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Conserved domains on  [gi|568967027|ref|XP_006513452|]
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retinol dehydrogenase 16 isoform X1 [Mus musculus]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10176849)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase similar to corticosteroid 11-beta-dehydrogenase isozyme 2 that catalyzes the conversion of cortisol to the inactive metabolite cortisone; 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

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 4.57e-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: 409.75  E-value: 4.57e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTE--KGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRGLW 107
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 108 GLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRVSLF-GGGYCISKYGVEAF 186
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 187 SDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLcSNTQM--LWDQTSSEIREIYGEKYLASYLKRLNKLDKRCNKDLSGV 264
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSEL-WEKQAkkLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPV 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 568967027 265 TDCMEHALTACHPRTRYSAGWDAKLFYLPLSYLPTFLVDALL 306
Cdd:cd09805  240 IDSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 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 4.57e-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: 409.75  E-value: 4.57e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTE--KGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRGLW 107
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 108 GLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRVSLF-GGGYCISKYGVEAF 186
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 187 SDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLcSNTQM--LWDQTSSEIREIYGEKYLASYLKRLNKLDKRCNKDLSGV 264
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSEL-WEKQAkkLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPV 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 568967027 265 TDCMEHALTACHPRTRYSAGWDAKLFYLPLSYLPTFLVDALL 306
Cdd:cd09805  240 IDSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
27-306 4.91e-51

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 169.28  E-value: 4.91e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRN---KTSDRLETVILDVTKTESIVTATQWVKEHVGn 103
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAelrAAGARVEVVALDVTDPDAVAALAEAVLARFG- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 rGLWGLVNNAGISTPsGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSL-FGGGYCISKY 181
Cdd:COG0300   82 -PIDVLVNNAGVGGG-GPFEELDLEDLRRVFEVNVFGPVRLTRALLPlMRARGRGRIVNVSSVAGLRGLpGMAAYAASKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 182 GVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLCSNTQMLwdqtSSEIreiygekylasylkrlnkldkrcnkdl 261
Cdd:COG0300  160 ALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPLL----SPEE--------------------------- 208

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568967027 262 sgVTDCMEHALTacHPRTRYSAGWDAKLFYLPLSYLPTfLVDALL 306
Cdd:COG0300  209 --VARAILRALE--RGRAEVYVGWDARLLARLLRLLPR-LFDRLL 248
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 30-218 8.18e-47

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 156.23  E-value: 8.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027   30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLT----EKGAEELRNkTSDRLETVILDVTKTESIVTATQWVKEHVGnrG 105
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSeeklEAVAKELGA-LGGKALFIQGDVTDRAQVKALVEQAVERLG--R 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  106 LWGLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSLFGGG-YCISKYGV 183
Cdd:pfam00106  78 LDILVNNAGI-TGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPYPGGSaYSASKAAV 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568967027  184 EAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSAR 218
Cdd:pfam00106 157 IGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
PRK05993 PRK05993
SDR family oxidoreductase;
30-310 8.51e-42

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 145.94  E-value: 8.51e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNktsDRLETVILDVTKTESIVTATQWVKEHVGNRgLWGL 109
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEA---EGLEAFQLDYAEPESIAALVAQVLELSGGR-LDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 110 VNNAGISTPSG----PNEWMKKQdfahvLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVMGRVSL-FGGGYCISKYGV 183
Cdd:PRK05993  81 FNNGAYGQPGAvedlPTEALRAQ-----FEANFFGWHDLTRRVIPVMRKqGQGRIVQCSSILGLVPMkYRGAYNASKFAI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 184 EAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLCSNTQMlwDQTSSEIREIYgekylASYLKRLNKlDKRCNKDLSG 263
Cdd:PRK05993 156 EGLSLTLRMELQGSGIHVSLIEPGPIETRFRANALAAFKRWI--DIENSVHRAAY-----QQQMARLEG-GGSKSRFKLG 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 568967027 264 VTDCME---HALTACHPRTRYSAGWDAKLFYLPLSYLPTFLVDALLYWTS 310
Cdd:PRK05993 228 PEAVYAvllHALTAPRPRPHYRVTTPAKQGALLKRLLPARWLYRLLRKAA 277
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 32-214 3.86e-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: 103.44  E-value: 3.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027   32 VFITGCDSGFGTLLARQLDRRGMRVLAACLT-EKGAEELRNKTSD---RLETVILDVTKTESIVTATQWVKEHVGnrGLW 107
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSsEEGAEEVVEELKAlgvKALGVVLDVSDREDVKAVVEEIEEELG--TID 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  108 GLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGrvsLFGGG----YCISKYG 182
Cdd:TIGR01830  79 ILVNNAGI-TRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRsGRIINISSVVG---LMGNAgqanYAASKAG 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 568967027  183 VEAFSDSLRRELSYFGVKVAIIEPGFFLTGVT 214
Cdd:TIGR01830 155 VIGFTKSLAKELASRNITVNAVAPGFIDTDMT 186
 
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 4.57e-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: 409.75  E-value: 4.57e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTE--KGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRGLW 107
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 108 GLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRVSLF-GGGYCISKYGVEAF 186
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 187 SDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLcSNTQM--LWDQTSSEIREIYGEKYLASYLKRLNKLDKRCNKDLSGV 264
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSEL-WEKQAkkLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPV 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 568967027 265 TDCMEHALTACHPRTRYSAGWDAKLFYLPLSYLPTFLVDALL 306
Cdd:cd09805  240 IDSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 30-288 1.82e-62

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


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 198.61  E-value: 1.82e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGnrGLWGL 109
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFG--RIDVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 110 VNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSL-FGGGYCISKYGVEAFS 187
Cdd:cd05374   79 VNNAGYGL-FGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGsGRIVNVSSVAGLVPTpFLGPYCASKAALEALS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 188 DSLRRELSYFGVKVAIIEPGFFLTGVtssarlcSNTQMLWDQTSSEIreiygEKYLASYLKRLNKLDKRCNKDLSG--VT 265
Cdd:cd05374  158 ESLRLELAPFGIKVTIIEPGPVRTGF-------ADNAAGSALEDPEI-----SPYAPERKEIKENAAGVGSNPGDPekVA 225

                        250       260
                 ....*....|....*....|...
gi 568967027 266 DCMEHALTACHPRTRYSAGWDAK 288
Cdd:cd05374  226 DVIVKALTSESPPLRYFLGSDAL 248
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
27-306 4.91e-51

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 169.28  E-value: 4.91e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRN---KTSDRLETVILDVTKTESIVTATQWVKEHVGn 103
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAelrAAGARVEVVALDVTDPDAVAALAEAVLARFG- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 rGLWGLVNNAGISTPsGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSL-FGGGYCISKY 181
Cdd:COG0300   82 -PIDVLVNNAGVGGG-GPFEELDLEDLRRVFEVNVFGPVRLTRALLPlMRARGRGRIVNVSSVAGLRGLpGMAAYAASKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 182 GVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLCSNTQMLwdqtSSEIreiygekylasylkrlnkldkrcnkdl 261
Cdd:COG0300  160 ALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPLL----SPEE--------------------------- 208

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568967027 262 sgVTDCMEHALTacHPRTRYSAGWDAKLFYLPLSYLPTfLVDALL 306
Cdd:COG0300  209 --VARAILRALE--RGRAEVYVGWDARLLARLLRLLPR-LFDRLL 248
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 28-218 9.30e-49

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: 163.04  E-value: 9.30e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  28 QDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGnrGLW 107
Cdd:COG4221    4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFG--RLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 108 GLVNNAGISTPsGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSL-FGGGYCISKYGVEA 185
Cdd:COG4221   82 VLVNNAGVALL-GPLEELDPEDWDRMIDVNVKGVLYVTRAALPaMRARGSGHIVNISSIAGLRPYpGGAVYAATKAAVRG 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568967027 186 FSDSLRRELSYFGVKVAIIEPGFFLTGVTSSAR 218
Cdd:COG4221  161 LSESLRAELRPTGIRVTVIEPGAVDTEFLDSVF 193
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 30-218 8.18e-47

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 156.23  E-value: 8.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027   30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLT----EKGAEELRNkTSDRLETVILDVTKTESIVTATQWVKEHVGnrG 105
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSeeklEAVAKELGA-LGGKALFIQGDVTDRAQVKALVEQAVERLG--R 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  106 LWGLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSLFGGG-YCISKYGV 183
Cdd:pfam00106  78 LDILVNNAGI-TGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPYPGGSaYSASKAAV 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568967027  184 EAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSAR 218
Cdd:pfam00106 157 IGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
PRK05993 PRK05993
SDR family oxidoreductase;
30-310 8.51e-42

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 145.94  E-value: 8.51e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNktsDRLETVILDVTKTESIVTATQWVKEHVGNRgLWGL 109
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEA---EGLEAFQLDYAEPESIAALVAQVLELSGGR-LDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 110 VNNAGISTPSG----PNEWMKKQdfahvLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVMGRVSL-FGGGYCISKYGV 183
Cdd:PRK05993  81 FNNGAYGQPGAvedlPTEALRAQ-----FEANFFGWHDLTRRVIPVMRKqGQGRIVQCSSILGLVPMkYRGAYNASKFAI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 184 EAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLCSNTQMlwDQTSSEIREIYgekylASYLKRLNKlDKRCNKDLSG 263
Cdd:PRK05993 156 EGLSLTLRMELQGSGIHVSLIEPGPIETRFRANALAAFKRWI--DIENSVHRAAY-----QQQMARLEG-GGSKSRFKLG 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 568967027 264 VTDCME---HALTACHPRTRYSAGWDAKLFYLPLSYLPTFLVDALLYWTS 310
Cdd:PRK05993 228 PEAVYAvllHALTAPRPRPHYRVTTPAKQGALLKRLLPARWLYRLLRKAA 277
PRK08017 PRK08017
SDR family oxidoreductase;
30-308 2.02e-40

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 141.76  E-value: 2.02e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAAClteKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRgLWGL 109
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAAC---RKPDDVARMNSLGFTGILLDLDDPESVERAADEVIALTDNR-LYGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 110 VNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVR-KARGRVVNVSSVMGRVSLFG-GGYCISKYGVEAFS 187
Cdd:PRK08017  79 FNNAGFGV-YGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLpHGEGRIVMTSSVMGLISTPGrGAYAASKYALEAWS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 188 DSLRRELSYFGVKVAIIEPGFFLTGVTSSArlcsntqmlwDQTSSEireiygekylasylKRLNK--LDKRCNKDLSGVT 265
Cdd:PRK08017 158 DALRMELRHSGIKVSLIEPGPIRTRFTDNV----------NQTQSD--------------KPVENpgIAARFTLGPEAVV 213

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 568967027 266 DCMEHALTACHPRTRYSAGWDAKLFYLPLSYLPTFLVDALLYW 308
Cdd:PRK08017 214 PKLRHALESPKPKLRYPVTLVTHAVMVLKRLLPGRMMDKILRG 256
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 25-218 3.99e-38

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: 135.68  E-value: 3.99e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  25 SHLQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELR---NKTSDRLETVILDVTKTESIVTATQWVKEHV 101
Cdd:COG1028    2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAaelRAAGGRALAVAADVTDEAAVEALVAAAVAAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 102 GnrGLWGLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLFG-GGYCIS 179
Cdd:COG1028   82 G--RLDILVNNAGI-TPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGgGRIVNISSIAGLRGSPGqAAYAAS 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568967027 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSAR 218
Cdd:COG1028  159 KAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALL 197
PRK06914 PRK06914
SDR family oxidoreductase;
30-298 5.84e-38

