNFYGLAK 159

                        170       180
                 ....*....|....*....|....*..
gi 165377241 181 YGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK07774 160 VGLNGLTQQLARELGGMNIRVNAIAPG 186
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 27-206 7.16e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 73.15  E-value: 7.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGL 106
Cdd:PRK06841  13 LSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRIDI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 wgLVNNAGIStPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSFFGG-GYCISKYGVE 184
Cdd:PRK06841  93 --LVNSAGVA-LLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRhMIAAGGGKIVNLASQAGVVALERHvAYCASKAGVV 169

                        170       180
                 ....*....|....*....|..
gi 165377241 185 AFSDSLRRELSYFGVKVAIIEP 206
Cdd:PRK06841 170 GMTKVLALEWGPYGITVNAISP 191
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 27-211 7.90e-15

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 72.83  E-value: 7.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLET-------VILDVTKTESIVAATQWVKE 99
Cdd:PRK12827   4 LDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAVAAGIEAaggkalgLAFDVRDFAATRAALDAGVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 100 RVGnrGLWGLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR--GRVVNVSSVMGRMSFFGG-GY 176
Cdd:PRK12827  84 EFG--RLDILVNNAGI-ATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARrgGRIVNIASVAGVRGNRGQvNY 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 165377241 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK12827 161 AASKAGLIGLTKTLANELAPRGITVNAVAPGAINT 195
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 27-236 8.85e-15

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 72.47  E-value: 8.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVL-----AACLTEKGAEELRnKTSDRLETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK12937   3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAvnyagSAAAADELVAEIE-AAGGRAIAVQADVADAAAVTRLFDAAETAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 102 GnrGLWGLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKArGRVVNVSSVMGRMSFFGGG-YCISK 180
Cdd:PRK12937  82 G--RIDVLVNNAGV-MPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQG-GRIINLSTSVIALPLPGYGpYAASK 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 165377241 181 YGVEAFSDSLRRELSYFGVKVAIIEPGgfktcvtssdrlSSNTKMIWDKASSEVKE 236
Cdd:PRK12937 158 AAVEGLVHVLANELRGRGITVNAVAPG------------PVATELFFNGKSAEQID 201
PRK06947 PRK06947
SDR family oxidoreductase;
30-236 9.85e-15

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 72.53  E-value: 9.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRV-------LAAclTEKGAEELRnKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVginyardAAA--AEETADAVR-AAGGRACVVAGDVANEADVIAMFDAVQSAFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 nrGLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR----GRVVNVSSVMGRMsffgGG--- 175
Cdd:PRK06947  80 --RLDALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRggrgGAIVNVSSIASRL----GSpne 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 165377241 176 ---YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSS-------DRLSSNTKMIWDKASSEVKE 236
Cdd:PRK06947 154 yvdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHASggqpgraARLGAQTPLGRAGEADEVAE 224
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 23-211 1.33e-14

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 72.24  E-value: 1.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  23 VVSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAE---ELRNKTSDRLETVILDVTKTESIVAATQWVKE 99
Cdd:PRK13394   1 MMSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANavaDEINKAGGKAIGVAMDVTNEDAVNAGIDKVAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 100 RVGNRGLwgLVNNAGISTPSgPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR--GRVVNVSSVMGRM-SFFGGGY 176
Cdd:PRK13394  81 RFGSVDI--LVSNAGIQIVN-PIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHSHEaSPLKSAY 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 165377241 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK13394 158 VTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRT 192
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 27-214 2.25e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 71.71  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQegiKAHAAPFNVTHKQEVEAAIEHIEKDIG- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 rGLWGLVNNAGISTPSGPNEWmKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSV---MGRMSFfgGGYCIS 179
Cdd:PRK08085  86 -PIDVLINNAGIQRRHPFTEF-PEQEWNDVIAVNQTAVFLVSQAVARyMVKRQAGKIINICSMqseLGRDTI--TPYAAS 161

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 165377241 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVT 214
Cdd:PRK08085 162 KGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMT 196
PRK07201 PRK07201
SDR family oxidoreductase;
18-204 2.50e-14

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 73.45  E-value: 2.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  18 FRERQVVSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVIL---DVTKTESIVAAT 94
Cdd:PRK07201 360 ARRRDLRGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAytcDLTDSAAVDHTV 439

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  95 QWVKERVGNRGLwgLVNNAGIST-PSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSS--VMGRMS 170
Cdd:PRK07201 440 KDILAEHGHVDY--LVNNAGRSIrRSVENSTDRFHDYERTMAVNYFGAVRLILGLLPHMRERRfGHVVNVSSigVQTNAP 517

                        170       180       190
                 ....*....|....*....|....*....|....
gi 165377241 171 FFgGGYCISKYGVEAFSDSLRRELSYFGVKVAII 204
Cdd:PRK07201 518 RF-SAYVASKAALDAFSDVAASETLSDGITFTTI 550
PRK06194 PRK06194
hypothetical protein; Provisional
 27-218 3.73e-14

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 71.59  E-value: 3.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMR-VLAACLT---EKGAEELRNKTSDRLeTVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK06194   4 FAGKVAVITGAASGFGLAFARIGAALGMKlVLADVQQdalDRAVAELRAQGAEVL-GVRTDVSDAAQVEALADAALERFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 NRGLwgLVNNAGIStpSGPNEW-MKKQDFARVLDVNLLGMIEVTLSMLPLVRKA-------RGRVVNVSSVMGRMSFFGG 174
Cdd:PRK06194  83 AVHL--LFNNAGVG--AGGLVWeNSLADWEWVLGVNLWGVIHGVRAFTPLMLAAaekdpayEGHIVNTASMAGLLAPPAM 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 165377241 175 G-YCISKYGVEAFSDSLRRELSYFG--VKVAIIEPGGFKTCVTSSDR 218
Cdd:PRK06194 159 GiYNVSKHAVVSLTETLYQDLSLVTdqVGASVLCPYFVPTGIWQSER 205
PRK05866 PRK05866
SDR family oxidoreductase;
27-201 3.88e-14

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 71.31  E-value: 3.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDR---LETVILDVTKTESIVAATQWVKERVGn 103
Cdd:PRK05866  38 LTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAggdAMAVPCDLSDLDAVDALVADVEKRIG- 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 rGLWGLVNNAGISTPSGPNEWMKK-QDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSS--VMGRMSFFGGGYCIS 179
Cdd:PRK05866 117 -GVDILINNAGRSIRRPLAESLDRwHDVERTMVLNYYAPLRLIRGLAPgMLERGDGHIINVATwgVLSEASPLFSVYNAS 195

                        170       180
                 ....*....|....*....|..
gi 165377241 180 KYGVEAFSDSLRRELSYFGVKV 201
Cdd:PRK05866 196 KAALSAVSRVIETEWGDRGVHS 217
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 27-239 4.56e-14

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 70.68  E-value: 4.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELrnktsdRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDY------PFATFVLDVSDAAAVAQVCQRLLAETG--PL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 WGLVNNAGISTPsGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMG---RMSFfgGGYCISKYG 182
Cdd:PRK08220  78 DVLVNAAGILRM-GATDSLSDEDWQQTFAVNAGGAFNLFRAVMPqFRRQRSGAIVTVGSNAAhvpRIGM--AAYGASKAA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 183 VEAFSDSLRRELSYFGVKVAIIEPGgfktcvtssdrlSSNTKM---IWDKASSEVKEIYG 239
Cdd:PRK08220 155 LTSLAKCVGLELAPYGVRCNVVSPG------------STDTDMqrtLWVDEDGEQQVIAG 202
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 32-227 5.33e-14

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


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 70.19  E-value: 5.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLtekgAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGLWGLVN 111
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIALDL----PFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHG--PIDALVN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 112 NAGISTPsGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMG---RMSFfgGGYCISKYGVEAFS 187
Cdd:cd05331   75 CAGVLRP-GATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRtGAIVTVASNAAhvpRISM--AAYGASKAALASLS 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 165377241 188 DSLRRELSYFGVKVAIIEPGgfktcvtssdrlSSNTKMIW 227
Cdd:cd05331  152 KCLGLELAPYGVRCNVVSPG------------STDTAMQR 179
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 27-211 5.84e-14

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 70.53  E-value: 5.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLT-EKGAEELRN---KTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK08936   5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSdEEEANDVAEeikKAGGEAIAVKGDVTVESDVVNLIQTAVKEFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 NRGLWglVNNAGISTPSgPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRK--ARGRVVNVSSVMGRMSF--FgGGYCI 178
Cdd:PRK08936  85 TLDVM--INNAGIENAV-PSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEhdIKGNIINMSSVHEQIPWplF-VHYAA 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 165377241 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK08936 161 SKGGVKLMTETLAMEYAPKGIRVNNIGPGAINT 193
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 27-238 7.05e-14

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


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 69.91  E-value: 7.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEELRnKTSDRLET--------VILDVTK--TESIVAATQW 96
Cdd:cd05340    2 LNDRIILVTGASDGIGREAALTYARYGATVI---LLGRNEEKLR-QVADHINEeggrqpqwFILDLLTctSENCQQLAQR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  97 VKERVGNrgLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRM-SFFGG 174
Cdd:cd05340   78 IAVNYPR--LDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQgRANWG 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 165377241 175 GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSSDRLSSNTKMIwdKASSEVKEIY 238
Cdd:cd05340  156 AYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRASAFPTEDPQKL--KTPADIMPLY 217
PRK06949 PRK06949
SDR family oxidoreductase;
27-207 7.40e-14

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 70.18  E-value: 7.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV-LAACLTEKgAEELRNKTSDR---LETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVvLASRRVER-LKELRAEIEAEggaAHVVSLDVTDYQSIKAAVAHAETEAG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 NRGLwgLVNNAGISTPSGPNEwMKKQDFARVLDVNLLGMI----EVTLSMLPLVR-----KARGRVVNVSSVMG-RMSFF 172
Cdd:PRK06949  86 TIDI--LVNNSGVSTTQKLVD-VTPADFDFVFDTNTRGAFfvaqEVAKRMIARAKgagntKPGGRIINIASVAGlRVLPQ 162

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 165377241 173 GGGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK06949 163 IGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPG 197
PRK06484 PRK06484
short chain dehydrogenase; Validated
 28-211 8.19e-14

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 71.80  E-value: 8.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLw 107
Cdd:PRK06484   4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDV- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 108 gLVNNAGISTPS-GPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR--GRVVNVSSVMGRMSFFG-GGYCISKYGV 183
Cdd:PRK06484  83 -LVNNAGVTDPTmTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGhgAAIVNVASGAGLVALPKrTAYSASKAAV 161

                        170       180
                 ....*....|....*....|....*...
gi 165377241 184 EAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK06484 162 ISLTRSLACEWAAKGIRVNAVLPGYVRT 189
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 13-214 8.29e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 69.98  E-value: 8.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  13 TLLRFFRerqvvshLQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEELRNK----TSDRLETVIL--DVTK 86
Cdd:PRK08213   3 TVLELFD-------LSGKTALVTGGSRGLGLQIAEALGEAGARVV---LSARKAEELEEAaahlEALGIDALWIaaDVAD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  87 TESIVAATQWVKERVGNRGLwgLVNNAGiSTPSGPNEWMKKQDFARVLDVNLLGMIEVT-----LSMLPlvRKArGRVVN 161
Cdd:PRK08213  73 EADIERLAEETLERFGHVDI--LVNNAG-ATWGAPAEDHPVEAWDKVMNLNVRGLFLLSqavakRSMIP--RGY-GRIIN 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 165377241 162 VSSVMGrmsfFGG---------GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVT 214
Cdd:PRK08213 147 VASVAG----LGGnppevmdtiAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMT 204
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 26-219 1.12e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 69.55  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAcltekgAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrG 105
Cdd:PRK06523   6 ELAGKRALVTGGTKGIGAATVARLLEAGARVVTT------ARSRPDDLPEGVEFVAADLTTAEGCAAVARAVLERLG--G 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 106 LWGLVNNAGIS-TPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSFFGG--GYCISKY 181
Cdd:PRK06523  78 VDILVHVLGGSsAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPgMIARGSGVIIHVTSIQRRLPLPESttAYAAAKA 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 165377241 182 GVEAFSDSLRRELSYFGVKVAIIEPGGFKTcvTSSDRL 219
Cdd:PRK06523 158 ALSTYSKSLSKEVAPKGVRVNTVSPGWIET--EAAVAL 193
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 27-211 1.27e-13