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 135.92  E-value: 5.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKT-----SDRLETVILDVTKTESIVTATQWVKEHvGNR 104
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQAtqlnlQQNIKVQQLDVTDQNSIHNFQLVLKEI-GRI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 105 GLwgLVNNAGisTPSG------PNEWMKKQdfahvLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLFG-GGY 176
Cdd:PRK06914  83 DL--LVNNAG--YANGgfveeiPVEEYRKQ-----FETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGlSPY 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGV-TSSARLCSNTQmlwDQTSSeireiYgEKYLASYLKRLNKldk 255
Cdd:PRK06914 154 VSSKYALEGFSESLRLELKPFGIDVALIEPGSYNTNIwEVGKQLAENQS---ETTSP-----Y-KEYMKKIQKHINS--- 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 568967027 256 rcNKDLSG----VTDCMEHALTACHPRTRYSAGWDAKLFYLPLSYLP 298
Cdd:PRK06914 222 --GSDTFGnpidVANLIVEIAESKRPKLRYPIGKGVKLMILAKKILP 266
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 32-211 1.30e-37

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: 133.95  E-value: 1.30e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSD--RLETVILDVTKTESIVTATQWVKEHVGnrGLWGL 109
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEALggNAVAVQADVSDEEDVEALVEEALEEFG--RLDIL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 110 VNNAGISTPsGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLFG-GGYCISKYGVEAFS 187
Cdd:cd05233   79 VNNAGIARP-GPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGgGRIVNISSVAGLRPLPGqAAYAASKAALEGLT 157

                        170       180
                 ....*....|....*....|....
gi 568967027 188 DSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:cd05233  158 RSLALELAPYGIRVNAVAPGLVDT 181
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 33-211 4.78e-37

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 133.50  E-value: 4.78e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  33 FITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGnrGLWGLVNN 112
Cdd:PRK06180   8 LITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFG--PIDVLVNN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 113 AGI----STPSGPNEWMKKQdfahvLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLFG-GGYCISKYGVEAF 186
Cdd:PRK06180  86 AGYghegAIEESPLAEMRRQ-----FEVNVFGAVAMTKAVLPGMRARRrGHIVNITSMGGLITMPGiGYYCGSKFALEGI 160

                        170       180
                 ....*....|....*....|....*
gi 568967027 187 SDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK06180 161 SESLAKEVAPFGIHVTAVEPGSFRT 185
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 27-217 3.74e-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: 130.78  E-value: 3.74e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLaacLT-------EKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKE 99
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLV---LSarreerlEEVKSECLELGAPSPHVVPLDMSDLEDAEQVVEEALK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 100 HVGnrGLWGLVNNAGISTPSgpnEWMKK--QDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSL-FGGG 175
Cdd:cd05332   78 LFG--GLDILINNAGISMRS---LFHDTsiDVDRKIMEVNYFGPVALTKAALPhLIERSQGSIVVVSSIAGKIGVpFRTA 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568967027 176 YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSA 217
Cdd:cd05332  153 YAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNA 194
PRK06182 PRK06182
short chain dehydrogenase; Validated
 28-306 7.16e-36

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 130.47  E-value: 7.16e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  28 QDKYVFITGCDSGFGTLLARQLDRRGMRVLAAClteKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRGLw 107
Cdd:PRK06182   2 QKKVALVTGASSGIGKATARRLAAQGYTVYGAA---RRVDKMEDLASLGVHPLSLDVTDEASIKAAVDTIIAEEGRIDV- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 108 gLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRV-SLFGGGYCISKYGVEA 185
Cdd:PRK06182  78 -LVNNAGYGS-YGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIyTPLGAWYHATKFALEG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 186 FSDSLRRELSYFGVKVAIIEPGFFLTGvtssarlcsntqmlWDQTSSE-IREI-----YGEKYLASYLKRLNKLDKRCNK 259
Cdd:PRK06182 156 FSDALRLEVAPFGIDVVVIEPGGIKTE--------------WGDIAADhLLKTsgngaYAEQAQAVAASMRSTYGSGRLS 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 568967027 260 DLSGVTDCMEHALTACHPRTRYSAGWDAKLFYLPLSYLPTFLVDALL 306
Cdd:PRK06182 222 DPSVIADAISKAVTARRPKTRYAVGFGAKPLIFLRRILPDRAFDRLI 268
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 27-216 4.48e-35

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 127.62  E-value: 4.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLT-EKGAEELRNKTSD---RLETVILDVTKTESIVTATQWVKEHVG 102
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASsEAGAEALVAEIGAlggKALAVQGDVSDAESVERAVDEAKAEFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 nrGLWGLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLFGGG-YCISK 180
Cdd:PRK05557  83 --GVDILVNNAGI-TRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRsGRIINISSVVGLMGNPGQAnYAASK 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568967027 181 YGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSS 216
Cdd:PRK05557 160 AGVIGFTKSLARELASRGITVNAVAPGFIETDMTDA 195
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 28-306 2.37e-33

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 123.47  E-value: 2.37e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  28 QDKYVFITGCDSGFGTLLARQLDRRGMRVLAAclTEKGAeelRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRGLw 107
Cdd:PRK06179   3 NSKVALVTGASSGIGRATAEKLARAGYRVFGT--SRNPA---RAAPIPGVELLELDVTDDASVQAAVDEVIARAGRIDV- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 108 gLVNNAGISTPSGPNEWMKKQDfAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSL-FGGGYCISKYGVEA 185
Cdd:PRK06179  77 -LVNNAGVGLAGAAEESSIAQA-QALFDTNVFGILRMTRAVLPHMRAQGsGRIINISSVLGFLPApYMALYAASKHAVEG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 186 FSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARlcsntqmlwdQTSSEireiygekyLASYLKRLNKLDKRCNK------ 259
Cdd:PRK06179 155 YSESLDHEVRQFGIRVSLVEPAYTKTNFDANAP----------EPDSP---------LAEYDRERAVVSKAVAKavkkad 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 568967027 260 DLSGVTDCMEHALTACHPRTRYSAGWDAKLFYLPLSYLPTFLVDALL 306
Cdd:PRK06179 216 APEVVADTVVKAALGPWPKMRYTAGGQASLLSKLRRFMPAGAVDKSL 262
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 32-217 7.39e-33

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: 121.25  E-value: 7.39e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRG-MRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRGLWGLV 110
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSAATELAALGASHSRLHILELDVTDEIAESAEAVAERLGDAGLDVLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 111 NNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKA-RGRVVNVSSVMGRVSLFGGG----YCISKYGVEA 185
Cdd:cd05325   81 NNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGaRAKIINISSRVGSIGDNTSGgwysYRASKAALNM 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568967027 186 FSDSLRRELSYFGVKVAIIEPGFFLTGVTSSA 217
Cdd:cd05325  161 LTKSLAVELKRDGITVVSLHPGWVRTDMGGPF 192
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
30-218 1.86e-31

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 117.94  E-value: 1.86e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGA----EELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRG 105
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCakdwFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGPVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 106 LwgLVNNAGISTPSGPNEwMKKQDFAHVLDVNLLGMIEVTLSMLPLVR-KARGRVVNVSSVMGRVSLFGG-GYCISKYGV 183
Cdd:PRK12824  83 I--LVNNAGITRDSVFKR-MSHQEWNDVINTNLNSVFNVTQPLFAAMCeQGYGRIINISSVNGLKGQFGQtNYSAAKAGM 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568967027 184 EAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSAR 218
Cdd:PRK12824 160 IGFTKALASEGARYGITVNCIAPGYIATPMVEQMG 194
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
27-214 6.22e-31

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 116.41  E-value: 6.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTS---DRLETVILDVTKTESIVTATQWVKEHVGn 103
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRaagGEARVLVFDVSDEAAVRALIEAAVEAFG- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 rGLWGLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLFGGG-YCISKY 181
Cdd:PRK05653  82 -ALDILVNNAGI-TRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARyGRIVNISSVSGVTGNPGQTnYSAAKA 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568967027 182 GVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVT 214
Cdd:PRK05653 160 GVIGFTKALALELASRGITVNAVAPGFIDTDMT 192
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 33-212 9.91e-31

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 116.68  E-value: 9.91e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  33 FITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNrgLWGLVNN 112
Cdd:PRK08263   7 FITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGR--LDIVVNN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 113 AGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLFGGG-YCISKYGVEAFSDSL 190
Cdd:PRK08263  85 AGYGL-FGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRsGHIIQISSIGGISAFPMSGiYHASKWALEGMSEAL 163

                        170       180
                 ....*....|....*....|..
gi 568967027 191 RRELSYFGVKVAIIEPGFFLTG 212
Cdd:PRK08263 164 AQEVAEFGIKVTLVEPGGYSTD 185
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 27-211 1.48e-30

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: 115.71  E-value: 1.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNK---TSDRLETVILDVTKTESIVTATQWVKEHVGn 103
Cdd:cd08934    1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADEleaEGGKALVLELDVTDEQQVDAAVERTVEALG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 rGLWGLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVR-KARGRVVNVSSVMGRVSLFG-GGYCISKY 181
Cdd:cd08934   80 -RLDILVNNAGIML-LGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLlRNKGTIVNISSVAGRVAVRNsAVYNATKF 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 568967027 182 GVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:cd08934  158 GVNAFSEGLRQEVTERGVRVVVIEPGTVDT 187
PRK09291 PRK09291
SDR family oxidoreductase;
30-212 2.48e-30

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 115.10  E-value: 2.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDR---LETVILDVTKTESIVTATQW---Vkehvgn 103
Cdd:PRK09291   3 KTILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRglaLRVEKLDLTDAIDRAQAAEWdvdV------ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 rglwgLVNNAGISTpSG-----PNEWMKKQdfahvLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSL-FGGGY 176
Cdd:PRK09291  77 -----LLNNAGIGE-AGavvdiPVELVREL-----FETNVFGPLELTQGFVRkMVARGKGKVVFTSSMAGLITGpFTGAY 145

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568967027 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTG 212
Cdd:PRK09291 146 CASKHALEAIAEAMHAELKPFGIQVATVNPGPYLTG 181
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 30-217 5.24e-30

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


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 113.49  E-value: 5.24e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRG--MRVLAACLTEKG---AEELRNKTSDrLETVILDVTKTESIVTATQWVKEHVGnr 104
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGpgTVILTARDVERGqaaVEKLRAEGLS-VRFHQLDVTDDASIEAAADFVEEKYG-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 105 GLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLfggGYCISKYGV 183
Cdd:cd05324   78 GLDILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPaGRIVNVSSGLGSLTS---AYGVSKAAL 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568967027 184 EAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSA 217
Cdd:cd05324  155 NALTRILAKELKETGIKVNACCPGWVKTDMGGGK 188
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 30-214 7.82e-30

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: 113.41  E-value: 7.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGA---EELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGnrGL 106
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAaetVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFG--PV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 107 WGLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLFG-GGYCISKYGVE 184
Cdd:cd05333   79 DILVNNAGI-TRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRsGRIINISSVVGLIGNPGqANYAASKAGVI 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 568967027 185 AFSDSLRRELSYFGVKVAIIEPGFFLTGVT 214
Cdd:cd05333  158 GFTKSLAKELASRGITVNAVAPGFIDTDMT 187
PRK05693 PRK05693
SDR family oxidoreductase;
32-217 9.94e-30

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 114.12  E-value: 9.94e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRGMRVLAaclTEKGAEELRNKTSDRLETVILDVTKTESIVT-ATQWVKEHvgnRGLWGLV 110
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWA---TARKAEDVEALAAAGFTAVQLDVNDGAALARlAEELEAEH---GGLDVLI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 111 NNAGIST--P--SGPNEWMKKQdfahvLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMG-RVSLFGGGYCISKYGVEA 185
Cdd:PRK05693  78 NNAGYGAmgPllDGGVEAMRRQ-----FETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGvLVTPFAGAYCASKAAVHA 152

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568967027 186 FSDSLRRELSYFGVKVAIIEPGFFLTGVTSSA 217
Cdd:PRK05693 153 LSDALRLELAPFGVQVMEVQPGAIASQFASNA 184
PRK05650 PRK05650
SDR family oxidoreductase;
32-218 3.44e-28

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 109.74  E-value: 3.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVTATQWVKEHVGnrGLWG 108
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREaggDGFYQRCDVRDYSQLTALAQACEEKWG--GIDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 109 LVNNAGISTPSGPNEwMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSL-FGGGYCISKYGVEAF 186
Cdd:PRK05650  81 IVNNAGVASGGFFEE-LSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKsGRIVNIASMAGLMQGpAMSSYNVAKAGVVAL 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568967027 187 SDSLRRELSYFGVKVAIIEPGFFLTGVTSSAR 218
Cdd:PRK05650 160 SETLLVELADDEIGVHVVCPSFFQTNLLDSFR 191
PRK12826 PRK12826
SDR family oxidoreductase;
27-211 4.01e-28

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 109.24  E-value: 4.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVTATQWVKEHVGn 103
Cdd:PRK12826   4 LEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAaggKARARQVDVRDRAALKAAVAAGVEDFG- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 rGLWGLVNNAGIStPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSLFGG--GYCISK 180
Cdd:PRK12826  83 -RLDILVANAGIF-PLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPaLIRAGGGRIVLTSSVAGPRVGYPGlaHYAASK 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568967027 181 YGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK12826 161 AGLVGFTRALALELAARNITVNSVHPGGVDT 191
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 29-211 8.23e-28

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


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 108.11  E-value: 8.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  29 DKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTE----KGAEELR---NKTSDRLETVILDVTKTESIVTATQWVKEhv 101
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSEskleEAVEEIEaeaNASGQKVSYISADLSDYEEVEQAFAQAVE-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 102 gnrglWG-----LVNNAGISTPsGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLFG-G 174
Cdd:cd08939   79 -----KGgppdlVVNCAGISIP-GLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRpGHIVFVSSQAALVGIYGyS 152

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568967027 175 GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:cd08939  153 AYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDT 189
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 27-203 1.33e-27

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 108.90  E-value: 1.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNK--TSDRLETVILDVTKTESIVTATQWVKEHVGnr 104
Cdd:PRK05872   7 LAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAElgGDDRVLTVVADVTDLAAMQAAAEEAVERFG-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 105 GLWGLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVmgrvSLFGGG-----YCIS 179
Cdd:PRK05872  85 GIDVVVANAGI-ASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSL----AAFAAApgmaaYCAS 159

                        170       180
                 ....*....|....*....|....
gi 568967027 180 KYGVEAFSDSLRRELSYFGVKVAI 203
Cdd:PRK05872 160 KAGVEAFANALRLEVAHHGVTVGS 183
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 30-207 2.49e-27

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: 106.98  E-value: 2.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLaacLT-------EKGAEELRNKTSDRLETVILDVTKTESIvtatqwvKEHVG 102
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLI---LTgrraerlQELADELGAKFPVKVLPLQLDVSDRESI-------EAALE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 N-----RGLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSLFGGG- 175
Cdd:cd05346   71 NlpeefRDIDILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPiMIARNQGHIINLGSIAGRYPYAGGNv 150

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568967027 176 YCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:cd05346  151 YCATKAAVRQFSLNLRKDLIGTGIRVTNIEPG 182
PRK06482 PRK06482
SDR family oxidoreductase;
33-218 3.66e-27

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 107.12  E-value: 3.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  33 FITGCDSGFGTLLARQLDRRGMRVlAACLTEKGA-EELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRGLwgLVN 111
Cdd:PRK06482   6 FITGASSGFGRGMTERLLARGDRV-AATVRRPDAlDDLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAALGRIDV--VVS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 112 NAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLFGGG-YCISKYGVEAFSDS 189
Cdd:PRK06482  83 NAGYGL-FGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGgGRIVQVSSEGGQIAYPGFSlYHATKWGIEGFVEA 161

                        170       180
                 ....*....|....*....|....*....
gi 568967027 190 LRRELSYFGVKVAIIEPGFFLTGVTSSAR 218
Cdd:PRK06482 162 VAQEVAPFGIEFTIVEPGPARTNFGAGLD 190
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 27-217 1.48e-26

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: 104.80  E-value: 1.48e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGM-RVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEhvgnrg 105
Cdd:cd05354    1 IKDKTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAAQAKD------ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 106 LWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKA-RGRVVNVSSVMGRVSLFG-GGYCISKYGV 183
Cdd:cd05354   75 VDVVINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANgGGAIVNLNSVASLKNFPAmGTYSASKSAA 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568967027 184 EAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSA 217
Cdd:cd05354  155 YSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGA 188
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 32-214 3.86e-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: 103.44  E-value: 3.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027   32 VFITGCDSGFGTLLARQLDRRGMRVLAACLT-EKGAEELRNKTSD---RLETVILDVTKTESIVTATQWVKEHVGnrGLW 107
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSsEEGAEEVVEELKAlgvKALGVVLDVSDREDVKAVVEEIEEELG--TID 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  108 GLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGrvsLFGGG----YCISKYG 182
Cdd:TIGR01830  79 ILVNNAGI-TRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRsGRIINISSVVG---LMGNAgqanYAASKAG 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 568967027  183 VEAFSDSLRRELSYFGVKVAIIEPGFFLTGVT 214
Cdd:TIGR01830 155 VIGFTKSLAKELASRNITVNAVAPGFIDTDMT 186
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 30-208 5.48e-26

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: 102.83  E-value: 5.48e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRnKTSDRLETVILDVTKTESIVTATQWVKEHVGnrGLWGL 109
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALS-ASGGDVEAVPYDARDPEDARALVDALRDRFG--RIDVL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 110 VNNAGISTPSGPNEWMKKQDFAHvLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMG-RVSLFGGGYCISKYGVEAFS 187
Cdd:cd08932   78 VHNAGIGRPTTLREGSDAELEAH-FSINVIAPAELTRALLPaLREAGSGRVVFLNSLSGkRVLAGNAGYSASKFALRALA 156

                        170       180
                 ....*....|....*....|.
gi 568967027 188 DSLRRELSYFGVKVAIIEPGF 208
Cdd:cd08932  157 HALRQEGWDHGVRVSAVCPGF 177
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 32-214 6.40e-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: 100.39  E-value: 6.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRN---KTSDRLETVILDVTKTESIVTATQWVKEHVGNRGLwg 108
Cdd:cd05339    2 VLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANnvrKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTI-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 109 LVNNAGISTPSGPNEwMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSLFGGG-YCISKYGVEAF 186
Cdd:cd05339   80 LINNAGVVSGKKLLE-LPDEEIEKTFEVNTLAHFWTTKAFLPdMLERNHGHIVTIASVAGLISPAGLAdYCASKAAAVGF 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568967027 187 SDSLRRELSYF---GVKVAIIEPGFFLTGVT 214
Cdd:cd05339  159 HESLRLELKAYgkpGIKTTLVCPYFINTGMF 189
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 32-211 1.70e-24

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


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 98.99  E-value: 1.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRGMRVLAACLTEKG----AEELRNKTSDRLeTVILDVTKTESIVTATQWVKEHVGNRGLW 107
Cdd:cd05360    3 VVITGASSGIGRATALAFAERGAKVVLAARSAEAlhelAREVRELGGEAI-AVVADVADAAQVERAADTAVERFGRIDTW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 108 glVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMG-RVSLFGGGYCISKYGVEA 185
Cdd:cd05360   82 --VNNAGVAV-FGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPhLRRRGGGALINVGSLLGyRSAPLQAAYSASKHAVRG 158

                        170       180
                 ....*....|....*....|....*...
gi 568967027 186 FSDSLRRELSYFGVKVAI--IEPGFFLT 211
Cdd:cd05360  159 FTESLRAELAHDGAPISVtlVQPTAMNT 186
PRK09072 PRK09072
SDR family oxidoreductase;
26-206 1.83e-24

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 99.63  E-value: 1.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  26 HLQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTS--DRLETVILDVTKTESIVTATQWVKEHvgn 103
Cdd:PRK09072   2 DLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPypGRHRWVVADLTSEAGREAVLARAREM--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 RGLWGLVNNAGISTPSgpneWMKKQDFAHV---LDVNLLGMIEVTLSMLPLVRKA-RGRVVNVSSVMGRVSLFG-GGYCI 178
Cdd:PRK09072  79 GGINVLINNAGVNHFA----LLEDQDPEAIerlLALNLTAPMQLTRALLPLLRAQpSAMVVNVGSTFGSIGYPGyASYCA 154

                        170       180
                 ....*....|....*....|....*...
gi 568967027 179 SKYGVEAFSDSLRRELSYFGVKVAIIEP 206
Cdd:PRK09072 155 SKFALRGFSEALRRELADTGVRVLYLAP 182
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 30-207 3.87e-24

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


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 98.69  E-value: 3.87e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDR---RGMRVLAAC--LTEKG--AEELRNKTSDRLETVILDVTKTESIVTATQWVKEhvg 102
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLASdpsKRFKVYATMrdLKKKGrlWEAAGALAGGTLETLQLDVCDSKSVAAAVERVTE--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 nRGLWGLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSL-FGGGYCISK 180
Cdd:cd09806   78 -RHVDVLVCNAGVGL-LGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGsGRILVTSSVGGLQGLpFNDVYCASK 155

                        170       180
                 ....*....|....*....|....*..
gi 568967027 181 YGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:cd09806  156 FALEGLCESLAVQLLPFNVHLSLIECG 182
PRK06181 PRK06181
SDR family oxidoreductase;
29-211 4.17e-24

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 98.90  E-value: 4.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  29 DKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKG----AEELRNKTSDRLeTVILDVTKTESIVTATQWVKEHVGnr 104
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRlaslAQELADHGGEAL-VVPTDVSDAEACERLIEAAVARFG-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 105 GLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRVSLFG-GGYCISKYGV 183
Cdd:PRK06181  78 GIDILVNNAGITMWSRFDELTDLSVFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTrSGYAASKHAL 157

                        170       180
                 ....*....|....*....|....*...
gi 568967027 184 EAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK06181 158 HGFFDSLRIELADDGVAVTVVCPGFVAT 185
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 20-207 6.37e-24

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 98.21  E-value: 6.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  20 VRQVVSHLQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLET-VILDVTKTESIVTATQWVK 98
Cdd:PRK12829   2 AIDLLKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPGAKVTaTVADVADPAQVERVFDTAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  99 EHVGnrGLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKA-RGRVV-NVSSVMGRVSL-FGGG 175
Cdd:PRK12829  82 ERFG--GLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASgHGGVIiALSSVAGRLGYpGRTP 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568967027 176 YCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK12829 160 YAASKWAVVGLVKSLAIELGPLGIRVNAILPG 191
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 27-215 8.10e-24

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 98.09  E-value: 8.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEElrnkTSDRLETVI---LDVTKTESIVTATQWVkehvgn 103
Cdd:PRK07825   3 LRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKE----TAAELGLVVggpLDVTDPASFAAFLDAV------ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 RGLWG----LVNNAGIsTPSGPnewMKKQDFAHV---LDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSLFGGG 175
Cdd:PRK07825  73 EADLGpidvLVNNAGV-MPVGP---FLDEPDAVTrriLDVNVYGVILGSKLAAPrMVPRGRGHVVNVASLAGKIPVPGMA 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568967027 176 -YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTS 215
Cdd:PRK07825 149 tYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELIA 189
PRK08264 PRK08264
SDR family oxidoreductase;
26-217 1.01e-23