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 69.13  E-value: 1.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacltekgaeeLRNKTSDRLETV---------------ILD---VTKTE 88
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVI-----------LLGRTEEKLEAVydeieaaggpqpaiiPLDlltATPQN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  89 SI-VAATqwVKERVGNrgLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVM 166
Cdd:PRK08945  79 YQqLADT--IEEQFGR--LDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPaASLVFTSSSV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 165377241 167 GRMS-FFGGGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK08945 155 GRQGrANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRT 200
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 30-211 1.52e-13

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


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 69.42  E-value: 1.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACL----TEKGAEELRNKTSDRLETVI-LDVTKTESIVA-ATQWVKERvgn 103
Cdd:cd09807    2 KTVIITGANTGIGKETARELARRGARVIMACRdmakCEEAAAEIRRDTLNHEVIVRhLDLASLKSIRAfAAEFLAEE--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 RGLWGLVNNAGI-STPsgpnEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVM---GRMSF------- 171
Cdd:cd09807   79 DRLDVLINNAGVmRCP----YSKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKsAPSRIVNVSSLAhkaGKINFddlnsek 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 165377241 172 ---FGGGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd09807  155 synTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRT 197
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 29-217 1.89e-13

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 68.45  E-value: 1.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGaeelrnKTSDRLETVILDVTKTESivAATQWVKErvgnrgLWG 108
Cdd:PRK06550   5 TKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDKP------DLSGNFHFLQLDLSDDLE--PLFDWVPS------VDI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 109 LVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSffGGG---YCISKYGVE 184
Cdd:PRK06550  71 LCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPqMLERKSGIIINMCSIASFVA--GGGgaaYTASKHALA 148

                        170       180       190
                 ....*....|....*....|....*....|...
gi 165377241 185 AFSDSLRRELSYFGVKVAIIEPGGFKTCVTSSD 217
Cdd:PRK06550 149 GFTKQLALDYAKDGIQVFGIAPGAVKTPMTAAD 181
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 27-207 1.90e-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: 1.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAC----LTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:cd05343    4 WRGRVALVTGASVGIGAAVARALVQHGMKVVGCArrvdKIEALAAECQSAGYPTLFPYQCDLSNEEQILSMFSAIRTQHQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 nrGLWGLVNNAGISTP----SGPNEWMKKqdfarVLDVNLLGMIEVT---LSMLPLVRKARGRVVNVSSVMGR----MSF 171
Cdd:cd05343   84 --GVDVCINNAGLARPepllSGKTEGWKE-----MFDVNVLALSICTreaYQSMKERNVDDGHIININSMSGHrvppVSV 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 165377241 172 FgGGYCISKYGVEAFSDSLRRELSYF--GVKVAIIEPG 207
Cdd:cd05343  157 F-HFYAATKHAVTALTEGLRQELREAktHIRATSISPG 193
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
30-222 2.54e-13

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 68.56  E-value: 2.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE-KGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLWG 108
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTEnKELTKLAEQYNSNLTFHSLDLQDVHELETNFNEILSSIQEDNVSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 109 --LVNNAGISTPSGPNEWMKKQDFARVLDVNLLgmIEVTLSMLPLVR----KARGRVVNVSSVMGRMSFFG-GGYCISKY 181
Cdd:PRK06924  82 ihLINNAGMVAPIKPIEKAESEELITNVHLNLL--APMILTSTFMKHtkdwKVDKRVINISSGAAKNPYFGwSAYCSSKA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 165377241 182 GVEAFSDS--LRRELSYFGVKVAIIEPGGFKTCVTSSDRLSSN 222
Cdd:PRK06924 160 GLDMFTQTvaTEQEEEEYPVKIVAFSPGVMDTNMQAQIRSSSK 202
PRK07074 PRK07074
SDR family oxidoreductase;
29-211 3.28e-13

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 68.26  E-value: 3.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD-RLETVILDVTKTESIVAAtqwVKERVGNRGLW 107
Cdd:PRK07074   2 KRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDaRFVPVACDLTDAASLAAA---LANAAAERGPV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 108 G-LVNNAGISTP-----SGPNEWmkKQDFARVLDVNLLGMIEVTLSMLplvRKARGRVVNVSSVMGrMSFFGG-GYCISK 180
Cdd:PRK07074  79 DvLVANAGAARAaslhdTTPASW--RADNALNLEAAYLCVEAVLEGML---KRSRGAVVNIGSVNG-MAALGHpAYSAAK 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 165377241 181 YGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK07074 153 AGLIHYTKLLAVEYGRFGIRANAVAPGTVKT 183
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 27-206 3.66e-13

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: 67.88  E-value: 3.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDrLETVILDVtktesivAATQWVKERVGNRGL 106
Cdd:cd05351    5 FAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPG-IEPVCVDL-------SDWDATEEALGSVGP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 W-GLVNNAGISTPSgPNEWMKKQDFARVLDVNLLGMIEVTLSMLP--LVRKARGRVVNVSSVMGRMSFFG-GGYCISKYG 182
Cdd:cd05351   77 VdLLVNNAAVAILQ-PFLEVTKEAFDRSFDVNVRAVIHVSQIVARgmIARGVPGSIVNVSSQASQRALTNhTVYCSTKAA 155

                        170       180
                 ....*....|....*....|....
gi 165377241 183 VEAFSDSLRRELSYFGVKVAIIEP 206
Cdd:cd05351  156 LDMLTKVMALELGPHKIRVNSVNP 179
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 27-211 3.88e-13

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: 68.00  E-value: 3.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAC----LTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:cd05369    1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGrkpeVLEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLKEFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 NrgLWGLVNNAGISTPSgPNEWMKKQDFARVLDVNLLGMIEVTLSMLP--LVRKARGRVVNVSSVMgrmSFFGGGYCI-- 178
Cdd:cd05369   81 K--IDILINNAAGNFLA-PAESLSPNGFKTVIDIDLNGTFNTTKAVGKrlIEAKHGGSILNISATY---AYTGSPFQVhs 154

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 165377241 179 --SKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd05369  155 aaAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPT 189
PRK07775 PRK07775
SDR family oxidoreductase;
25-211 3.89e-13

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 68.24  E-value: 3.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  25 SHLQDKYVFITGCDSGFGNLLARQLDRRGMRV-LAACLTEKGAEELRNKTSDRLETVI--LDVTKTESIVAATQWVKERV 101
Cdd:PRK07775   6 PHPDRRPALVAGASSGIGAATAIELAAAGFPVaLGARRVEKCEELVDKIRADGGEAVAfpLDVTDPDSVKSFVAQAEEAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 102 GNRGLwgLVNNAGISTPSGPNEwMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSS-VMGRMSFFGGGYCIS 179
Cdd:PRK07775  86 GEIEV--LVSGAGDTYFGKLHE-ISTEQFESQVQIHLVGANRLATAVLPgMIERRRGDLIFVGSdVALRQRPHMGAYGAA 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 165377241 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK07775 163 KAGLEAMVTNLQMELEGTGVRASIVHPGPTLT 194
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 30-211 4.00e-13

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: 67.88  E-value: 4.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELrnKTSDRLETVILDVTKTESIVAATQWVkERVGNrglwgL 109
Cdd:cd05368    3 KVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKEL--ERGPGITTRVLDVTDKEQVAALAKEE-GRIDV-----L 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 110 VNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSFFGG--GYCISKYGVEAF 186
Cdd:cd05368   75 FNCAGF-VHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPkMLARKDGSIINMSSVASSIKGVPNrfVYSTTKAAVIGL 153

                        170       180
                 ....*....|....*....|....*
gi 165377241 187 SDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd05368  154 TKSVAADFAQQGIRCNAICPGTVDT 178
PRK09242 PRK09242
SDR family oxidoreductase;
27-216 6.52e-13

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 67.46  E-value: 6.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD-----RLETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK09242   7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEefperEVHGLAADVSDDEDRRAILDWVEDHW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 102 GnrGLWGLVNNAGISTPSGPNEWmKKQDFARVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVMGRMSFFGGG-YCIS 179
Cdd:PRK09242  87 D--GLHILVNNAGGNIRKAAIDY-TEDEWRGIFETNLFSAFELSRYAHPLLKQhASSAIVNIGSVSGLTHVRSGApYGMT 163

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 165377241 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSS 216
Cdd:PRK09242 164 KAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSG 200
PRK08628 PRK08628
SDR family oxidoreductase;
26-204 6.96e-13

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 67.29  E-value: 6.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  26 HLQDKYVFITGCDSGFGNLLARQLDRRG-MRVLAACLTEKG--AEELRNKTSdRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK08628   4 NLKDKVVIVTGGASGIGAAISLRLAEEGaIPVIFGRSAPDDefAEELRALQP-RAEFVQVDLTDDAQCRDAVEQTVAKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 nrGLWGLVNNAG----ISTPSGPnewmkkQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVM-----GRMSffg 173
Cdd:PRK08628  83 --RIDGLVNNAGvndgVGLEAGR------EAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISSKTaltgqGGTS--- 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 165377241 174 gGYCISKYGVEAFSDSLRRELSYFGVKV-AII 204
Cdd:PRK08628 152 -GYAAAKGAQLALTREWAVALAKDGVRVnAVI 182
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 29-209 9.53e-13

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 66.98  E-value: 9.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTS-----DRLETVILDVTKTESIVAATQWVKERVGN 103
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINaeygeGMAYGFGADATSEQSVLALSRGVDEIFGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 RGLwgLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMI----EVTLSMLPlvRKARGRVVNVSSVMGRM-SFFGGGYCI 178
Cdd:PRK12384  82 VDL--LVYNAGIAK-AAFITDFQLGDFDRSLQVNLVGYFlcarEFSRLMIR--DGIQGRIIQINSKSGKVgSKHNSGYSA 156

                        170       180       190
                 ....*....|....*....|....*....|.
gi 165377241 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGGF 209
Cdd:PRK12384 157 AKFGGVGLTQSLALDLAEYGITVHSLMLGNL 187
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 34-219 1.28e-12

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 66.90  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  34 ITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEE----LRNKTSDrLETVILDVTKTESIVAATQWVKERVGNRGLwgL 109
Cdd:PRK05876  11 ITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQavnhLRAEGFD-VHGVMCDVRHREEVTHLADEAFRLLGHVDV--V 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 110 VNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP--LVRKARGRVVNVSSVMGRMSFFG-GGYCISKYGVEAF 186
Cdd:PRK05876  88 FSNAGIVV-GGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPrlLEQGTGGHVVFTASFAGLVPNAGlGAYGVAKYGVVGL 166

                        170       180       190
                 ....*....|....*....|....*....|....
gi 165377241 187 SDSLRRELSYFGVKVAIIEPGGFKT-CVTSSDRL 219
Cdd:PRK05876 167 AETLAREVTADGIGVSVLCPMVVETnLVANSERI 200
PRK07023 PRK07023
SDR family oxidoreductase;
34-217 2.11e-12