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 96.88  E-value: 1.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  26 HLQDKYVFITGCDSGFGTLLARQLDRRG-MRVLAACltekgaeelRNKTS-----DRLETVILDVTKTESIVTATqwvkE 99
Cdd:PRK08264   3 DIKGKVVLVTGANRGIGRAFVEQLLARGaAKVYAAA---------RDPESvtdlgPRVVPLQLDVTDPASVAAAA----E 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 100 HVGNRGLwgLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSL-FGGGYC 177
Cdd:PRK08264  70 AASDVTI--LVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPvLAANGGGAIVNVLSVLSWVNFpNLGTYS 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568967027 178 ISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSA 217
Cdd:PRK08264 148 ASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAAGL 187
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-208 1.03e-23

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 97.25  E-value: 1.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACL-TEKGAEELRNK---TSDRLETVILDVTKTESIVTATQWVKEHVG 102
Cdd:PRK12825   4 LMGRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEAveaLGRRAQAVQADVTDKAALEAAVAAAVERFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 nrGLWGLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLFG-GGYCISK 180
Cdd:PRK12825  84 --RIDILVNNAGI-FEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRgGRIVNISSVAGLPGWPGrSNYAAAK 160

                        170       180
                 ....*....|....*....|....*...
gi 568967027 181 YGVEAFSDSLRRELSYFGVKVAIIEPGF 208
Cdd:PRK12825 161 AGLVGLTKALARELAEYGITVNMVAPGD 188
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 38-216 1.15e-23

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: 96.73  E-value: 1.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027   38 DSGFGTLLARQLDRRGMRVLAACLTEKGAEELRnKTSDRLETVIL--DVTKTESIVTATQWVKEHVGnrGLWGLVNNAGI 115
Cdd:pfam13561   5 ESGIGWAIARALAEEGAEVVLTDLNEALAKRVE-ELAEELGAAVLpcDVTDEEQVEALVAAAVEKFG--RLDILVNNAGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  116 STP-SGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLvRKARGRVVNVSSVMGRVSLFGGG-YCISKYGVEAFSDSLRRE 193
Cdd:pfam13561  82 APKlKGPFLDTSREDFDRALDVNLYSLFLLAKAALPL-MKEGGSIVNLSSIGAERVVPNYNaYGAAKAALEALTRYLAVE 160

                         170       180
                  ....*....|....*....|...
gi 568967027  194 LSYFGVKVAIIEPGFFLTGVTSS 216
Cdd:pfam13561 161 LGPRGIRVNAISPGPIKTLAASG 183
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 30-216 2.24e-23

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


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 96.04  E-value: 2.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGnrGLWGL 109
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFG--GLDAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 110 VNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTL-SMLPLVRKARGRVVNVSSVMGRVSLFGG-GYCISKYGVEAFS 187
Cdd:cd08929   79 VNNAGVGV-MKPVEELTPEEWRLVLDTNLTGAFYCIHkAAPALLRRGGGTIVNVGSLAGKNAFKGGaAYNASKFGLLGLS 157

                        170       180
                 ....*....|....*....|....*....
gi 568967027 188 DSLRRELSYFGVKVAIIEPGFFLTGVTSS 216
Cdd:cd08929  158 EAAMLDLREANIRVVNVMPGSVDTGFAGS 186
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 27-233 2.40e-23

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: 96.33  E-value: 2.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVlaaCLTEKGAEEL---------RNKTSDRLETVILDVTKTESIVTATQWV 97
Cdd:cd05364    1 LSGKVAIITGSSSGIGAGTAILFARLGARL---ALTGRDAERLeetrqsclqAGVSEKKILLVVADLTEEEGQDRIISTT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  98 KEHVGNRGLwgLVNNAGISTPsGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRVSLFGG-GY 176
Cdd:cd05364   78 LAKFGRLDI--LVNNAGILAK-GGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGRSFPGVlYY 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568967027 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLCSNTQMLWDQTSSE 233
Cdd:cd05364  155 CISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRMGMPEEQYIKFLSRAKE 211
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 30-211 4.13e-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: 4.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEK--GAEEL-RNKTSDRLETVILDVTKTESIVTATQWVKEHVGnrGL 106
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENpgAAAELqAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFG--RV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 107 WGLVNNAGISTPSGPNEWMK-KQDFAHVLDVNLLGMIEVTLSMLPLVRKAR----GRVVNVSSVMG-----RVSLfgggY 176
Cdd:cd05323   79 DILINNAGILDEKSYLFAGKlPPPWEKTIDVNLTGVINTTYLALHYMDKNKggkgGVIVNIGSVAGlypapQFPV----Y 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568967027 177 CISKYGVEAFSDSLRRELSY-FGVKVAIIEPGFFLT 211
Cdd:cd05323  155 SASKHGVVGFTRSLADLLEYkTGVRVNAICPGFTNT 190
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 27-218 1.99e-22

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: 93.53  E-value: 1.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDrLETVILDVTKTESIVTATQWV-KEHvgnRG 105
Cdd:cd05370    3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN-IHTIVLDVGDAESVEALAEALlSEY---PN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 106 LWGLVNNAGIstpsgpnewMKKQDFAHV----------LDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSLFGG 174
Cdd:cd05370   79 LDILINNAGI---------QRPIDLRDPasdldkadteIDTNLIGPIRLIKAFLPhLKKQPEATIVNVSSGLAFVPMAAN 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568967027 175 G-YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSAR 218
Cdd:cd05370  150 PvYCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERR 194
PRK07326 PRK07326
SDR family oxidoreductase;
27-207 4.03e-22

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 92.77  E-value: 4.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVIL--DVTKTESIVTATQWVKEHVGnr 104
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGNVLGLaaDVRDEADVQRAVDAIVAAFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 105 GLWGLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRvSLFGGG--YCISKYG 182
Cdd:PRK07326  82 GLDVLIANAGVGH-FAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGT-NFFAGGaaYNASKFG 159

                        170       180
                 ....*....|....*....|....*
gi 568967027 183 VEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK07326 160 LVGFSEAAMLDLRQYGIKVSTIMPG 184
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 27-206 4.09e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 94.60  E-value: 4.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKG----AEELRNKTSDRLeTVILDVTKTESIVTATQWVKEHVG 102
Cdd:PRK07109   6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGlealAAEIRAAGGEAL-AVVADVADAEAVQAAADRAEEELG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 NRGLWglVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSL-FGGGYCISK 180
Cdd:PRK07109  85 PIDTW--VNNAMVTV-FGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRhMRPRDRGAIIQVGSALAYRSIpLQSAYCAAK 161

                        170       180
                 ....*....|....*....|....*...
gi 568967027 181 YGVEAFSDSLRRELSYFG--VKVAIIEP 206
Cdd:PRK07109 162 HAIRGFTDSLRCELLHDGspVSVTMVQP 189
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 27-214 9.82e-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: 92.04  E-value: 9.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVTATQWVKEHVGN 103
Cdd:cd05347    3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKegvEATAFTCDVSDEEAIKAAVEAIEEDFGK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 RGLwgLVNNAGISTPSgPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMgrvSLFGG----GYCI 178
Cdd:cd05347   83 IDI--LVNNAGIIRRH-PAEEFPEAEWRDVIDVNLNGVFFVSQAVARhMIKQGHGKIINICSLL---SELGGppvpAYAA 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568967027 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVT 214
Cdd:cd05347  157 SKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMT 192
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 27-205 1.46e-21

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: 91.38  E-value: 1.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAAcltekG--AEELRNKTSDR--LETVILDVTKTESIVTATQWVKEHVG 102
Cdd:COG3967    3 LTGNTILITGGTSGIGLALAKRLHARGNTVIIT-----GrrEEKLEEAAAANpgLHTIVLDVADPASIAALAEQVTAEFP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 nrGLWGLVNNAGISTP----SGPNEWmkkQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSLFG-GGY 176
Cdd:COG3967   78 --DLNVLINNAGIMRAedllDEAEDL---ADAEREITTNLLGPIRLTAAFLPhLKAQPEAAIVNVSSGLAFVPLAVtPTY 152

                        170       180
                 ....*....|....*....|....*....
gi 568967027 177 CISKYGVEAFSDSLRRELSYFGVKVaiIE 205
Cdd:COG3967  153 SATKAALHSYTQSLRHQLKDTSVKV--IE 179
PRK07024 PRK07024
SDR family oxidoreductase;
32-214 3.85e-21

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 90.37  E-value: 3.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRGMRV-LAACLTE---KGAEELRNktSDRLETVILDVTKTESIVTATQWVKEHVGNRGLw 107
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLgLVARRTDalqAFAARLPK--AARVSVYAADVRDADALAAAAADFIAAHGLPDV- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 108 gLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSML-PLVRKARGRVVNVSSVMGRVSLFGGG-YCISKYGVEA 185
Cdd:PRK07024  82 -VIANAGISVGTLTEEREDLAVFREVMDTNYFGMVATFQPFIaPMRAARRGTLVGIASVAGVRGLPGAGaYSASKAAAIK 160

                        170       180
                 ....*....|....*....|....*....
gi 568967027 186 FSDSLRRELSYFGVKVAIIEPGFFLTGVT 214
Cdd:PRK07024 161 YLESLRVELRPAGVRVVTIAPGYIRTPMT 189
FabG-like PRK07231
SDR family oxidoreductase;
27-250 4.13e-21

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 90.27  E-value: 4.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKG----AEELRnkTSDRLETVILDVTKTESIVTATQWVKEHVG 102
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAaervAAEIL--AGGRAIAVAADVSDEADVEAAVAAALERFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 nrGLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMG-RVSLFGGGYCISK 180
Cdd:PRK07231  81 --SVDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGgGAIVNVASTAGlRPRPGLGWYNASK 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967027 181 YGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSarlcsntqmLWDQTSSEIReiygEKYLASY-LKRL 250
Cdd:PRK07231 159 GAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEA---------FMGEPTPENR----AKFLATIpLGRL 216
PRK07832 PRK07832
SDR family oxidoreductase;
30-219 2.01e-20

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 88.95  E-value: 2.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLaacLTEKGAEELRNKTSD---RLETVI----LDVTKTESIVTATQWVKEHVG 102
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELF---LTDRDADGLAQTVADaraLGGTVPehraLDISDYDAVAAFAADIHAAHG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 NRGLwgLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGR-VVNVSSVMGRVSL-FGGGYCIS 179
Cdd:PRK07832  78 SMDV--VMNIAGISA-WGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPpMVAAGRGGhLVNVSSAAGLVALpWHAAYSAS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568967027 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARL 219
Cdd:PRK07832 155 KFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVNTVEI 194
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 30-222 2.49e-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: 87.51  E-value: 2.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKT-SDRLETVILDVTKTESIVTATQWVKEHVGNRgLWG 108
Cdd:cd08931    1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELgAENVVAGALDVTDRAAWAAALADFAAATGGR-LDA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 109 LVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARG-RVVNVSSVMGrvsLFG----GGYCISKYGV 183
Cdd:cd08931   80 LFNNAGVGR-GGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGaRVINTASSSA---IYGqpdlAVYSATKFAV 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568967027 184 EAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLCSN 222
Cdd:cd08931  156 RGLTEALDVEWARHGIRVADVWPWFVDTPILTKGETGAA 194
PRK08219 PRK08219
SDR family oxidoreductase;
34-193 2.50e-20

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 87.68  E-value: 2.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  34 ITGCDSGFGTLLARQLDRRgMRVLAACLTEKGAEELRNkTSDRLETVILDVTKTESIVTATqwvkEHVGnrGLWGLVNNA 113
Cdd:PRK08219   8 ITGASRGIGAAIARELAPT-HTLLLGGRPAERLDELAA-ELPGATPFPVDLTDPEAIAAAV----EQLG--RLDVLVHNA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 114 GISTPsGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMG-RVSLFGGGYCISKYGVEAFSDSLRR 192
Cdd:PRK08219  80 GVADL-GPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGlRANPGWGSYAASKFALRALADALRE 158


                 .
gi 568967027 193 E 193
Cdd:PRK08219 159 E 159
PRK06484 PRK06484
short chain dehydrogenase; Validated
 32-211 5.97e-20

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 89.91  E-value: 5.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQwvkehvGNRGLWG--- 108
Cdd:PRK06484 272 VAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFA------QIQARWGrld 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 109 -LVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKArGRVVNVSSVMGRVSLFG-GGYCISKYGVEAF 186
Cdd:PRK06484 346 vLVNNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG-GVIVNLGSIASLLALPPrNAYCASKAAVTML 424

                        170       180
                 ....*....|....*....|....*
gi 568967027 187 SDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK06484 425 SRSLACEWAPAGIRVNTVAPGYIET 449
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 27-214 1.04e-19

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: 86.28  E-value: 1.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGnrGL 106
Cdd:cd05341    3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFG--RL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 107 WGLVNNAGISTPsGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKA-RGRVVNVSSVMGRVSLFG-GGYCISKYGVE 184
Cdd:cd05341   81 DVLVNNAGILTG-GTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAgGGSIINMSSIEGLVGDPAlAAYNASKGAVR 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568967027 185 AFSDSLRREL--SYFGVKVAIIEPGFFLTGVT 214
Cdd:cd05341  160 GLTKSAALECatQGYGIRVNSVHPGYIYTPMT 191
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 29-211 2.87e-19

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


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 85.74  E-value: 2.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  29 DKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNK-----TSDRLETVILDVTKTESIVTATQWVKEhvGN 103
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEikketGNAKVEVIQLDLSSLASVRQFAEEFLA--RF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 RGLWGLVNNAGISTPSgpnEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLFGGG------- 175
Cdd:cd05327   79 PRLDILINNAGIMAPP---RRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASApSRIVNVSSIAHRAGPIDFNdldlenn 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568967027 176 --------YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:cd05327  156 keyspykaYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRT 199
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 24-214 3.17e-19

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 85.02  E-value: 3.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  24 VSHLQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVTATQWVKEH 100
Cdd:PRK12939   2 ASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAaggRAHAIAADLADPASVQRFFDAAAAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 101 VGnrGLWGLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVR-KARGRVVNVSSvmgRVSLFG----GG 175
Cdd:PRK12939  82 LG--GLDGLVNNAGI-TNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRdSGRGRIVNLAS---DTALWGapklGA 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568967027 176 YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVT 214
Cdd:PRK12939 156 YVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEAT 194
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 24-211 4.07e-19

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 84.67  E-value: 4.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  24 VSHLQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEK-GAEELRNKTSDRLETVIL---DVTKTESIVTATQWVKE 99
Cdd:PRK12935   1 MVQLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKeAAENLVNELGKEGHDVYAvqaDVSKVEDANRLVEEAVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 100 HVGNRGLwgLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLFG-GGYC 177
Cdd:PRK12935  81 HFGKVDI--LVNNAGI-TRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEeGRIISISSIIGQAGGFGqTNYS 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568967027 178 ISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK12935 158 AAKAGMLGFTKSLALELAKTNVTVNAICPGFIDT 191
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 32-207 5.12e-19

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 84.42  E-value: 5.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRGLwgLVN 111
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDV--LVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 112 NAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSLFGGG-YCISKYGVEAFSDS 189
Cdd:PRK10538  81 NAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPgMVERNHGHIINIGSTAGSWPYAGGNvYGATKAFVRQFSLN 160

                        170
                 ....*....|....*...
gi 568967027 190 LRRELSYFGVKVAIIEPG 207
Cdd:PRK10538 161 LRTDLHGTAVRVTDIEPG 178
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
27-218 1.09e-18

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 83.52  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAAC-----LTEKGAEELRNKTSDRLETViLDVTKTESIVTATQWVKEHV 101
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAGCgpnspRRVKWLEDQKALGFDFIASE-GNVGDWDSTKAAFDKVKAEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 102 GNRGLwgLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSLFG-GGYCIS 179
Cdd:PRK12938  80 GEIDV--LVNNAGI-TRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDgMVERGWGRIINISSVNGQKGQFGqTNYSTA 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568967027 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSAR 218
Cdd:PRK12938 157 KAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIR 195
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 25-218 1.15e-18

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 83.68  E-value: 1.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  25 SHLQDKYVFITGCDSGFGTLLARQLDRRGMRVlaACL---TEKGAEELRNKTSdrlETVILDVTKTESIVTATQWVKEHV 101
Cdd:PRK06463   3 MRFKGKVALITGGTRGIGRAIAEAFLREGAKV--AVLynsAENEAKELREKGV---FTIKCDVGNRDQVKKSKEVVEKEF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 102 GNRGLwgLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMG-----RVSLFggg 175
Cdd:PRK06463  78 GRVDV--LVNNAGIMY-LMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKnGAIVNIASNAGigtaaEGTTF--- 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568967027 176 YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSAR 218
Cdd:PRK06463 152 YAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLSGK 194
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-207 1.29e-18

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 83.35  E-value: 1.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAAC-LTEKGAEELRNKTSDRLETVIL---DVTKTESIVTATQWVKEHVG 102
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYdINEEAAQELLEEIKEEGGDAIAvkaDVSSEEDVENLVEQIVEKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 nrGLWGLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSL-FGGGYCISK 180
Cdd:PRK05565  83 --KIDILVNNAGISN-FGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPyMIKRKSGVIVNISSIWGLIGAsCEVLYSASK 159

                        170       180
                 ....*....|....*....|....*..
gi 568967027 181 YGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK05565 160 GAVNAFTKALAKELAPSGIRVNAVAPG 186
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 30-211 1.60e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 83.23  E-value: 1.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDrlETVILDVTKTESIVTAtqwVKEHVGnrgLWGL 109
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGC--EPLRLDVGDDAAIRAA---LAAAGA---FDGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 110 VNNAGISTPSGPNEwMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKAR-GRVVNVSSVMGRVSL-FGGGYCISKYGVEAF 186
Cdd:PRK07060  82 VNCAGIASLESALD-MTAEGFDRVMAVNARGAALVARHVARaMIAAGRgGSIVNVSSQAALVGLpDHLAYCASKAALDAI 160

                        170       180
                 ....*....|....*....|....*
gi 568967027 187 SDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK07060 161 TRVLCVELGPHGIRVNSVNPTVTLT 185
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 27-214 2.14e-18

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 82.66  E-value: 2.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRV-LAACLTEKgAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGnrG 105
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVgLHGTRVEK-LEALAAELGERVKIFPANLSDRDEVKALGQKAEADLE--G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 106 LWGLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSML-PLVRKARGRVVNVSSVMGRVSLFG-GGYCISKYGV 183
Cdd:PRK12936  81 VDILVNNAGI-TKDGLFVRMSDEDWDSVLEVNLTATFRLTRELThPMMRRRYGRIINITSVVGVTGNPGqANYCASKAGM 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568967027 184 EAFSDSLRRELSYFGVKVAIIEPGFFLTGVT 214
Cdd:PRK12936 160 IGFSKSLAQEIATRNVTVNCVAPGFIESAMT 190
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 32-214 2.61e-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: 82.38  E-value: 2.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVTATQWVKEHVGnrGLWG 108
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNpnpSVEVEILDVTDEERNQLVIAELEAELG--GLDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 109 LVNNAGISTPSgPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSLFGG-GYCISKYGVEAF 186
Cdd:cd05350   79 VIINAGVGKGT-SLGDLSFKAFRETIDTNLLGAAAILEAALPqFRAKGRGHLVLISSVAALRGLPGAaAYSASKAALSSL 157

                        170       180
                 ....*....|....*....|....*...
gi 568967027 187 SDSLRRELSYFGVKVAIIEPGFFLTGVT 214
Cdd:cd05350  158 AESLRYDVKKRGIRVTVINPGFIDTPLT 185
PRK08267 PRK08267
SDR family oxidoreductase;
30-310 3.28e-18

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 82.29  E-value: 3.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNK-TSDRLETVILDVTKtesivtATQWVK------EHVG 102
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAElGAGNAWTGALDVTD------RAAWDAaladfaAATG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 NRgLWGLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARG-RVVNVSSVMGrvsLFGGG----YC 177
Cdd:PRK08267  76 GR-LDVLFNNAGILR-GGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGaRVINTSSASA---IYGQPglavYS 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 178 ISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFltgvtssarlcsNTQMLwDQTSSEIReiygekylASYLKRLnkldkrc 257
Cdd:PRK08267 151 ATKFAVRGLTEALDLEWRRHGIRVADVMPLFV------------DTAML-DGTSNEVD--------AGSTKRL------- 202

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568967027 258 nkdlsGV----TDCMEHALTACHPRTR--YSAGWDAKLFYLPLSYLPTFLVDALLYWTS 310
Cdd:PRK08267 203 -----GVrltpEDVAEAVWAAVQHPTRlhWPVGKQAKLLAFLARLSPGFVRRLINKSLA 256
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 29-208 5.68e-18

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


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 81.50  E-value: 5.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  29 DKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTE----KGAEELRNKTSDRLETVILDVTKTESIVTAtqwVKEHVGNR 104
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQekldAVAKEIEEKYGVETKTIAADFSAGDDIYER---IEKELEGL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 105 GLWGLVNNAGISTP-SGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRV-SLFGGGYCISKY 181
Cdd:cd05356   78 DIGILVNNVGISHSiPEYFLETPEDELQDIINVNVMATLKMTRLILPgMVKRKKGAIVNISSFAGLIpTPLLATYSASKA 157

                        170       180
                 ....*....|....*....|....*..
gi 568967027 182 GVEAFSDSLRRELSYFGVKVAIIEPGF 208
Cdd:cd05356  158 FLDFFSRALYEEYKSQGIDVQSLLPYL 184
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 27-207 1.08e-17

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


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 80.89  E-value: 1.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEK-GAEEL-RNKTSDRLETVIL--DVTKTESIVTATQWVKEHVG 102
Cdd:cd05358    1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEdAAEEVvEEIKAVGGKAIAVqaDVSKEEDVVALFQSAIKEFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 NRGLWglVNNAGISTPSGPNEwMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR--GRVVNVSSVMGRVSLFG-GGYCIS 179
Cdd:cd05358   81 TLDIL--VNNAGLQGDASSHE-MTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKikGKIINMSSVHEKIPWPGhVNYAAS 157

                        170       180
                 ....*....|....*....|....*...
gi 568967027 180 KYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:cd05358  158 KGGVKMMTKTLAQEYAPKGIRVNAIAPG 185
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 27-211 1.14e-17

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: 81.03  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSD-----RLETVILDVTKTESIVTATQWVKEHV 101
Cdd:cd05330    1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEiapdaEVLLIKADVSDEAQVEAYVDATVEQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 102 GNrgLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMG-RVSLFGGGYCIS 179
Cdd:cd05330   81 GR--IDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGsGMIVNTASVGGiRGVGNQSGYAAA 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568967027 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:cd05330  159 KHGVVGLTRNSAVEYGQYGIRINAIAPGAILT 190
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 27-217 1.37e-17