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 65.80  E-value: 2.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  34 ITGCDSGFGNLLARQLDRRGMRVLaaCLTEKGAEELRNKTSDRLETVILDVTKTEsivAATQWVKERVGNRGLWG----- 108
Cdd:PRK07023   6 VTGHSRGLGAALAEQLLQPGIAVL--GVARSRHPSLAAAAGERLAEVELDLSDAA---AAAAWLAGDLLAAFVDGasrvl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 109 LVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVMGRMSFFG-GGYCISKYGVEAF 186
Cdd:PRK07023  81 LINNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDaAERRILHISSGAARNAYAGwSVYCATKAALDHH 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 165377241 187 SDSLRRELSYfGVKVAIIEPG----GFKTCVTSSD 217
Cdd:PRK07023 161 ARAVALDANR-ALRIVSLAPGvvdtGMQATIRATD 194
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
30-211 2.51e-12

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 65.90  E-value: 2.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLE---TVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:PRK08643   3 KVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGkaiAVKADVSDRDQVFAAVRQVVDTFG--DL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 WGLVNNAGIStPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR--GRVVNVSSVMGRMSFFG-GGYCISKYGV 183
Cdd:PRK08643  81 NVVVNNAGVA-PTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGhgGKIINATSQAGVVGNPElAVYSSTKFAV 159

                        170       180
                 ....*....|....*....|....*...
gi 165377241 184 EAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK08643 160 RGLTQTAARDLASEGITVNAYAPGIVKT 187
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 27-228 2.59e-12

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: 65.43  E-value: 2.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV----LAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:cd05352    6 LKGKVAIVTGGSRGIGLAIARALAEAGADVaiiyNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 NrgLWGLVNNAGISTPSgPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVMGRMSFFG---GGYCI 178
Cdd:cd05352   86 K--IDILIANAGITVHK-PALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKqGKGSLIITASMSGTIVNRPqpqAAYNA 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 165377241 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTssDRLSSNTKMIWD 228
Cdd:cd05352  163 SKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLT--DFVDKELRKKWE 210
PRK07831 PRK07831
SDR family oxidoreductase;
27-219 3.52e-12

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 65.44  E-value: 3.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGC-DSGFGNLLARQLDRRGMRVLAACLTEK----GAEELRNKT-SDRLETVILDVTKTESIVAATQWVKER 100
Cdd:PRK07831  15 LAGKVVLVTAAaGTGIGSATARRALEEGARVVISDIHERrlgeTADELAAELgLGRVEAVVCDVTSEAQVDALIDAAVER 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 101 VGnrGLWGLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP--LVRKARGRVVNVSSVMG-RMSFFGGGYC 177
Cdd:PRK07831  95 LG--RLDVLVNNAGLGG-QTPVVDMTDDEWSRVLDVTLTGTFRATRAALRymRARGHGGVIVNNASVLGwRAQHGQAHYA 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 165377241 178 ISKYGVEAFSDSLRRELSYFGVKVAIIEPG----GFKTCVTSSDRL 219
Cdd:PRK07831 172 AAKAGVMALTRCSALEAAEYGVRINAVAPSiamhPFLAKVTSAELL 217
PRK06138 PRK06138
SDR family oxidoreductase;
26-211 5.40e-12

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 64.79  E-value: 5.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD--RLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:PRK06138   2 RLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAggRAFARQGDVGSAEAVEALVDFVAARWG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 rGLWGLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSvmgRMSFFGG----GYCI 178
Cdd:PRK06138  81 -RLDVLVNNAGFGC-GGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGgGSIVNTAS---QLALAGGrgraAYVA 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 165377241 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK06138 156 SKGAIASLTRAMALDHATDGIRVNAVAPGTIDT 188
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 27-211 6.59e-12

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: 64.79  E-value: 6.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLT-EKG---AEELRNK--TSDRLETvilDVTKTESIVAATQWVKER 100
Cdd:cd08935    3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNqEKGdkvAKEITALggRAIALAA---DVLDRASLERAREEIVAQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 101 VGNRGLwgLVNNAGISTPSG--PNEW-----------MKKQDFARVLDVNLLGmiEVTLSML---PLVRKARGRVVNVSS 164
Cdd:cd08935   80 FGTVDI--LINGAGGNHPDAttDPEHyepeteqnffdLDEEGWEFVFDLNLNG--SFLPSQVfgkDMLEQKGGSIINISS 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 165377241 165 vMGRMSFFG--GGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd08935  156 -MNAFSPLTkvPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVT 203
PRK06139 PRK06139
SDR family oxidoreductase;
27-197 6.95e-12

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 65.13  E-value: 6.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMR-VLAACLTE---KGAEELRNKTSDRLeTVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK06139   5 LHGAVVVITGASSGIGQATAEAFARRGARlVLAARDEEalqAVAEECRALGAEVL-VVPTDVTDADQVKALATQAASFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 NRGLWglVNNAGI-------STPSGPNEwmkkqdfaRVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVMGRMSF-FG 173
Cdd:PRK06139  84 RIDVW--VNNVGVgavgrfeETPIEAHE--------QVIQTNLIGYMRDAHAALPIFKKqGHGIFINMISLGGFAAQpYA 153

                        170       180
                 ....*....|....*....|....
gi 165377241 174 GGYCISKYGVEAFSDSLRRELSYF 197
Cdd:PRK06139 154 AAYSASKFGLRGFSEALRGELADH 177
PLN02253 PLN02253
xanthoxin dehydrogenase
 27-211 8.16e-12

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 64.46  E-value: 8.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVIL--DVTKTESIVAATQWVKERVGNR 104
Cdd:PLN02253  16 LLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNVCFFhcDVTVEDDVSRAVDFTVDKFGTL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 105 GLwgLVNNAGISTPSGPN-EWMKKQDFARVLDVNL----LGMIEVTLSMLPLvrkARGRVVNVSSVMGRMSFFG-GGYCI 178
Cdd:PLN02253  96 DI--MVNNAGLTGPPCPDiRNVELSEFEKVFDVNVkgvfLGMKHAARIMIPL---KKGSIVSLCSVASAIGGLGpHAYTG 170

                        170       180       190
                 ....*....|....*....|....*....|...
gi 165377241 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PLN02253 171 SKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPT 203
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
27-206 1.09e-11

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 65.25  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACL----TEKGAEELRNKtsDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK08324 420 LAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLdeeaAEAAAAELGGP--DRALGVACDVTDEAAVQAAFEEAALAFG 497

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 nrGLWGLVNNAGIStPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKA--RGRVVNVSS---VMGRMSFfgGGYC 177
Cdd:PRK08324 498 --GVDIVVSNAGIA-ISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQglGGSIVFIASknaVNPGPNF--GAYG 572

                        170       180       190
                 ....*....|....*....|....*....|...
gi 165377241 178 ISKygveAFSDSLRR----ELSYFGVKVAIIEP 206
Cdd:PRK08324 573 AAK----AAELHLVRqlalELGPDGIRVNGVNP 601
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-218 1.56e-11

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 63.60  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAE--ELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNR 104
Cdd:PRK06935  13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWDEtrRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 105 GLwgLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMgrmSFFGG----GYCIS 179
Cdd:PRK06935  93 DI--LVNNAGT-IRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKvMAKQGSGKIINIASML---SFQGGkfvpAYTAS 166

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 165377241 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSSDR 218
Cdd:PRK06935 167 KHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAPIR 205
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 109-207 1.81e-11

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: 62.15  E-value: 1.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 109 LVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSF-FGGGYCISKYGVEAF 186
Cdd:cd02266   35 VVHNAAILD-DGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRlGRFILISSVAGLFGApGLGGYAASKAALDGL 113

                         90       100
                 ....*....|....*....|.
gi 165377241 187 SDSLRRELSYFGVKVAIIEPG 207
Cdd:cd02266  114 AQQWASEGWGNGLPATAVACG 134
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 28-210 2.07e-11

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: 63.12  E-value: 2.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAE----ELRNKTSDRLETVILDVTKTESIVAATQWVKERVGN 103
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEqlkeELTNLYKNRVIALELDITSKESIKELIESYLEKFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 rgLWGLVNNAGIS--TPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVMG----RMSFFGGG- 175
Cdd:cd08930   81 --IDILINNAYPSpkVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKqGKGSIINIASIYGviapDFRIYENTq 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 165377241 176 ------YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFK 210
Cdd:cd08930  159 myspveYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGIL 199
PRK06172 PRK06172
SDR family oxidoreductase;
27-211 2.22e-11

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 62.85  E-value: 2.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEE----LRNKTSDRLeTVILDVTKTESIvaaTQWVKERVG 102
Cdd:PRK06172   5 FSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEEtvalIREAGGEAL-FVACDVTRDAEV---KALVEQTIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 NRG-LWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGmieVTLSM---LP-LVRKARGRVVNVSSVMGRMSFFG-GGY 176
Cdd:PRK06172  81 AYGrLDYAFNNAGIEIEQGRLAEGSEAEFDAIMGVNVKG---VWLCMkyqIPlMLAQGGGAIVNTASVAGLGAAPKmSIY 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 165377241 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK06172 158 AASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDT 192
PRK06398 PRK06398
aldose dehydrogenase; Validated
 27-165 2.62e-11

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 62.93  E-value: 2.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKgaeelRNKTSDRLEtviLDVTKTESIVAATQWVKERVGNRGL 106
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEP-----SYNDVDYFK---VDVSNKEQVIKGIDYVISKYGRIDI 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 wgLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSV 165
Cdd:PRK06398  76 --LVNNAGIES-YGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDkGVIINIASV 132
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 30-207 4.04e-11

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: 62.08  E-value: 4.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVL------AACLtEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:cd08940    3 KVALVTGSTSGIGLGIARALAAAGANIVlngfgdAAEI-EAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 rGLWGLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFFG-GGYCISKY 181
Cdd:cd08940   81 -GVDILVNNAGIQH-VAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGwGRIINIASVHGLVASANkSAYVAAKH 158

                        170       180
                 ....*....|....*....|....*.
gi 165377241 182 GVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:cd08940  159 GVVGLTKVVALETAGTGVTCNAICPG 184
PRK12746 PRK12746
SDR family oxidoreductase;
24-211 4.63e-11

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 61.97  E-value: 4.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  24 VSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGA--EELRNKTSDRLETVIL--DVTKTESIVAATQWVKE 99
Cdd:PRK12746   1 MKNLDGKVALVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAadETIREIESNGGKAFLIeaDLNSIDGVKKLVEQLKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 100 ----RVGNRGLWGLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRkARGRVVNVSSVMGRMSFFGG- 174
Cdd:PRK12746  81 elqiRVGTSEIDILVNNAGIGT-QGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLR-AEGRVINISSAEVRLGFTGSi 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 165377241 175 GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK12746 159 AYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKT 195
PRK06124 PRK06124
SDR family oxidoreductase;
27-230 4.88e-11

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 62.04  E-value: 4.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEELRNKTSD------RLETVILDVTKTESIVAATQWVKER 100
Cdd:PRK06124   9 LAGQVALVTGSARGLGFEIARALAGAGAHVL---VNGRNAATLEAAVAAlraaggAAEALAFDIADEEAVAAAFARIDAE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 101 VGnrGLWGLVNNAGISTPSGPNEwMKKQDFARVLDVNLLGMIevTLSMLPLVRKAR---GRVVNVSSVMGRMSFFGGG-Y 176
Cdd:PRK06124  86 HG--RLDILVNNVGARDRRPLAE-LDDAAIRALLETDLVAPI--LLSRLAAQRMKRqgyGRIIAITSIAGQVARAGDAvY 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 165377241 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTcvtssdrlSSNTKMIWDKA 230
Cdd:PRK06124 161 PAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFAT--------ETNAAMAADPA 206
PRK06953 PRK06953
SDR family oxidoreductase;
30-185 5.40e-11

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 61.24  E-value: 5.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSdrlETVILDVTKTESiVAATQWvkeRVGNRGLWGL 109
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQALGA---EALALDVADPAS-VAGLAW---KLDGEALDAA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 110 VNNAGISTP-SGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRM----SFFGGGYCISKYGVE 184
Cdd:PRK06953  75 VYVAGVYGPrTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSRMGSIgdatGTTGWLYRASKAALN 154


                 .
gi 165377241 185 A 185
Cdd:PRK06953 155 D 155
PRK07069 PRK07069
short chain dehydrogenase; Validated
 33-167 5.51e-11

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 61.65  E-value: 5.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  33 FITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEELRNKTSDRLET---------VILDVTKTESIVAATQWVKERVGn 103
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVF---LTDINDAAGLDAFAAEINAahgegvafaAVQDVTDEAQWQALLAQAADAMG- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 165377241 104 rGLWGLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMG 167
Cdd:PRK07069  79 -GLSVLVNNAGVGS-FGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQpASIVNISSVAA 141
PRK08251 PRK08251
SDR family oxidoreductase;
30-207 6.25e-11

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 61.49  E-value: 6.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGmRVLAAC------LTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGn 103
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKG-RDLALCarrtdrLEELKAELLARYPGIKVAVAALDVNDHDQVFEVFAEFRDELG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 rGLWGLVNNAGIST--PSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLplvRKA-RGRVVNVSSVMGRMSFFG--GGYCI 178
Cdd:PRK08251  81 -GLDRVIVNAGIGKgaRLGTGKFWANKATAETNFVAALAQCEAAMEIF---REQgSGHLVLISSVSAVRGLPGvkAAYAA 156

                        170       180
                 ....*....|....*....|....*....
gi 165377241 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK08251 157 SKAGVASLGEGLRAELAKTPIKVSTIEPG 185
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 27-209 7.83e-11

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: 61.34  E-value: 7.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVL------AACltEKGAEELrnKTSDRLETVILDVTKTESIVAATQWVKER 100
Cdd:cd08942    4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIisarkaEAC--ADAAEEL--SAYGECIAIPADLSSEEGIEALVARVAER 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 101 vgNRGLWGLVNNAGiSTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-----GRVVNVSSV-----MGRMS 170
Cdd:cd08942   80 --SDRLDVLVNNAG-ATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAAtaenpARVINIGSIagivvSGLEN 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 165377241 171 FfggGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGF 209
Cdd:cd08942  157 Y---SYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRF 192
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 32-221 1.04e-10

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


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 60.83  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGMRVL-----AACLTEKGAEELRNKTSdRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVVinyrkSKDAAAEVAAEIEELGG-KAVVVRADVSQPQDVEEMFAAVKERFG--RL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 WGLVNNAGISTPSGPNEwMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSS------VMGRMsFFGGgyciS 179
Cdd:cd05359   78 DVLVSNAAAGAFRPLSE-LTPAHWDAKMNTNLKALVHCAQQAAKLMRERGgGRIVAISSlgsiraLPNYL-AVGT----A 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 165377241 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGgfktcVTSSDRLSS 221
Cdd:cd05359  152 KAALEALVRYLAVELGPRGIRVNAVSPG-----VIDTDALAH 188
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 27-211 1.10e-10

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: 60.83  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNrgL 106
Cdd:cd05348    2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGK--L 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 WGLVNNAGI-----STPSGPNEWMKKQdFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGrmsFF--GGG--YC 177
Cdd:cd05348   80 DCFIGNAGIwdystSLVDIPEEKLDEA-FDELFHINVKGYILGAKAALPALYATEGSVIFTVSNAG---FYpgGGGplYT 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 165377241 178 ISKYGVEAfsdsLRRELSY-FG--VKVAIIEPGGFKT 211
Cdd:cd05348  156 ASKHAVVG----LVKQLAYeLAphIRVNGVAPGGMVT 188
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 30-242 1.40e-10

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: 60.48  E-value: 1.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACL----TEKGAEELRNKtsDRLETVILDVTKTESIVAATQWVKERVGnrG 105
Cdd:cd08943    2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIdpeiAEKVAEAAQGG--PRALGVQCDVTSEAQVQSAFEQAVLEFG--G 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 106 LWGLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR--GRVVNVSSvmgRMSFFGG----GYCIS 179
Cdd:cd08943   78 LDIVVSNAGIAT-SSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGigGNIVFNAS---KNAVAPGpnaaAYSAA 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 165377241 180 KygveAFSDSLRR----ELSYFGVKVAIIEPGGFKtcvtssdRLSSNTKMIWDKASSEVKEIYGEKF 242
Cdd:cd08943  154 K----AAEAHLARclalEGGEDGIRVNTVNPDAVF-------RGSKIWEGVWRAARAKAYGLLEEEY 209
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 27-211 1.50e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 60.51  E-value: 1.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLetVILDVTKTESIVAATQWVKERVGNRGL 106
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGGLF--VPTDVTDEDAVNALFDTAAETYGSVDI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 wgLVNNAGISTP-------SGPNEWmkkqdfARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMsffGGG--- 175
Cdd:PRK06057  83 --AFNNAGISPPeddsilnTGLDAW------QRVQDVNLTSVYLCCKAALPhMVRQGKGSIINTASFVAVM---GSAtsq 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 165377241 176 --YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK06057 152 isYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNT 189
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 27-218 1.55e-10

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 60.46  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV----LAACLTEKGAEELRNKTSDrLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIvfndINQELVDKGLAAYRELGIE-AHGYVCDVTDEDGVQAMVSQIEKEVG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 NRGLwgLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVM---GRMSFfgGGYCI 178
Cdd:PRK07097  87 VIDI--LVNNAGI-IKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPsMIKKGHGKIINICSMMselGRETV--SAYAA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 165377241 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSSDR 218
Cdd:PRK07097 162 AKGGLKMLTKNIASEYGEANIQCNGIGPGYIATPQTAPLR 201
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 32-167 2.12e-10

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: 60.20  E-value: 2.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEkgAEelrnktsdrletVILDVTKTESIVAATQWVKERVGnRGLWGLVN 111
Cdd:cd05328    2 IVITGAASGIGAATAELLEDAGHTVIGIDLRE--AD------------VIADLSTPEGRAAAIADVLARCS-GVLDGLVN 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 165377241 112 NAGISTPSGPNEwmkkqdfarVLDVNLLGMIEVTLSMLPLVRKARG-RVVNVSSVMG 167
Cdd:cd05328   67 CAGVGGTTVAGL---------VLKVNYFGLRALMEALLPRLRKGHGpAAVVVSSIAG 114
PRK12743 PRK12743
SDR family oxidoreductase;
28-217 2.15e-10

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 60.05  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  28 QDKYVFITGCDSGFGNLLARQLDRRGMRVlaaCLT----EKGA----EELRnKTSDRLETVILDVTKTESIVAATQWVKE 99
Cdd:PRK12743   1 MAQVAIVTASDSGIGKACALLLAQQGFDI---GITwhsdEEGAketaEEVR-SHGVRAEIRQLDLSDLPEGAQALDKLIQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 100 RVGnrGLWGLVNNAGistpSGPNEWMKKQDFA---RVLDVNLLGmievtlSMLPLVRKAR--------GRVVNVSSVMGR 168
Cdd:PRK12743  77 RLG--RIDVLVNNAG----AMTKAPFLDMDFDewrKIFTVDVDG------AFLCSQIAARhmvkqgqgGRIINITSVHEH 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 165377241 169 MSFFGGG-YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSSD 217
Cdd:PRK12743 145 TPLPGASaYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIATPMNGMD 194
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 27-207 2.78e-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: 2.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWG--SI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 WGLVNNAGISTPSgPNEWMKKQDFARVLDVNLLGMievtLSMLPLVRKAR------GRVVNVSSVMGRM-SFFGGGYCIS 179
Cdd:cd05363   79 DILVNNAALFDLA-PIVDITRESYDRLFAINVSGT----LFMMQAVARAMiaqgrgGKIINMASQAGRRgEALVGVYCAT 153

                        170       180
                 ....*....|....*....|....*...
gi 165377241 180 KYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:cd05363  154 KAAVISLTQSAGLNLIRHGINVNAIAPG 181
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 26-211 3.48e-10

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 59.48  E-value: 3.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  26 HLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVI---LDVTKTESIVAATQWVKERVG 102
Cdd:PRK06113   8 RLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFacrCDITSEQELSALADFALSKLG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 nrGLWGLVNNAGistPSGPNEW-MKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVV-NVSSVMG-----RMSFFGGg 175
Cdd:PRK06113  88 --KVDILVNNAG---GGGPKPFdMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVIlTITSMAAenkniNMTSYAS- 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 165377241 176 yciSKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK06113 162 ---SKAAASHLVRNMAFDLGEKNIRVNGIAPGAILT 194
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
32-209 3.64e-10

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 59.61  E-value: 3.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCdSGF-GNLLARQLDRRGMRVLAACLTEKGAEELRNktSDRLETVILDVTKTESIVAATQWVkERVgnrglwglV 110
Cdd:COG0451    2 ILVTGG-AGFiGSHLARRLLARGHEVVGLDRSPPGAANLAA--LPGVEFVRGDLRDPEALAAALAGV-DAV--------V 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 111 NNAGISTPSGpnewmkkQDFARVLDVNLLGmievTLSMLPLVRKAR-GRVVNVSSvmgrMSFFGGG-------------- 175
Cdd:COG0451   70 HLAAPAGVGE-------EDPDETLEVNVEG----TLNLLEAARAAGvKRFVYASS----SSVYGDGegpidedtplrpvs 134

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 165377241 176 -YCISKYGVEAFSDSLRRElsyFGVKVAIIEPGGF 209
Cdd:COG0451  135 pYGASKLAAELLARAYARR---YGLPVTILRPGNV 166
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 27-211 4.63e-10

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 59.14  E-value: 4.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLT-EKG---AEELRNKTSDRLeTVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK08277   8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNqEKAeavVAEIKAAGGEAL-AVKADVLDKESLEQARQQILEDFG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 NRGLwgLVNNAGISTPSG--PNEW------------MKKQDFARVLDVNLLGmievtlSMLP-------LVRKARGRVVN 161
Cdd:PRK08277  87 PCDI--LINGAGGNHPKAttDNEFhelieptktffdLDEEGFEFVFDLNLLG------TLLPtqvfakdMVGRKGGNIIN 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 165377241 162 VSSvmgrMSFFGG-----GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK08277 159 ISS----MNAFTPltkvpAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLT 209
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 27-211 1.03e-09

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 58.04  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAFG--KL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 WGLVNNAGISTPSGPNEWMKKQD----FARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGrmsFFGGG----YCI 178
Cdd:PRK06200  82 DCFVGNAGIWDYNTSLVDIPAETldtaFDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLSNSS---FYPGGggplYTA 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 165377241 179 SKYGVEAfsdsLRRELSYF---GVKVAIIEPGGFKT 211
Cdd:PRK06200 159 SKHAVVG----LVRQLAYElapKIRVNGVAPGGTVT 190
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 25-184 1.30e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 57.71  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  25 SHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAC--LTEKG---AEELRnKTSDRLETVILDVTKTESIVAATQWVKE 99
Cdd:PRK06198   2 GRLDGKVALVTGGTQGLGAAIARAFAERGAAGLVICgrNAEKGeaqAAELE-ALGAKAVFVQADLSDVEDCRRVVAAADE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 100 RVGnrGLWGLVNNAGIST-----PSGPnewmkkQDFARVLDVNLLG----MIEVTLSMLPlvRKARGRVVNVSSvmgrMS 170
Cdd:PRK06198  81 AFG--RLDALVNAAGLTDrgtilDTSP------ELFDRHFAVNVRApfflMQEAIKLMRR--RKAEGTIVNIGS----MS 146

                        170
                 ....*....|....*....
gi 165377241 171 FFGG-----GYCISKYGVE 184
Cdd:PRK06198 147 AHGGqpflaAYCASKGALA 165
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 27-211 1.45e-09