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: 80.61  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGnrGL 106
Cdd:cd08944    1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFG--GL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 107 WGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVR-KARGRVVNVSSVMGRV-SLFGGGYCISKYGVE 184
Cdd:cd08944   79 DLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIaRGGGSIVNLSSIAGQSgDPGYGAYGASKAAIR 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568967027 185 AFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSA 217
Cdd:cd08944  159 NLTRTLAAELRHAGIRCNALAPGLIDTPLLLAK 191
PRK05855 PRK05855
SDR family oxidoreductase;
29-218 1.68e-17

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 82.72  E-value: 1.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  29 DKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEElrnkTSDRLE-------TVILDVTKTESIVTATQWV-KEH 100
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAER----TAELIRaagavahAYRVDVSDADAMEAFAEWVrAEH 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 101 vgnrglwG----LVNNAGISTpSGPNEWMKKQDFAHVLDVNLLG-----------MIEvtlsmlplvRKARGRVVNVSSV 165
Cdd:PRK05855 391 -------GvpdiVVNNAGIGM-AGGFLDTSAEDWDRVLDVNLWGvihgcrlfgrqMVE---------RGTGGHIVNVASA 453

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568967027 166 MGrvslFG-----GGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSAR 218
Cdd:PRK05855 454 AA----YApsrslPAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVATTR 507
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 26-218 2.01e-17

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 80.00  E-value: 2.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  26 HLQDKYVFITGCDSGFGTLLARQLDRRGMRvLAacLTEKGAEELRNKTSD------RLETVILDVTKTESIVTATQWVKE 99
Cdd:PRK08217   2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAK-LA--LIDLNQEKLEEAVAEcgalgtEVRGYAANVTDEEDVEATFAQIAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 100 HVGnrGLWGLVNNAGI-------STPSGP-NEWMKKQDFAHVLDVNLLGMI----EVTLSMLPLVRKarGRVVNVSSV-- 165
Cdd:PRK08217  79 DFG--QLNGLINNAGIlrdgllvKAKDGKvTSKMSLEQFQSVIDVNLTGVFlcgrEAAAKMIESGSK--GVIINISSIar 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568967027 166 ---MGRVSlfgggYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSAR 218
Cdd:PRK08217 155 agnMGQTN-----YSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMK 205
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-206 2.41e-17

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 79.73  E-value: 2.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKG----AEELrNKTSDRLETVILDVTKTESIVTATQWVKEHVG 102
Cdd:PRK07666   5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENlkavAEEV-EAYGVKVVIATADVSDYEEVTAAIEQLKNELG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 NRGLwgLVNNAGISTPSG-----PNEWMKkqdfahVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMG-RVSLFGGG 175
Cdd:PRK07666  84 SIDI--LINNAGISKFGKfleldPAEWEK------IIQVNLMGVYYATRAVLPsMIERQSGDIINISSTAGqKGAAVTSA 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568967027 176 YCISKYGVEAFSDSLRRELSYFGVKVAIIEP 206
Cdd:PRK07666 156 YSASKFGVLGLTESLMQEVRKHNIRVTALTP 186
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 31-218 8.41e-17

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: 78.10  E-value: 8.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  31 YVFITGCDSGFGTLLARQLDRRGMRVLAACLTE------KGAEELRNktSDRLETVILDVTKT---ESIVTATQWV-KEH 100
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARseeplqELKEELRP--GLRVTTVKADLSDAagvEQLLEAIRKLdGER 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 101 VGnrglwgLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR--GRVVNVSSVMGRVSLFG-GGYC 177
Cdd:cd05367   79 DL------LINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGlkKTVVNVSSGAAVNPFKGwGLYC 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568967027 178 ISKYGVEAFSDSLRRELSyfGVKVAIIEPGFFLTGVTSSAR 218
Cdd:cd05367  153 SSKAARDMFFRVLAAEEP--DVRVLSYAPGVVDTDMQREIR 191
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 27-208 1.51e-16

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 77.69  E-value: 1.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVTATQWVKEHVGn 103
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDlgrRALAVPTDITDEDQCANLVALALERFG- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 rGLWGLVNNAGISTPSGPNEwmkKQDFAH---VLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRVSLFG-GGYCIS 179
Cdd:PRK07890  82 -RVDALVNNAFRVPSMKPLA---DADFAHwraVIELNVLGTLRLTQAFTPALAESGGSIVMINSMVLRHSQPKyGAYKMA 157

                        170       180
                 ....*....|....*....|....*....
gi 568967027 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGF 208
Cdd:PRK07890 158 KGALLAASQSLATELGPQGIRVNSVAPGY 186
PRK07454 PRK07454
SDR family oxidoreductase;
32-207 1.90e-16

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 77.31  E-value: 1.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRGMRVL----AACLTEKGAEELRNKTSdRLETVILDVTKTESIVTATQWVKEHVGNRGLw 107
Cdd:PRK07454   9 ALITGASSGIGKATALAFAKAGWDLAlvarSQDALEALAAELRSTGV-KAAAYSIDLSNPEAIAPGIAELLEQFGCPDV- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 108 gLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLFG-GGYCISKYGVEA 185
Cdd:PRK07454  87 -LINNAGMAY-TGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGgGLIINVSSIAARNAFPQwGAYCVSKAALAA 164

                        170       180
                 ....*....|....*....|..
gi 568967027 186 FSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK07454 165 FTKCLAEEERSHGIRVCTITLG 186
PRK06114 PRK06114
SDR family oxidoreductase;
27-230 2.22e-16

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 77.13  E-value: 2.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVlaACLTEKGAEELRnKTSDRLET-------VILDVTKTESIVTATQWVKE 99
Cdd:PRK06114   6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADV--ALFDLRTDDGLA-ETAEHIEAagrraiqIAADVTSKADLRAAVARTEA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 100 HVGNRGLwgLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGmieVTLS-------MLPlvrKARGRVVNVSSVMGRVS-- 170
Cdd:PRK06114  83 ELGALTL--AVNAAGIAN-ANPAEEMEEEQWQTVMDINLTG---VFLScqaearaMLE---NGGGSIVNIASMSGIIVnr 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967027 171 -LFGGGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLCSNTQMLWDQT 230
Cdd:PRK06114 154 gLLQAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTRPEMVHQTKLFEEQT 214
PRK08589 PRK08589
SDR family oxidoreductase;
27-207 2.63e-16

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 77.51  E-value: 2.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELR--NKTSDRLETVILDVTKTESIVTATQWVKEHVGNR 104
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDkiKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 105 GLwgLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRVS-LFGGGYCISKYGV 183
Cdd:PRK08589  84 DV--LFNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAAdLYRSGYNAAKGAV 161

                        170       180
                 ....*....|....*....|....
gi 568967027 184 EAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK08589 162 INFTKSIAIEYGRDGIRANAIAPG 185
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 28-211 3.05e-16

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: 77.19  E-value: 3.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  28 QDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNK--TSDRLETVIL--DVTKTESIVTATQWVKEHVGN 103
Cdd:cd08933    8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESElnRAGPGSCKFVpcDVTKEEDIKTLISVTVERFGR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 rgLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRV-SLFGGGYCISKYG 182
Cdd:cd08933   88 --IDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIgQKQAAPYVATKGA 165

                        170       180
                 ....*....|....*....|....*....
gi 568967027 183 VEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:cd08933  166 ITAMTKALAVDESRYGVRVNCISPGNIWT 194
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 27-207 3.45e-16

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


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 76.73  E-value: 3.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVI-LDVTKTESIVTATQWVKEHVGNrg 105
Cdd:cd05326    2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFVhCDVTVEADVRAAVDTAVARFGR-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 106 LWGLVNNAGI-STPSGPNEWMKKQDFAHVLDVNL----LGMIEVTLSMLPlvrKARGRVVNVSSVMGRVSLFGG-GYCIS 179
Cdd:cd05326   80 LDIMFNNAGVlGAPCYSILETSLEEFERVLDVNVygafLGTKHAARVMIP---AKKGSIVSVASVAGVVGGLGPhAYTAS 156

                        170       180
                 ....*....|....*....|....*...
gi 568967027 180 KYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:cd05326  157 KHAVLGLTRSAATELGEHGIRVNCVSPY 184
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 27-211 3.52e-16

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 76.85  E-value: 3.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGA---EELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGn 103
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAaaaAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 rGLWGLVNNAGISTPSgPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRV-SLFGGGYCISKY 181
Cdd:PRK12429  81 -GVDILVNNAGIQHVA-PIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGgGRIINMASVHGLVgSAGKAAYVSAKH 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 568967027 182 GVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK12429 159 GLIGLTKVVALEGATHGVTVNAICPGYVDT 188
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 29-212 4.28e-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: 76.54  E-value: 4.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  29 DKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKG----AEELRnKTSDRLETVILDVTKTESIVTATQWVKEHVGnr 104
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENleraASELR-AGGAGVLAVVADLTDPEDIDRLVEKAGDAFG-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 105 GLWGLVNNAGiSTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLFGGGYC-ISKYG 182
Cdd:cd05344   78 RVDILVNNAG-GPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLTVKEPEPNLVLSnVARAG 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 568967027 183 VEAFSDSLRRELSYFGVKVAIIEPGFFLTG 212
Cdd:cd05344  157 LIGLVKTLSRELAPDGVTVNSVLPGYIDTE 186
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 26-211 5.02e-16

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 75.99  E-value: 5.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  26 HLQDKYVFITGCDSGFGTLLARQLDRRGMRVLaacLTEKGAEELRNKTSDRLETVI----LDVTKTESIVTATQWVKEHV 101
Cdd:PRK12828   4 SLQGKVVAITGGFGGLGRATAAWLAARGARVA---LIGRGAAPLSQTLPGVPADALriggIDLVDPQAARRAVDEVNRQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 102 GnrGLWGLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSLFG-GGYCIS 179
Cdd:PRK12828  81 G--RLDALVNIAGA-FVWGTIADGDADTWDRMYGVNVKTTLNASKAALPaLTASGGGRIVNIGAGAALKAGPGmGAYAAA 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568967027 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK12828 158 KAGVARLTEALAAELLDRGITVNAVLPSIIDT 189
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 27-229 7.32e-16

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: 75.83  E-value: 7.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRV----LAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVG 102
Cdd:cd05352    6 LKGKVAIVTGGSRGIGLAIARALAEAGADVaiiyNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 NrgLWGLVNNAGISTPSgPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVMGRV---SLFGGGYCI 178
Cdd:cd05352   86 K--IDILIANAGITVHK-PALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKqGKGSLIITASMSGTIvnrPQPQAAYNA 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568967027 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARlcSNTQMLWDQ 229
Cdd:cd05352  163 SKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVD--KELRKKWES 211
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 27-211 1.22e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 75.08  E-value: 1.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRGL 106
Cdd:PRK06841  13 LSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRIDI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 107 wgLVNNAGIStPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSLFGG-GYCISKYGVE 184
Cdd:PRK06841  93 --LVNSAGVA-LLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRhMIAAGGGKIVNLASQAGVVALERHvAYCASKAGVV 169

                        170       180
                 ....*....|....*....|....*..
gi 568967027 185 AFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK06841 170 GMTKVLALEWGPYGITVNAISPTVVLT 196
PRK06949 PRK06949
SDR family oxidoreductase;
27-211 1.33e-15

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 75.18  E-value: 1.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRV-LAACLTEKgAEELRNKTSDR---LETVILDVTKTESIVTATQWVKEHVG 102
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVvLASRRVER-LKELRAEIEAEggaAHVVSLDVTDYQSIKAAVAHAETEAG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 NRGLwgLVNNAGISTPSGPNEwMKKQDFAHVLDVNLLGMI----EVTLSMLPLVR-----KARGRVVNVSSVMG-RVSLF 172
Cdd:PRK06949  86 TIDI--LVNNSGVSTTQKLVD-VTPADFDFVFDTNTRGAFfvaqEVAKRMIARAKgagntKPGGRIINIASVAGlRVLPQ 162