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: 57.54  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEEL--RNKTSDRLETVILDVTKTESIVAATQWVKERVGNR 104
Cdd:cd08937    2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLaeILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 105 GLwgLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRmsffgGG----YCIS 179
Cdd:cd08937   82 DV--LINNVGGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPhMLERQQGVIVNVSSIATR-----GIyripYSAA 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 165377241 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd08937  155 KGGVNALTASLAFEHARDGIRVNAVAPGGTEA 186
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 27-207 1.92e-09

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 57.33  E-value: 1.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:PRK08265   4 LAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFG--RV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 WGLVNNA------GIStpSGPNEWMkkqdfaRVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRMSFFGGG-YCIS 179
Cdd:PRK08265  82 DILVNLActylddGLA--SSRADWL------AALDVNLVSAAMLAQAAHPHLARGGGAIVNFTSISAKFAQTGRWlYPAS 153

                        170       180
                 ....*....|....*....|....*...
gi 165377241 180 KYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK08265 154 KAAIRQLTRSMAMDLAPDGIRVNSVSPG 181
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 33-215 2.54e-09

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 56.89  E-value: 2.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  33 FITGCDSGFGNLLARQLDRRGMRVLAACLTEkgAEELRnKTSDRLET-------VILDVTKTESIVAATQWVKERVGnrG 105
Cdd:PRK12745   6 LVTGGRRGIGLGIARALAAAGFDLAINDRPD--DEELA-ATQQELRAlgvevifFPADVADLSAHEAMLDAAQAAWG--R 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 106 LWGLVNNAGISTPS-GPNEWMKKQDFARVLDVNLLGMI----EVTLSML--PLVRKARGR-VVNVSSVMGRM-SFFGGGY 176
Cdd:PRK12745  81 IDCLVNNAGVGVKVrGDLLDLTPESFDRVLAINLRGPFfltqAVAKRMLaqPEPEELPHRsIVFVSSVNAIMvSPNRGEY 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 165377241 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTS 215
Cdd:PRK12745 161 CISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTA 199
PRK06123 PRK06123
SDR family oxidoreductase;
29-225 3.26e-09

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 56.33  E-value: 3.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEK-GAEELRNKTSDRLETVIL---DVTKTESIVAATQWVKERVGNr 104
Cdd:PRK06123   2 RKVMIITGASRGIGAATALLAAERGYAVCLNYLRNRdAAEAVVQAIRRQGGEALAvaaDVADEADVLRLFEAVDRELGR- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 105 gLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMI----EVTLSMLPLVRKARGRVVNVSSVMGRMSFFGG--GYCI 178
Cdd:PRK06123  81 -LDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSFlcarEAVKRMSTRHGGRGGAIVNVSSMAARLGSPGEyiDYAA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 165377241 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSS-------DRLSSNTKM 225
Cdd:PRK06123 160 SKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASggepgrvDRVKAGIPM 213
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 30-216 4.04e-09

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: 56.31  E-value: 4.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACL-TEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLwg 108
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYrSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDT-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 109 LVNNAGISTPSGPN--------EWmkkQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVM---GRMSFfgGGY 176
Cdd:cd05349   79 IVNNALIDFPFDPDqrktfdtiDW---EDYQQQLEGAVKGALNLLQAVLPDFKERGsGRVINIGTNLfqnPVVPY--HDY 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 165377241 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSS 216
Cdd:cd05349  154 TTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKVTDASA 193
PRK07577 PRK07577
SDR family oxidoreductase;
27-211 4.26e-09

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 55.89  E-value: 4.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACltekgaeelRNKTSD---RLETVIL-DVTKTESIVAATqwvkerVG 102
Cdd:PRK07577   1 MSSRTVLVTGATKGIGLALSLRLANLGHQVIGIA---------RSAIDDfpgELFACDLaDIEQTAATLAQI------NE 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 NRGLWGLVNNAGISTPsGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSvmgrMSFFGG----GYC 177
Cdd:PRK07577  66 IHPVDAIVNNVGIALP-QPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREqGRIVNICS----RAIFGAldrtSYS 140

                        170       180       190
                 ....*....|....*....|....*....|....
gi 165377241 178 ISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK07577 141 AAKSALVGCTRTWALELAEYGITVNAVAPGPIET 174
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 27-215 5.69e-09

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: 55.92  E-value: 5.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDR---LETVILDVTKTESIVAATQWVKERVGN 103
Cdd:cd05329    4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKgfkVEGSVCDVSSRSERQELMDTVASHFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 RgLWGLVNNAGISTPSGPNEWMKKqDFARVLDVNLLGMIEVTLSMLPLV-RKARGRVVNVSSVMGRMSF-FGGGYCISKY 181
Cdd:cd05329   84 K-LNILVNNAGTNIRKEAKDYTEE-DYSLIMSTNFEAAYHLSRLAHPLLkASGNGNIVFISSVAGVIAVpSGAPYGATKG 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 165377241 182 GVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTS 215
Cdd:cd05329  162 ALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVE 195
PRK06101 PRK06101
SDR family oxidoreductase;
32-236 9.35e-09

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 54.88  E-value: 9.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELrNKTSDRLETVILDVTKTESIVAATQwvkervgnrglwglvn 111
Cdd:PRK06101   4 VLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDEL-HTQSANIFTLAFDVTDHPGTKAALS---------------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 112 nagiSTPSGPNEW--------------MKKQDFARVLDVNLLGMIEVTLSMLPLVRKARgRVVNVSSVMGRMSF-FGGGY 176
Cdd:PRK06101  67 ----QLPFIPELWifnagdceymddgkVDATLMARVFNVNVLGVANCIEGIQPHLSCGH-RVVIVGSIASELALpRAEAY 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 165377241 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTssDRLSSNTKMI--WDKASSEVKE 236
Cdd:PRK06101 142 GASKAAVAYFARTLQLDLRPKGIEVVTVFPGFVATPLT--DKNTFAMPMIitVEQASQEIRA 201
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 32-211 1.54e-08

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


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 54.07  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEELRNKTSDRLE-TVILDVTKTESIVAATQwvkeRVGNRGLWglV 110
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLL---LSGRDAGALAGLAAEVGAlARPADVAAELEVWALAQ----ELGPLDLL--V 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 111 NNAGISTPSgPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVrKARGRVVNVSSVMGRMSFFG-GGYCISKYGVEAFSDS 189
Cdd:cd11730   72 YAAGAILGK-PLARTKPAAWRRILDANLTGAALVLKHALALL-AAGARLVFLGAYPELVMLPGlSAYAAAKAALEAYVEV 149

                        170       180
                 ....*....|....*....|..
gi 165377241 190 LRRELSyfGVKVAIIEPGGFKT 211
Cdd:cd11730  150 ARKEVR--GLRLTLVRPPAVDT 169
PRK07035 PRK07035
SDR family oxidoreductase;
27-211 1.56e-08

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 54.64  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV------LAACltEKGAEELRNKtSDRLETVILDVTKTESIVAATQWVKER 100
Cdd:PRK07035   6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVivssrkLDGC--QAVADAIVAA-GGKAEALACHIGEMEQIDALFAHIRER 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 101 VGNrgLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVMG-RMSFFGGGYCI 178
Cdd:PRK07035  83 HGR--LDILVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEqGGGSIVNVASVNGvSPGDFQGIYSI 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 165377241 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK07035 161 TKAAVISMTKAFAKECAPFGIRVNALLPGLTDT 193
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 27-207 3.01e-08

(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: 53.48  E-value: 3.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLteKGAEELRNKTSDRLETVILDVTK--------TESIVAATQWVK 98
Cdd:cd05353    3 FDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDL--GGDRKGSGKSSSAADKVVDEIKAaggkavanYDSVEDGEKIVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  99 ERVGNRG-LWGLVNNAGI----STPSgpnewMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRMSFF 172
Cdd:cd05353   81 TAIDAFGrVDILVNNAGIlrdrSFAK-----MSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKfGRIINTSSAAGLYGNF 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 165377241 173 G-GGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:cd05353  156 GqANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA 191
PRK06500 PRK06500
SDR family oxidoreductase;
25-207 3.85e-08

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 53.42  E-value: 3.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  25 SHLQDKYVFITGCDSGFGNLLARQLDRRGMRV---------LAACLTEKGAEEL--RNKTSDrletvildvtktesiVAA 93
Cdd:PRK06500   2 SRLQGKTALITGGTSGIGLETARQFLAEGARVaitgrdpasLEAARAELGESALviRADAGD---------------VAA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  94 TQWVKERVGNRG--LWGLVNNAGISTpSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVS-SV---MG 167
Cdd:PRK06500  67 QKALAQALAEAFgrLDAVFINAGVAK-FAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPASIVLNGSiNAhigMP 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 165377241 168 RMSFfgggYCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK06500 146 NSSV----YAASKAALLSLAKTLSGELLPRGIRVNAVSPG 181
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 28-241 4.37e-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: 53.24  E-value: 4.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAACL----TEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGN 103
Cdd:cd05322    1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADInsenAEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 RGLwgLVNNAGISTpSGPNEWMKKQDFARVLDVNLLG--MIEVTLSMLPLVRKARGRVVNVSSVMGRM-SFFGGGYCISK 180
Cdd:cd05322   81 VDL--LVYSAGIAK-SAKITDFELGDFDRSLQVNLVGyfLCAREFSKLMIRDGIQGRIIQINSKSGKVgSKHNSGYSAAK 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 165377241 181 YGVEAFSDSLRRELSYFGVKVAIIEPGGFktcvTSSDRLSSNTKMIWDK---ASSEVKEIYGEK 241
Cdd:cd05322  158 FGGVGLTQSLALDLAEHGITVNSLMLGNL----LKSPMFQSLLPQYAKKlgiKESEVEQYYIDK 217
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 27-211 6.18e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 52.88  E-value: 6.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRV---------LAACLTEKGAeeLRNKTSDRLETVilDVTKTESIVAATQWV 97
Cdd:PRK05875   5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVmivgrnpdkLAAAAEEIEA--LKGAGAVRYEPA--DVTDEDQVARAVDAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  98 KERVGnrGLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLG-MIEVTLSMLPLVRKARGRVVNVSSVMGRMS--FFgG 174
Cdd:PRK05875  81 TAWHG--RLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGtMYVLKHAARELVRGGGGSFVGISSIAASNThrWF-G 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 165377241 175 GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK05875 158 AYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRT 194
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 30-211 6.99e-08

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: 52.58  E-value: 6.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnrGLWGL 109
Cdd:cd09761    2 KVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLG--RIDVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 110 VNNAGISTPsGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRMSFFGG-GYCISKYGVEAFSD 188
Cdd:cd09761   80 VNNAARGSK-GILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAFQSEPDSeAYAASKGGLVALTH 158

                        170       180
                 ....*....|....*....|...
gi 165377241 189 SLRRELSYFgVKVAIIEPGGFKT 211
Cdd:cd09761  159 ALAMSLGPD-IRVNCISPGWINT 180
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 32-211 9.40e-08

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: 52.19  E-value: 9.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAeelrNKTSDRLET-------VILDVTKTESIVAATQWVKERVGnr 104
Cdd:cd05365    2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGA----EAVAAAIQQaggqaigLECNVTSEQDLEAVVKATVSQFG-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 105 GLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMG-----RMSFFGGgyci 178
Cdd:cd05365   76 GITILVNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGgGAILNISSMSSenknvRIAAYGS---- 151

                        170       180       190
                 ....*....|....*....|....*....|...
gi 165377241 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd05365  152 SKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKT 184
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 30-215 1.18e-07

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: 52.39  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFG-----NLLARQLDRRGMRVLAACLTEKGAEELRNKTSD-------RLETVILDVTKTESIVAATQWV 97
Cdd:cd08941    2 KVVLVTGANSGLGlaiceRLLAEDDENPELTLILACRNLQRAEAACRALLAshpdarvVFDYVLVDLSNMVSVFAAAKEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  98 KERVgnRGLWGLVNNAGIstpsGPNE---W-------------------MKKQ--------------DFARVLDVNLLGM 141
Cdd:cd08941   82 KKRY--PRLDYLYLNAGI----MPNPgidWigaikevltnplfavtnptYKIQaegllsqgdkatedGLGEVFQTNVFGH 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 142 IEVTLSMLPLVRKAR--GRVVNVSSVMGRMSFFG----------GGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGF 209
Cdd:cd08941  156 YYLIRELEPLLCRSDggSQIIWTSSLNASPKYFSlediqhlkgpAPYSSSKYLVDLLSLALNRKFNKLGVYSYVVHPGIC 235


                 ....*.
gi 165377241 210 KTCVTS 215
Cdd:cd08941  236 TTNLTY 241
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 34-216 1.27e-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: 51.69  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  34 ITGCDSGFGNLLARQLDRRGMRVL------AACLTEKGAEELR-NKTSDRLETVILDVTKTESIVAATQwvkERVGnrGL 106
Cdd:cd05337    6 VTGASRGIGRAIATELAARGFDIAindlpdDDQATEVVAEVLAaGRRAIYFQADIGELSDHEALLDQAW---EDFG--RL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 WGLVNNAGISTPsgpnewmKKQD--------FARVLDVNLLGMI----EVTLSML--PLVRKA-RGRVVNVSSVMGRM-S 170
Cdd:cd05337   81 DCLVNNAGIAVR-------PRGDlldltedsFDRLIAINLRGPFfltqAVARRMVeqPDRFDGpHRSIIFVTSINAYLvS 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 165377241 171 FFGGGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSS 216
Cdd:cd05337  154 PNRGEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAP 199
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 27-218 1.96e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 51.57  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKG-AEElrnkTSDRLE-------TVILDVTKT---ESIVAATq 95
Cdd:PRK06701  44 LKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEdANE----TKQRVEkegvkclLIPGDVSDEafcKDAVEET- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  96 wVKErVGnrGLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVrKARGRVVNVSSVMGRMsffGGG 175
Cdd:PRK06701 119 -VRE-LG--RLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL-KQGSAIINTGSITGYE---GNE 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 165377241 176 ----YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSSDR 218
Cdd:PRK06701 191 tlidYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPLIPSDF 237
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-218 2.56e-07

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 51.03  E-value: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE-KGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRG 105
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEpTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEFGHID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 106 LwgLVNNAGISTPSGPNEWmKKQDFARVLDVNllgmIEVTLSMLPLVRKA------RGRVVNVSSVmgrMSFFGG----G 175
Cdd:PRK08993  88 I--LVNNAGLIRREDAIEF-SEKDWDDVMNLN----IKSVFFMSQAAAKHfiaqgnGGKIINIASM---LSFQGGirvpS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 165377241 176 YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSSDR 218
Cdd:PRK08993 158 YTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLR 200
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 32-211 2.67e-07

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: 50.84  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVIL----DVTKTESIVAATQWVKERVGNRGLw 107
Cdd:cd05373    2 AAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKavptDARDEDEVIALFDLIEEEIGPLEV- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 108 gLVNNAGISTPSGPNEwMKKQDFARVLDVNLLGMI----EVTLSMLPlvrKARGRVV---NVSSVMGRMSF--FGGGyci 178
Cdd:cd05373   81 -LVYNAGANVWFPILE-TTPRVFEKVWEMAAFGGFlaarEAAKRMLA---RGRGTIIftgATASLRGRAGFaaFAGA--- 152

                        170       180       190
                 ....*....|....*....|....*....|....
gi 165377241 179 sKYGVEAFSDSLRRELSYFGVKVA-IIEPGGFKT 211
Cdd:cd05373  153 -KFALRALAQSMARELGPKGIHVAhVIIDGGIDT 185
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 27-211 3.13e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 50.70  E-value: 3.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLaacLTEKGAEELrnktsDRL---------ETVIL--DVTKTESIVAATQ 95
Cdd:PRK07478   4 LNGKVAIITGASSGIGRAAAKLFAREGAKVV---VGARRQAEL-----DQLvaeiraeggEAVALagDVRDEAYAKALVA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  96 WVKERVGnrGLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMSFFGG 174
Cdd:PRK07478  76 LAVERFG--GLDIAFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPaMLARGGGSLIFTSTFVGHTAGFPG 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 165377241 175 --GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK07478 154 maAYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDT 192
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-216 4.70e-07

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 50.09  E-value: 4.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACL-TEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGnRG 105
Cdd:PRK08642   3 ISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHqSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEHFG-KP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 106 LWGLVNNA-------GISTPSGPN-EWmkkQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSvmgrmSFFGG-- 174
Cdd:PRK08642  82 ITTVVNNAladfsfdGDARKKADDiTW---EDFQQQLEGSVKGALNTIQAALPGMREQGfGRIINIGT-----NLFQNpv 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 165377241 175 ----GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSS 216
Cdd:PRK08642 154 vpyhDYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTTDASA 199
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 27-211 5.24e-07

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 50.15  E-value: 5.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVL-----AACLtEKGAEELRNKTSDrLETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVIlngrdPAKL-AAAAESLKGQGLS-AHALAFDVTDHDAVRAAIDAFEAEI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 102 GNRGLwgLVNNAGISTPSgPNEWMKKQDFARVLDVNLLGMIEVTLSML-PLVRKARGRVVNVSSVMGRMSFFG-GGYCIS 179
Cdd:PRK07523  86 GPIDI--LVNNAGMQFRT-PLEDFPADAFERLLRTNISSVFYVGQAVArHMIARGAGKIINIASVQSALARPGiAPYTAT 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 165377241 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK07523 163 KGAVGNLTKGMATDWAKHGLQCNAIAPGYFDT 194
PRK05854 PRK05854
SDR family oxidoreductase;
27-168 6.15e-07

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 50.06  E-value: 6.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTE-KG---AEELRNKTSD-RLETVILDVTKTESIVAATQWVKERv 101
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRaKGeaaVAAIRTAVPDaKLSLRALDLSSLASVAALGEQLRAE- 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 165377241 102 gNRGLWGLVNNAGISTPsgPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGR 168
Cdd:PRK05854  91 -GRPIHLLINNAGVMTP--PERQTTADGFELQFGTNHLGHFALTAHLLPLLRAGRARVTSQSSIAAR 154
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 30-207 7.37e-07

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: 49.41  E-value: 7.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKtesiVAATQWVKERVGNRGLW-G 108
Cdd:cd08951    8 KRIFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSS----LAETRKLADQVNAIGRFdA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 109 LVNNAGIStpSGPNEWMKKQDFARVLDVNLLGMIEVTlsmlPLVRKARgRVVNVSSVMGR--------MSFFG------G 174
Cdd:cd08951   84 VIHNAGIL--SGPNRKTPDTGIPAMVAVNVLAPYVLT----ALIRRPK-RLIYLSSGMHRggnaslddIDWFNrgendsP 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 165377241 175 GYCISKYGVEAFSDSLRRelSYFGVKVAIIEPG 207
Cdd:cd08951  157 AYSDSKLHVLTLAAAVAR--RWKDVSSNAVHPG 187
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-218 1.05e-06

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 49.13  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAacLTEKGAEELRNK---TSDRLETVILDVTKTESIVAATQWVKERVGN 103
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVG--VGVAEAPETQAQveaLGRKFHFITADLIQQKDIDSIVSQAVEVMGH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 RGLwgLVNNAGISTPSGPNEWmKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR--GRVVNVSSVMgrmSFFGG----GYC 177
Cdd:PRK12481  84 IDI--LINNAGIIRRQDLLEF-GNKDWDDVININQKTVFFLSQAVAKQFVKQGngGKIINIASML---SFQGGirvpSYT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 165377241 178 ISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSSDR 218
Cdd:PRK12481 158 ASKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAALR 198
PRK08278 PRK08278
SDR family oxidoreductase;
27-201 1.32e-06

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 48.75  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMR-VLAACLTEK----------GAEELRNKTSDRLeTVILDVTKTESIVAATQ 95
Cdd:PRK08278   4 LSGKTLFITGASRGIGLAIALRAARDGANiVIAAKTAEPhpklpgtihtAAEEIEAAGGQAL-PLVGDVRDEDQVAAAVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  96 WVKERVGnrGLWGLVNNAG-ISTPSGPNEWMKKQDFarVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMgRMS--F 171
Cdd:PRK08278  83 KAVERFG--GIDICVNNASaINLTGTEDTPMKRFDL--MQQINVRGTFLVSQACLPHLKKSEnPHILTLSPPL-NLDpkW 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 165377241 172 FGG--GYCISKYGVEAFSDSLRRELSYFGVKV 201
Cdd:PRK08278 158 FAPhtAYTMAKYGMSLCTLGLAEEFRDDGIAV 189
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-207 1.60e-06

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 49.06  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLaaCLTEKGAEELRNKTSDRL--ETVILDVTKTESIVAATQWVKERVGnr 104
Cdd:PRK08261 208 LAGKVALVTGAARGIGAAIAEVLARDGAHVV--CLDVPAAGEALAAVANRVggTALALDITAPDAPARIAEHLAERHG-- 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 105 GLWGLVNNAGIS---TpsgpnewMKKQDFAR---VLDVNLLGMIEVTLSML-PLVRKARGRVVNVSSVMGRMSFFG-GGY 176
Cdd:PRK08261 284 GLDIVVHNAGITrdkT-------LANMDEARwdsVLAVNLLAPLRITEALLaAGALGDGGRIVGVSSISGIAGNRGqTNY 356

                        170       180       190
                 ....*....|....*....|....*....|.
gi 165377241 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK08261 357 AASKAGVIGLVQALAPLLAERGITINAVAPG 387
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 27-233 1.76e-06

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: 48.31  E-value: 1.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEelrnKTSDRLETVILDVTKT----------ESIVAATQw 96
Cdd:cd08936    8 LANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVD----RAVATLQGEGLSVTGTvchvgkaedrERLVATAV- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  97 vkERVGnrGLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVMGRMSFFG-G 174
Cdd:cd08936   83 --NLHG--GVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKrGGGSVVIVSSVAAFHPFPGlG 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 175 GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTcvtssdrlsSNTKMIW-DKASSE 233
Cdd:cd08936  159 PYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKT---------SFSSALWmDKAVEE 209
PRK07062 PRK07062
SDR family oxidoreductase;
27-168 1.81e-06

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 48.50  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVlAACLTE----KGAE-ELRNKTSD-RLETVILDVTKTESIVAATQWVKER 100
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASV-AICGRDeerlASAEaRLREKFPGaRLLAARCDVLDEADVAAFAAAVEAR 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 165377241 101 VGnrGLWGLVNNAG---IST-PSGPNE-WMKKqdfarvLDVNLLGMIEVTLSMLPLVRKA-RGRVVNVSSVMGR 168
Cdd:PRK07062  85 FG--GVDMLVNNAGqgrVSTfADTTDDaWRDE------LELKYFSVINPTRAFLPLLRASaAASIVCVNSLLAL 150
PRK08177 PRK08177
SDR family oxidoreductase;
30-211 2.90e-06

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 47.33  E-value: 2.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETviLDVTKTESIVAATQWVKERVGNRglwgL 109
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIEK--LDMNDPASLDQLLQRLQGQRFDL----L 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 110 VNNAGISTPSG-PNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRMSFFGGG----YCISKYGVE 184
Cdd:PRK08177  76 FVNAGISGPAHqSAADATAAEIGQLFLTNAIAPIRLARRLLGQVRPGQGVLAFMSSQLGSVELPDGGemplYKASKAALN 155

                        170       180
                 ....*....|....*....|....*..
gi 165377241 185 AFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK08177 156 SMTRSFVAELGEPTLTVLSMHPGWVKT 182
PRK05867 PRK05867
SDR family oxidoreductase;
27-211 4.28e-06