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568967027 173 GGGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK06949 163 IGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDT 201
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
27-207 1.60e-15

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 74.68  E-value: 1.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGnrGL 106
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFG--GI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 107 WGLVNNAGISTPSGPNEwMKKQDFAHVLDVNLLGMI----EVTLSMLPlvRKARGRVVNVSSVMGR-----VSLfgggYC 177
Cdd:PRK07067  82 DILFNNAALFDMAPILD-ISRDSYDRLFAVNVKGLFflmqAVARHMVE--QGRGGKIINMASQAGRrgealVSH----YC 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 568967027 178 ISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK07067 155 ATKAAVISYTQSAALALIRHGINVNAIAPG 184
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 23-211 1.62e-15

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 74.93  E-value: 1.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  23 VVSHLQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAE---ELRNKTSDRLETVILDVTKTESIVTATQWVKE 99
Cdd:PRK13394   1 MMSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANavaDEINKAGGKAIGVAMDVTNEDAVNAGIDKVAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 100 HVGNRGLwgLVNNAGISTPSgPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR--GRVVNVSSVMGRV-SLFGGGY 176
Cdd:PRK13394  81 RFGSVDI--LVSNAGIQIVN-PIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHSHEaSPLKSAY 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568967027 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK13394 158 VTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRT 192
PRK06194 PRK06194
hypothetical protein; Provisional
 27-218 2.19e-15

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 75.05  E-value: 2.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMR-VLAACLT---EKGAEELRNKTSDRLeTVILDVTKTESIVTATQWVKEHVG 102
Cdd:PRK06194   4 FAGKVAVITGAASGFGLAFARIGAALGMKlVLADVQQdalDRAVAELRAQGAEVL-GVRTDVSDAAQVEALADAALERFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 NRGLwgLVNNAGIStpSGPNEW-MKKQDFAHVLDVNLLGMIEVTLSMLPLVRKA-------RGRVVNVSSVMGRVSLFGG 174
Cdd:PRK06194  83 AVHL--LFNNAGVG--AGGLVWeNSLADWEWVLGVNLWGVIHGVRAFTPLMLAAaekdpayEGHIVNTASMAGLLAPPAM 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568967027 175 G-YCISKYGVEAFSDSLRRELSYFG--VKVAIIEPGFFLTGVTSSAR 218
Cdd:PRK06194 159 GiYNVSKHAVVSLTETLYQDLSLVTdqVGASVLCPYFVPTGIWQSER 205
PRK07063 PRK07063
SDR family oxidoreductase;
27-214 2.53e-15

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 74.32  E-value: 2.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRV----LAACLTEKGAEELRNKTSD-RLETVILDVTKTESIVTATQWVKEHV 101
Cdd:PRK07063   5 LAGKVALVTGAAQGIGAAIARAFAREGAAValadLDAALAERAAAAIARDVAGaRVLAVPADVTDAASVAAAVAAAEEAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 102 GnrGLWGLVNNAGISTPSGPNEwMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSLFGG-GYCIS 179
Cdd:PRK07063  85 G--PLDVLVNNAGINVFADPLA-MTDEDWRRCFAVDLDGAWNGCRAVLPgMVERGRGSIVNIASTHAFKIIPGCfPYPVA 161

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568967027 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVT 214
Cdd:PRK07063 162 KHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLT 196
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 27-212 3.22e-15

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: 74.09  E-value: 3.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAAC----LTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVG 102
Cdd:cd05343    4 WRGRVALVTGASVGIGAAVARALVQHGMKVVGCArrvdKIEALAAECQSAGYPTLFPYQCDLSNEEQILSMFSAIRTQHQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 nrGLWGLVNNAGISTP----SGPNEWMKKqdfahVLDVNLLGMIEVT---LSMLPLVRKARGRVVNVSSVMGR----VSL 171
Cdd:cd05343   84 --GVDVCINNAGLARPepllSGKTEGWKE-----MFDVNVLALSICTreaYQSMKERNVDDGHIININSMSGHrvppVSV 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568967027 172 FgGGYCISKYGVEAFSDSLRRELSYF--GVKVAIIEPGFFLTG 212
Cdd:cd05343  157 F-HFYAATKHAVTALTEGLRQELREAktHIRATSISPGLVETE 198
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 27-238 6.50e-15

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


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 72.99  E-value: 6.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLaacLTEKGAEELRnKTSDRLET--------VILDVTK--TESIVTATQW 96
Cdd:cd05340    2 LNDRIILVTGASDGIGREAALTYARYGATVI---LLGRNEEKLR-QVADHINEeggrqpqwFILDLLTctSENCQQLAQR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  97 VKEHVGNrgLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRV-SLFGG 174
Cdd:cd05340   78 IAVNYPR--LDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQgRANWG 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568967027 175 GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLCSNTQMLwdQTSSEIREIY 238
Cdd:cd05340  156 AYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRASAFPTEDPQKL--KTPADIMPLY 217
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 33-241 7.72e-15

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


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 72.96  E-value: 7.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  33 FITGCDSGFGTLLARQLDRRGMRVLaacLTEKGAEELRnKTSDRLETVILDVTKTESIVTATQWVKEHVGN-RGLWG--- 108
Cdd:cd08945    7 LVTGATSGIGLAIARRLGKEGLRVF---VCARGEEGLA-TTVKELREAGVEADGRTCDVRSVPEIEALVAAaVARYGpid 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 109 -LVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP---LVRKARGRVVNVSSVMGRVS-LFGGGYCISKYGV 183
Cdd:cd08945   83 vLVNNAGRSG-GGATAELADELWLDVVETNLTGVFRVTKEVLKaggMLERGTGRIINIASTGGKQGvVHAAPYSASKHGV 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568967027 184 EAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARlcSNTQMLWDQTSSEIREIYGEK 241
Cdd:cd08945  162 VGFTKALGLELARTGITVNAVCPGFVETPMAASVR--EHYADIWEVSTEEAFDRITAR 217
PRK09242 PRK09242
SDR family oxidoreductase;
27-216 1.25e-14

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 72.47  E-value: 1.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSD-----RLETVILDVTKTESIVTATQWVKEHV 101
Cdd:PRK09242   7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEefperEVHGLAADVSDDEDRRAILDWVEDHW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 102 GnrGLWGLVNNAGISTPSGPNEWmKKQDFAHVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVMGRVSLFGGG-YCIS 179
Cdd:PRK09242  87 D--GLHILVNNAGGNIRKAAIDY-TEDEWRGIFETNLFSAFELSRYAHPLLKQhASSAIVNIGSVSGLTHVRSGApYGMT 163

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568967027 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSS 216
Cdd:PRK09242 164 KAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSG 200
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 27-211 1.95e-14

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: 72.11  E-value: 1.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLT-EKG---AEELRNK--TSDRLETvilDVTKTESIVTATQWVKEH 100
Cdd:cd08935    3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNqEKGdkvAKEITALggRAIALAA---DVLDRASLERAREEIVAQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 101 VGNRGLwgLVNNAGISTPSG--PNEW-----------MKKQDFAHVLDVNLLGmiEVTLSML---PLVRKARGRVVNVSS 164
Cdd:cd08935   80 FGTVDI--LINGAGGNHPDAttDPEHyepeteqnffdLDEEGWEFVFDLNLNG--SFLPSQVfgkDMLEQKGGSIINISS 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568967027 165 V-----MGRVSlfggGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:cd08935  156 MnafspLTKVP----AYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVT 203
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 13-214 2.03e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 71.90  E-value: 2.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  13 TLLRFFRvrqvvshLQDKYVFITGCDSGFGTLLARQLDRRGMRVLaacLTEKGAEELRNK----TSDRLETVIL--DVTK 86
Cdd:PRK08213   3 TVLELFD-------LSGKTALVTGGSRGLGLQIAEALGEAGARVV---LSARKAEELEEAaahlEALGIDALWIaaDVAD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  87 TESIVTATQWVKEHVGNRGLwgLVNNAGiSTPSGPNEWMKKQDFAHVLDVNLLGMIEVT-----LSMLPlvRKArGRVVN 161
Cdd:PRK08213  73 EADIERLAEETLERFGHVDI--LVNNAG-ATWGAPAEDHPVEAWDKVMNLNVRGLFLLSqavakRSMIP--RGY-GRIIN 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967027 162 VSSVMGrvsLFGG--------GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVT 214
Cdd:PRK08213 147 VASVAG---LGGNppevmdtiAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMT 204
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 27-254 2.20e-14

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


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 71.54  E-value: 2.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEK-GAEELR---NKTSDRLETVILDVTKTESIVTATQWVKEHVG 102
Cdd:cd05362    1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNYASSKaAAEEVVaeiEAAGGKAIAVQADVSDPSQVARLFDAAEKAFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 nrGLWGLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRkARGRVVNVSSVMGRVSL-FGGGYCISKY 181
Cdd:cd05362   81 --GVDILVNNAGV-MLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLR-DGGRIINISSSLTAAYTpNYGAYAGSKA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967027 182 GVEAFSDSLRRELSYFGVKVAIIEPGFFltgvtssarlcsNTQMLWDQTSSEIREIYGEkylASYLKRLNKLD 254
Cdd:cd05362  157 AVEAFTRVLAKELGGRGITVNAVAPGPV------------DTDMFYAGKTEEAVEGYAK---MSPLGRLGEPE 214
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 27-206 3.32e-14

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: 70.88  E-value: 3.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGnrGL 106
Cdd:cd05345    3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFG--RL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 107 WGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRV-VNVSSVMG---RVSLfgGGYCISKYG 182
Cdd:cd05345   81 DILVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGViINIASTAGlrpRPGL--TWYNASKGW 158

                        170       180
                 ....*....|....*....|....
gi 568967027 183 VEAFSDSLRRELSYFGVKVAIIEP 206
Cdd:cd05345  159 VVTATKAMAVELAPRNIRVNCLCP 182
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 27-207 4.34e-14

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 70.81  E-value: 4.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEElrnktsDRLETVILDVTKTESIVTATQWVKEHVGnrGL 106
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQH------ENYQFVPTDVSSAEEVNHTVAEIIEKFG--RI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 107 WGLVNNAGISTP---------SGPNEwMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMG-RVSLFGGG 175
Cdd:PRK06171  79 DGLVNNAGINIPrllvdekdpAGKYE-LNEAAFDKMFNINQKGVFLMSQAVARqMVKQHDGVIVNMSSEAGlEGSEGQSC 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568967027 176 YCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK06171 158 YAATKAALNSFTRSWAKELGKHNIRVVGVAPG 189
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 27-223 4.40e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 70.55  E-value: 4.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVTATQWVKEHVGn 103
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQegiKAHAAPFNVTHKQEVEAAIEHIEKDIG- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 rGLWGLVNNAGISTPSGPNEWmKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSV---MGRVSLfgGGYCIS 179
Cdd:PRK08085  86 -PIDVLINNAGIQRRHPFTEF-PEQEWNDVIAVNQTAVFLVSQAVARyMVKRQAGKIINICSMqseLGRDTI--TPYAAS 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568967027 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTS--------SARLCSNT 223
Cdd:PRK08085 162 KGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKalvedeafTAWLCKRT 213
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 27-207 4.58e-14