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 47.34  E-value: 4.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAClteKGAEELRnKTSDRLE-------TVILDVTKTESIVAATQWVKE 99
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAA---RHLDALE-KLADEIGtsggkvvPVCCDVSQHQQVTSMLDQVTA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 100 RVGnrGLWGLVNNAGISTPSGPNEwMKKQDFARVLDVNLLGM-IEVTLSMLPLVRKARG-RVVNVSSVMGRMSFFG---G 174
Cdd:PRK05867  83 ELG--GIDIAVCNAGIITVTPMLD-MPLEEFQRLQNTNVTGVfLTAQAAAKAMVKQGQGgVIINTASMSGHIINVPqqvS 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 165377241 175 GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK05867 160 HYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILT 196
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 27-211 5.32e-06

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: 47.06  E-value: 5.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVL----AACLTEKG-AEELRnKTSDRLETVILDVTKTESIVAATQWVKERV 101
Cdd:cd09763    1 LSGKIALVTGASRGIGRGIALQLGEAGATVYitgrTILPQLPGtAEEIE-ARGGKCIPVRCDHSDDDEVEALFERVAREQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 102 GNRgLWGLVNNA------GISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKA-RGRVVNVSSVMGRMSFFGG 174
Cdd:cd09763   80 QGR-LDILVNNAyaavqlILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAgKGLIVIISSTGGLEYLFNV 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 165377241 175 GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:cd09763  159 AYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRT 195
PRK07814 PRK07814
SDR family oxidoreductase;
27-180 6.15e-06

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 46.70  E-value: 6.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVAATQWVKERVGN 103
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAagrRAHVVAADLAHPEATAGLAGQAVEAFGR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 104 RGLwgLVNNAGISTPSgPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRK--ARGRVVNVSSVMGRMSFFG-GGYCISK 180
Cdd:PRK07814  88 LDI--VVNNVGGTMPN-PLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEhsGGGSVINISSTMGRLAGRGfAAYGTAK 164
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 34-169 6.21e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 46.94  E-value: 6.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  34 ITGCDSGFGNLLARQLDRRGMRV-LAACLTEKG---AEELRNKTSDRLETVI-LDVTKTESIVAATQWVKERVGNRGLwg 108
Cdd:PRK06197  21 VTGANTGLGYETAAALAAKGAHVvLAVRNLDKGkaaAARITAATPGADVTLQeLDLTSLASVRAAADALRAAYPRIDL-- 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 165377241 109 LVNNAGISTPsgPNEwMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARG-RVVNVSSVMGRM 169
Cdd:PRK06197  99 LINNAGVMYT--PKQ-TTADGFELQFGTNHLGHFALTGLLLDRLLPVPGsRVVTVSSGGHRI 157
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 27-207 7.42e-06

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: 46.52  E-value: 7.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKgaEELRNKTSDRLET-----VIL--DVTKTESIVAATQWVKE 99
Cdd:cd05355   24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEE--EDDAEETKKLIEEegrkcLLIpgDLGDESFCRDLVKEVVK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 100 RVGnrGLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKArGRVVNVSSVMGrmsFFGGG---- 175
Cdd:cd05355  102 EFG--KLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKKG-SSIINTTSVTA---YKGSPhlld 175

                        170       180       190
                 ....*....|....*....|....*....|..
gi 165377241 176 YCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:cd05355  176 YAATKGAIVAFTRGLSLQLAEKGIRVNAVAPG 207
PRK09730 PRK09730
SDR family oxidoreductase;
34-237 7.77e-06

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 46.38  E-value: 7.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  34 ITGCDSGFGNLLARQLDRRGMRVLAACL-TEKGAEELRNK---TSDRLETVILDVTKTESIVAATQWVKERVGNrgLWGL 109
Cdd:PRK09730   6 VTGGSRGIGRATALLLAQEGYTVAVNYQqNLHAAQEVVNLitqAGGKAFVLQADISDENQVVAMFTAIDQHDEP--LAAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 110 VNNAGISTPSGPNEWMKKQDFARVLDVNLLGMI----EVTLSMLPLVRKARGRVVNVSSVMGRMSFFGG--GYCISKYGV 183
Cdd:PRK09730  84 VNNAGILFTQCTVENLTAERINRVLSTNVTGYFlccrEAVKRMALKHGGSGGAIVNVSSAASRLGAPGEyvDYAASKGAI 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 165377241 184 EAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSS-------DRLSSNTKMIWDKASSEVKEI 237
Cdd:PRK09730 164 DTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASggepgrvDRVKSNIPMQRGGQPEEVAQA 224
PRK09186 PRK09186
flagellin modification protein A; Provisional
 27-167 1.13e-05

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 46.14  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEEL-----RNKTSDRLETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELleslgKEFKSKKLSLVELDITDQESLEEFLSKSAEKY 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 165377241 102 GNrgLWGLVNNAgisTPSGPNeWMKK------QDFARVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMG 167
Cdd:PRK09186  82 GK--IDGAVNCA---YPRNKD-YGKKffdvslDDFNENLSLHLGSSFLFSQQFAKyFKKQGGGNLVNISSIYG 148
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 32-174 1.38e-05

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 45.97  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGM-RVLAACLTEKGAEELRNKT---SDRLETVILDVTKTESIvaaTQWVKE-RVGNRGL 106
Cdd:cd09810    4 VVITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQEVgmpKDSYSVLHCDLASLDSV---RQFVDNfRRTGRPL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 165377241 107 WGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARG---RVVNVSSVMGRMSFFGG 174
Cdd:cd09810   81 DALVCNAAVYLPTAKEPRFTADGFELTVGVNHLGHFLLTNLLLEDLQRSENaspRIVIVGSITHNPNTLAG 151
PRK07856 PRK07856
SDR family oxidoreductase;
27-193 1.40e-05

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 45.69  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNktsdrLETVILDVTKTESIVAATQWVKERVGnrGL 106
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETVDGRP-----AEFHAADVRDPDQVAALVDAIVERHG--RL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 107 WGLVNNAGIStPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRK--ARGRVVNVSSVMG-RMSFFGGGYCISKYGV 183
Cdd:PRK07856  77 DVLVNNAGGS-PYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQqpGGGSIVNIGSVSGrRPSPGTAAYGAAKAGL 155

                        170
                 ....*....|
gi 165377241 184 EAFSDSLRRE 193
Cdd:PRK07856 156 LNLTRSLAVE 165
PRK05717 PRK05717
SDR family oxidoreductase;
30-207 1.43e-05

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 45.65  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAAtqwVKERVGNRG-LWG 108
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFIAMDVADEAQVAAG---VAEVLGQFGrLDA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 109 LVNNAGISTP-SGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRMSFFGG-GYCISKYGVEAF 186
Cdd:PRK05717  88 LVCNAAIADPhNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHNGAIVNLASTRARQSEPDTeAYAASKGGLLAL 167

                        170       180
                 ....*....|....*....|.
gi 165377241 187 SDSLRRELSYfGVKVAIIEPG 207
Cdd:PRK05717 168 THALAISLGP-EIRVNAVSPG 187
PRK09135 PRK09135
pteridine reductase; Provisional
 28-207 1.78e-05

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 45.30  E-value: 1.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  28 QDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLT-----EKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVG 102
Cdd:PRK09135   5 SAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRsaaeaDALAAELNALRPGSAAALQADLLDPDALPELVAACVAAFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 103 nrGLWGLVNNAG--ISTPSG---PNEWmkkQDfarVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRMSFFGGG-Y 176
Cdd:PRK09135  85 --RLDALVNNASsfYPTPLGsitEAQW---DD---LFASNLKAPFFLSQAAAPQLRKQRGAIVNITDIHAERPLKGYPvY 156

                        170       180       190
                 ....*....|....*....|....*....|.
gi 165377241 177 CISKYGVEAFSDSLRRELSYfGVKVAIIEPG 207
Cdd:PRK09135 157 CAAKAALEMLTRSLALELAP-EVRVNAVAPG 186
PRK06128 PRK06128
SDR family oxidoreductase;
27-216 4.17e-05

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 44.46  E-value: 4.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACL--TEKGAEELRN--KTSDRLETVILDVTKTESIvaATQWVKERV- 101
Cdd:PRK06128  53 LQGRKALITGADSGIGRATAIAFAREGADIALNYLpeEEQDAAEVVQliQAEGRKAVALPGDLKDEAF--CRQLVERAVk 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 102 GNRGLWGLVNNAGISTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVrKARGRVVNVSSVMG-RMSFFGGGYCISK 180
Cdd:PRK06128 131 ELGGLDILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHL-PPGASIINTGSIQSyQPSPTLLDYASTK 209

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 165377241 181 YGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSS 216
Cdd:PRK06128 210 AAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPS 245
PRK07985 PRK07985
SDR family oxidoreductase;
27-207 4.84e-05

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 44.22  E-value: 4.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACL--TEKGAEELRNKTSDRLETVIL---DVTKTESIVAATQWVKERV 101
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISYLpvEEEDAQDVKKIIEECGRKAVLlpgDLSDEKFARSLVHEAHKAL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 102 GNRGLWGLVNNAGISTPSGPNewMKKQDFARVLDVNLLGMIEVTLSMLPLVRKArGRVVNVSSVMG-RMSFFGGGYCISK 180
Cdd:PRK07985 127 GGLDIMALVAGKQVAIPDIAD--LTSEQFQKTFAINVFALFWLTQEAIPLLPKG-ASIITTSSIQAyQPSPHLLDYAATK 203

                        170       180
                 ....*....|....*....|....*..
gi 165377241 181 YGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK07985 204 AAILNYSRGLAKQVAEKGIRVNIVAPG 230
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 34-164 6.14e-05

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: 43.74  E-value: 6.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  34 ITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRN---KTSDRLETV--ILDVTKTESIVAATQWVKERvgNRGLWG 108
Cdd:cd09808    6 ITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKeieTESGNQNIFlhIVDMSDPKQVWEFVEEFKEE--GKKLHV 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 165377241 109 LVNNAG-ISTPSGPNEWMKKQDFArvldVNLLGMIEVTLSMLPLVRKARG-RVVNVSS 164
Cdd:cd09808   84 LINNAGcMVNKRELTEDGLEKNFA----TNTLGTYILTTHLIPVLEKEEDpRVITVSS 137
PRK06196 PRK06196
oxidoreductase; Provisional
 27-170 8.86e-05

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 43.52  E-value: 8.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVL-AACLTEKGAEELRNktSDRLETVILDVTKTESIVA-ATQWVKERvgnR 104
Cdd:PRK06196  24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIvPARRPDVAREALAG--IDGVEVVMLDLADLESVRAfAERFLDSG---R 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 165377241 105 GLWGLVNNAGI----STPSGPNEWMKkqdFArvldVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRMS 170
Cdd:PRK06196  99 RIDILINNAGVmacpETRVGDGWEAQ---FA----TNHLGHFALVNLLWPaLAAGAGARVVALSSAGHRRS 162
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 1-220 1.79e-04

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 42.55  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241   1 MWLYLVALVGLWTLLRFFRE--RQV-VSHLQ-----DKY---VFITGCDSGFGNLLARQLDRRGMR-VLAACLTEK---G 65
Cdd:PLN02780  14 LWLLVLFVLGSLSILKFFFTilNWVyVYFLRpaknlKKYgswALVTGPTDGIGKGFAFQLARKGLNlVLVARNPDKlkdV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  66 AEELRNKTSD-RLETVILDVTKteSIVAATQWVKERVGNRGLWGLVNNAGISTPSGpnEWMKKQD---FARVLDVNLLGM 141
Cdd:PLN02780  94 SDSIQSKYSKtQIKTVVVDFSG--DIDEGVKRIKETIEGLDVGVLINNVGVSYPYA--RFFHEVDeelLKNLIKVNVEGT 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 142 IEVTLSMLP-LVRKARGRVVNVSS----VMGRMSFFgGGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSS 216
Cdd:PLN02780 170 TKVTQAVLPgMLKRKKGAIINIGSgaaiVIPSDPLY-AVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMASI 248


                 ....
gi 165377241 217 DRLS 220
Cdd:PLN02780 249 RRSS 252
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-206 1.93e-04

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 42.46  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVL-----AACLTEKGAEELRNKTSdRLETVILDVTKTESivaATQWVKERV 101
Cdd:PRK07792  10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVvndvaSALDASDVLDEIRAAGA-KAVAVAGDISQRAT---ADELVATAV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 102 GNRGLWGLVNNAGIsTPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVR-KAR-------GRVVNVSSVMGRMSFFG 173
Cdd:PRK07792  86 GLGGLDIVVNNAGI-TRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRaKAKaaggpvyGRIVNTSSEAGLVGPVG 164

                        170       180       190
                 ....*....|....*....|....*....|....
gi 165377241 174 -GGYCISKYGVEAFSDSLRRELSYFGVKVAIIEP 206
Cdd:PRK07792 165 qANYGAAKAGITALTLSAARALGRYGVRANAICP 198
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-211 2.89e-04

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 41.63  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAclTEKGAEE-------LRNKTSDRLeTVILDVTKTEsivAATQWVKE 99
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVN--AKKRAEEmnetlkmVKENGGEGI-GVLADVSTRE---GCETLAKA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 100 RVGN-RGLWGLVNNAGISTPSgpnEWMKKQD--FARVLDVNLLGMIEVTLSMLPLVRKArGRVVNVSSVMGRMSFFG-GG 175
Cdd:PRK06077  78 TIDRyGVADILVNNAGLGLFS---PFLNVDDklIDKHISTDFKSVIYCSQELAKEMREG-GAIVNIASVAGIRPAYGlSI 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 165377241 176 YCISKYGVEAFSDSLRRELSYfGVKVAIIEPGGFKT 211
Cdd:PRK06077 154 YGAMKAAVINLTKYLALELAP-KIRVNAIAPGFVKT 188
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 30-207 4.13e-04

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


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 41.11  E-value: 4.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  30 KYVFITGCDSGFGNLLARQLDRRGMRVLAACLT-EKGAEELR---NKTSDRLETVILDVTKTESIVAATQWVKERVGNRG 105
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRsEAEAQRLKdelNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 106 LwgLVNNAGI--STPSGPNEWmkkQDFARVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVM---GRMSFFGggYCIS 179
Cdd:cd05357   81 V--LVNNASAfyPTPLGQGSE---DAWAELFGINLKAPYLLIQAFARRLAGsRNGSIINIIDAMtdrPLTGYFA--YCMS 153

                        170       180
                 ....*....|....*....|....*...
gi 165377241 180 KYGVEAFSDSLRRELSYFgVKVAIIEPG 207
Cdd:cd05357  154 KAALEGLTRSAALELAPN-IRVNGIAPG 180
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
27-211 4.32e-04

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 41.24  E-value: 4.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGA-----EELRnKTSDRLETVILDVTKTESIVAATQWVKERV 101
Cdd:PRK08063   2 FSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAaeetaEEIE-ALGRKALAVKANVGDVEKIKEMFAQIDEEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 102 GnrGLWGLVNNAGistpSG---PNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSS-----VMGRMSFF 172
Cdd:PRK08063  81 G--RLDVFVNNAA----SGvlrPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGgGKIISLSSlgsirYLENYTTV 154

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 165377241 173 GggycISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKT 211
Cdd:PRK08063 155 G----VSKAALEALTRYLAVELAPKGIAVNAVSGGAVDT 189
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 27-182 5.12e-04

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 40.89  E-value: 5.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEK-----------GAEELRNKTSDRLeTVILDVTKTESIVAATQ 95
Cdd:cd09762    1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEphpklpgtiytAAEEIEAAGGKAL-PCIVDIRDEDQVRAAVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  96 WVKERVGnrGLWGLVNNA-GISTPSGPNEWMKKQDFarVLDVNLLGMIEVTLSMLPLVRKARG-RVVNVSSVMG-RMSFF 172
Cdd:cd09762   80 KAVEKFG--GIDILVNNAsAISLTGTLDTPMKRYDL--MMGVNTRGTYLCSKACLPYLKKSKNpHILNLSPPLNlNPKWF 155

                        170
                 ....*....|..
gi 165377241 173 GG--GYCISKYG 182
Cdd:cd09762  156 KNhtAYTMAKYG 167
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 25-207 5.14e-04

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 40.83  E-value: 5.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  25 SHLQDKYVFITGCD--SGFGNLLARQLDRRGMRVLAACLTEKGAE--------------ELRNKTSDRLETVILDVTKTE 88
Cdd:PRK12748   1 LPLMKKIALVTGASrlNGIGAAVCRRLAAKGIDIFFTYWSPYDKTmpwgmhdkepvllkEEIESYGVRCEHMEIDLSQPY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  89 SIVAATQWVKERVGNRGLwgLVNNAGISTPSGPNEwmkkqdfarvLDVNLLG---MIEVTLSMLpLVR--------KARG 157
Cdd:PRK12748  81 APNRVFYAVSERLGDPSI--LINNAAYSTHTRLEE----------LTAEQLDkhyAVNVRATML-LSSafakqydgKAGG 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 165377241 158 RVVNVSS--VMGRMSffgG--GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK12748 148 RIINLTSgqSLGPMP---DelAYAATKGAIEAFTKSLAPELAEKGITVNAVNPG 198
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 29-164 1.53e-03

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: 39.50  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  29 DKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEE-----LRNKTSDRLETVILDVTKTESIVAATQWVKERvgN 103
Cdd:cd09809    1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAavsriLEEWHKARVEAMTLDLASLRSVQRFAEAFKAK--N 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 165377241 104 RGLWGLVNNAGISTPSgpneWMKKQD-FARVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSS 164
Cdd:cd09809   79 SPLHVLVCNAAVFALP----WTLTEDgLETTFQVNHLGHFYLVQLLEDVLRRsAPARVIVVSS 137
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 66-207 2.14e-03

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 39.00  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  66 AEELRnKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLwgLVNNAGISTpsgpnewmkKQDF----ARVLD----VN 137
Cdd:PRK12859  60 QEELL-KNGVKVSSMELDLTQNDAPKELLNKVTEQLGYPHI--LVNNAAYST---------NNDFsnltAEELDkhymVN 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 165377241 138 LLGMIEVTLSMLPLVRKARG-RVVNVSSVMGRMSFFGG-GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK12859 128 VRATTLLSSQFARGFDKKSGgRIINMTSGQFQGPMVGElAYAATKGAIDALTSSLAAEVAHLGITVNAINPG 199
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 27-207 2.96e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 38.78  E-value: 2.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFgNL-LARQLDRRGMRV------------LAACLTEKGAEELrnktsdrleTVILDVTKTESIVAA 93
Cdd:PRK07576   7 FAGKNVVVVGGTSGI-NLgIAQAFARAGANVavasrsqekvdaAVAQLQQAGPEGL---------GVSADVRDYAAVEAA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  94 TQWVKERVGNRGLwgLVNNAGISTPSgPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRMSFFG 173
Cdd:PRK07576  77 FAQIADEFGPIDV--LVSGAAGNFPA-PAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPGASIIQISAPQAFVPMPM 153

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 165377241 174 GGY-CISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK07576 154 QAHvCAAKAGVDMLTRTLALEWGPEGIRVNSIVPG 188
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 31-218 3.77e-03

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 38.35  E-value: 3.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241   31 YVFITGCDSGFGNLLARQLDRR-----GMRVLAA---CLTEKGAEELRNKTSD-RLETVILDVTKTESIVAATQWVKERV 101
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKClkspgSVLVLSArndEALRQLKAEIGAERSGlRVVRVSLDLGAEAGLEQLLKALRELP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  102 GNRGLWG--LVNNAGI--STPSGPNEWMKKQDFARVLDVNLLGMIEVTLSMLPLVRKARG---RVVNVSSVMGRMSFFGG 174
Cdd:TIGR01500  82 RPKGLQRllLINNAGTlgDVSKGFVDLSDSTQVQNYWALNLTSMLCLTSSVLKAFKDSPGlnrTVVNISSLCAIQPFKGW 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 165377241  175 G-YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGGFKTCVTSSDR 218
Cdd:TIGR01500 162 AlYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQQVR 206
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
45-167 4.20e-03

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 38.06  E-value: 4.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  45 LARQLDRRGMRVLAACLTEKGAEelrnktsdrLETVI-LDVTKTESIVAATQWVKERVGnrglwGLVNNAGIStPSGPNE 123
Cdd:PRK12428   1 TARLLRFLGARVIGVDRREPGMT---------LDGFIqADLGDPASIDAAVAALPGRID-----ALFNIAGVP-GTAPVE 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 165377241 124 wmkkqdfaRVLDVNLLGMIEVTLSMLPLVRkARGRVVNVSSVMG 167
Cdd:PRK12428  66 --------LVARVNFLGLRHLTEALLPRMA-PGGAIVNVASLAG 100
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 27-174 5.93e-03

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. 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: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 38.13  E-value: 5.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  27 LQDKYVFITGCDSGFGNLLARQLDRRGMRVLAAC------LTEKGAEELRNKTSDRLETVILDVTKTEsivAATQWVKER 100
Cdd:cd05274  148 GLDGTYLITGGLGGLGLLVARWLAARGARHLVLLsrrgpaPRAAARAALLRAGGARVSVVRCDVTDPA---ALAALLAEL 224

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 165377241 101 VGNRGLWGLVNNAGISTPsGPNEWMKKQDFARVLDVNLLGmievTLSMLPLVRKARG-RVVNVSSVmgrMSFFGG 174
Cdd:cd05274  225 AAGGPLAGVIHAAGVLRD-ALLAELTPAAFAAVLAAKVAG----ALNLHELTPDLPLdFFVLFSSV---AALLGG 291
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 32-209 6.74e-03

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


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 37.22  E-value: 6.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRnktSDRLETVILDVTKTESIVAATQwvkervgnrGLWGLVN 111
Cdd:cd05243    2 VLVVGATGKVGRHVVRELLDRGYQVRALVRDPSQAEKLE---AAGAEVVVGDLTDAESLAAALE---------GIDAVIS 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 112 NAGISTPSGPNEWmkkqdfarvlDVNLLGMIEvtlsmlpLVRKARG----RVVNVSSVMGRMSFFG----GGYCISKYGV 183
Cdd:cd05243   70 AAGSGGKGGPRTE----------AVDYDGNIN-------LIDAAKKagvkRFVLVSSIGADKPSHPlealGPYLDAKRKA 132

                        170       180
                 ....*....|....*....|....*..
gi 165377241 184 EAFsdsLRRE-LSYfgvkvAIIEPGGF 209
Cdd:cd05243  133 EDY---LRASgLDY-----TIVRPGGL 151
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 32-209 8.99e-03

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


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 36.75  E-value: 8.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241  32 VFITGCdSGF-GNLLARQLDRRGMRVLAACLTEKGAEELRNktsDRLETVILDVTKTESIVAATQwvkervgnrGLWGLV 110
Cdd:COG0702    2 ILVTGA-TGFiGRRVVRALLARGHPVRALVRDPEKAAALAA---AGVEVVQGDLDDPESLAAALA---------GVDAVF 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377241 111 NNAGISTpsgpnewmkKQDFARVLDvnllgmievtlSMLPLVRKAR----GRVVNVSSvMGRMSFFGGGYCISKYGVE-A 185
Cdd:COG0702   69 LLVPSGP---------GGDFAVDVE-----------GARNLADAAKaagvKRIVYLSA-LGADRDSPSPYLRAKAAVEeA 127

                        170       180
                 ....*....|....*....|....
gi 165377241 186 FSDSlrrelsyfGVKVAIIEPGGF 209
Cdd:COG0702  128 LRAS--------GLPYTILRPGWF 143
 
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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