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 70.91  E-value: 4.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLT-EKGAEELRN---KTSDRLETVILDVTKTESIVTATQWVKEHVG 102
Cdd:PRK08936   5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSdEEEANDVAEeikKAGGEAIAVKGDVTVESDVVNLIQTAVKEFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 NRGLWglVNNAGISTPSgPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRK--ARGRVVNVSSVMGRV--SLFgGGYCI 178
Cdd:PRK08936  85 TLDVM--INNAGIENAV-PSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEhdIKGNIINMSSVHEQIpwPLF-VHYAA 160

                        170       180
                 ....*....|....*....|....*....
gi 568967027 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK08936 161 SKGGVKLMTETLAMEYAPKGIRVNNIGPG 189
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 34-211 5.59e-14

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 70.40  E-value: 5.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  34 ITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRnKTSDRLETVILDVTKTESIVTATQWVKEHVGNrgLWGLVNNA 113
Cdd:cd05371    7 VTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVA-KLGDNCRFVPVDVTSEKDVKAALALAKAKFGR--LDIVVNCA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 114 GIS----TPSGPNEWMKK-QDFAHVLDVNLLGmievTLSMLPLVRKA-----------RGRVVNVSSVMGRVSLFG-GGY 176
Cdd:cd05371   84 GIAvaakTYNKKGQQPHSlELFQRVINVNLIG----TFNVIRLAAGAmgknepdqggeRGVIINTASVAAFEGQIGqAAY 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568967027 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:cd05371  160 SASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDT 194
PRK06484 PRK06484
short chain dehydrogenase; Validated
 28-211 5.72e-14

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 72.19  E-value: 5.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  28 QDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRGLw 107
Cdd:PRK06484   4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDV- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 108 gLVNNAGISTPS-GPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR--GRVVNVSSVMGRVSLFG-GGYCISKYGV 183
Cdd:PRK06484  83 -LVNNAGVTDPTmTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGhgAAIVNVASGAGLVALPKrTAYSASKAAV 161

                        170       180
                 ....*....|....*....|....*...
gi 568967027 184 EAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK06484 162 ISLTRSLACEWAAKGIRVNAVLPGYVRT 189
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 27-239 7.05e-14

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 69.91  E-value: 7.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELrnktsdRLETVILDVTKTESIVTATQWVKEHVGnrGL 106
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDY------PFATFVLDVSDAAAVAQVCQRLLAETG--PL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 107 WGLVNNAGISTPsGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSLFG-GGYCISKYGVE 184
Cdd:PRK08220  78 DVLVNAAGILRM-GATDSLSDEDWQQTFAVNAGGAFNLFRAVMPqFRRQRSGAIVTVGSNAAHVPRIGmAAYGASKAALT 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568967027 185 AFSDSLRRELSYFGVKVAIIEPGffltgvtssarlCSNTQM---LWDQTSSEIREIYG 239
Cdd:PRK08220 157 SLAKCVGLELAPYGVRCNVVSPG------------STDTDMqrtLWVDEDGEQQVIAG 202
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 27-217 1.56e-13

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 68.98  E-value: 1.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLET-------VILDVTKTESIVTATQWVKE 99
Cdd:PRK12827   4 LDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAVAAGIEAaggkalgLAFDVRDFAATRAALDAGVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 100 HVGnrGLWGLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR--GRVVNVSSVMG-RVSLFGGGY 176
Cdd:PRK12827  84 EFG--RLDILVNNAGI-ATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARrgGRIVNIASVAGvRGNRGQVNY 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568967027 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSA 217
Cdd:PRK12827 161 AASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADNA 201
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 30-241 1.61e-13

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: 69.33  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACL----TEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGnrG 105
Cdd:cd05366    3 KVAIITGAAQGIGRAIAERLAADGFNIVLADLnleeAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFG--S 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 106 LWGLVNNAGIStPSGPNEWMKKQDFAHVLDVN----LLGMIEVTLSMLPLVRKarGRVVNVSSVMGRVSLFG-GGYCISK 180
Cdd:cd05366   81 FDVMVNNAGIA-PITPLLTITEEDLKKVYAVNvfgvLFGIQAAARQFKKLGHG--GKIINASSIAGVQGFPNlGAYSASK 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967027 181 YGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGvtssarlcsntqmLWDQTSSEIREIYGEK 241
Cdd:cd05366  158 FAVRGLTQTAAQELAPKGITVNAYAPGIVKTE-------------MWDYIDEEVGEIAGKP 205
PRK07775 PRK07775
SDR family oxidoreductase;
25-216 2.87e-13

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 68.63  E-value: 2.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  25 SHLQDKYVFITGCDSGFGTLLARQLDRRGMRV-LAACLTEKGAEELRNKTSDRLETVI--LDVTKTESIVTATQWVKEHV 101
Cdd:PRK07775   6 PHPDRRPALVAGASSGIGAATAIELAAAGFPVaLGARRVEKCEELVDKIRADGGEAVAfpLDVTDPDSVKSFVAQAEEAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 102 GNRGLwgLVNNAGISTPSGPNEwMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSS-VMGRVSLFGGGYCIS 179
Cdd:PRK07775  86 GEIEV--LVSGAGDTYFGKLHE-ISTEQFESQVQIHLVGANRLATAVLPgMIERRRGDLIFVGSdVALRQRPHMGAYGAA 162

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568967027 180 KYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSS 216
Cdd:PRK07775 163 KAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGMGWS 199
PRK06947 PRK06947
SDR family oxidoreductase;
30-236 4.77e-13

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 67.52  E-value: 4.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRV-------LAAclTEKGAEELRnKTSDRLETVILDVTKTESIVTATQWVKEHVG 102
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVginyardAAA--AEETADAVR-AAGGRACVVAGDVANEADVIAMFDAVQSAFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 nrGLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR----GRVVNVSSVMGRVslfgGG--- 175
Cdd:PRK06947  80 --RLDALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRggrgGAIVNVSSIASRL----GSpne 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967027 176 ---YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSS-------ARLCSNTQMLWDQTSSEIRE 236
Cdd:PRK06947 154 yvdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHASggqpgraARLGAQTPLGRAGEADEVAE 224
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 34-224 4.78e-13

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 68.06  E-value: 4.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  34 ITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEE----LRNKTSDrLETVILDVTKTESIVTATQWVKEHVGNRGLwgL 109
Cdd:PRK05876  11 ITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQavnhLRAEGFD-VHGVMCDVRHREEVTHLADEAFRLLGHVDV--V 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 110 VNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP--LVRKARGRVVNVSSVMGRVSLFG-GGYCISKYGVEAF 186
Cdd:PRK05876  88 FSNAGIVV-GGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPrlLEQGTGGHVVFTASFAGLVPNAGlGAYGVAKYGVVGL 166

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568967027 187 SDSLRRELSYFGVKVAIIEPgffltgVTSSARLCSNTQ 224
Cdd:PRK05876 167 AETLAREVTADGIGVSVLCP------MVVETNLVANSE 198
PRK07774 PRK07774
SDR family oxidoreductase;
27-207 6.01e-13

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 67.46  E-value: 6.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVI---LDVTKTESIVTATQWVKEHVGn 103
Cdd:PRK07774   4 FDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIavqVDVSDPDSAKAMADATVSAFG- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 rGLWGLVNNAGISTPSGPNEWMKK--QDFAHVLDVNLLGMIEVTLSMLPLVRKARG-RVVNVSSVMGrvSLFGGGYCISK 180
Cdd:PRK07774  83 -GIDYLVNNAAIYGGMKLDLLITVpwDYYKKFMSVNLDGALVCTRAVYKHMAKRGGgAIVNQSSTAA--WLYSNFYGLAK 159

                        170       180
                 ....*....|....*....|....*..
gi 568967027 181 YGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK07774 160 VGLNGLTQQLARELGGMNIRVNAIAPG 186
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 32-236 6.94e-13

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: 67.11  E-value: 6.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRGMRVLAACLtekgAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGnrGLWGLVN 111
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIALDL----PFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHG--PIDALVN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 112 NAGISTPsGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMG---RVSLfgGGYCISKYGVEAFS 187
Cdd:cd05331   75 CAGVLRP-GATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRtGAIVTVASNAAhvpRISM--AAYGASKAALASLS 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568967027 188 DSLRRELSYFGVKVAIIEPGffltgvtsSARlcsnTQMLWDQTSSEIRE 236
Cdd:cd05331  152 KCLGLELAPYGVRCNVVSPG--------STD----TAMQRTLWHDEDGA 188
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 26-219 1.01e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 66.85  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  26 HLQDKYVFITGCDSGFGTLLARQLDRRGMRVLAAcltekgAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGnrG 105
Cdd:PRK06523   6 ELAGKRALVTGGTKGIGAATVARLLEAGARVVTT------ARSRPDDLPEGVEFVAADLTTAEGCAAVARAVLERLG--G 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 106 LWGLVNNAGIS-TPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSLFGG--GYCISKY 181
Cdd:PRK06523  78 VDILVHVLGGSsAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPgMIARGSGVIIHVTSIQRRLPLPESttAYAAAKA 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568967027 182 GVEAFSDSLRRELSYFGVKVAIIEPGFFLTgvTSSARL 219
Cdd:PRK06523 158 ALSTYSKSLSKEVAPKGVRVNTVSPGWIET--EAAVAL 193
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 27-211 1.19e-12

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 66.85  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGcdsGFGTL---LARQLDRRGMRVLAACLT-EKG---AEELRNKTSDRLeTVILDVTKTESIVTATQWVKE 99
Cdd:PRK08277   8 LKGKVAVITG---GGGVLggaMAKELARAGAKVAILDRNqEKAeavVAEIKAAGGEAL-AVKADVLDKESLEQARQQILE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 100 HVGNRGLwgLVNNAGISTPSG--PNEW------------MKKQDFAHVLDVNLLGmievtlSMLP-------LVRKARGR 158
Cdd:PRK08277  84 DFGPCDI--LINGAGGNHPKAttDNEFhelieptktffdLDEEGFEFVFDLNLLG------TLLPtqvfakdMVGRKGGN 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568967027 159 VVNVSSV-----MGRVSlfggGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK08277 156 IINISSMnaftpLTKVP----AYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLT 209
PRK06139 PRK06139
SDR family oxidoreductase;
27-211 1.45e-12

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 67.05  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMR-VLAACLTE---KGAEELRNKTSDRLeTVILDVTKTESIVTATQWVKEHVG 102
Cdd:PRK06139   5 LHGAVVVITGASSGIGQATAEAFARRGARlVLAARDEEalqAVAEECRALGAEVL-VVPTDVTDADQVKALATQAASFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 NRGLWglVNNAGI-------STPSGPNEwmkkqdfaHVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVMGRVSL-FG 173
Cdd:PRK06139  84 RIDVW--VNNVGVgavgrfeETPIEAHE--------QVIQTNLIGYMRDAHAALPIFKKqGHGIFINMISLGGFAAQpYA 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568967027 174 GGYCISKYGVEAFSDSLRRELSYF-GVKVAIIEPGFFLT 211
Cdd:PRK06139 154 AAYSASKFGLRGFSEALRGELADHpDIHVCDVYPAFMDT 192
PRK07201 PRK07201
SDR family oxidoreductase;
18-204 1.70e-12

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 68.05  E-value: 1.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  18 FRVRQVVSHLQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVIL---DVTKTESIVTAT 94
Cdd:PRK07201 360 ARRRDLRGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAytcDLTDSAAVDHTV 439

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  95 QWVKEHVGNRGLwgLVNNAGIST-PSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSS--VMGRVS 170
Cdd:PRK07201 440 KDILAEHGHVDY--LVNNAGRSIrRSVENSTDRFHDYERTMAVNYFGAVRLILGLLPHMRERRfGHVVNVSSigVQTNAP 517

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568967027 171 LFgGGYCISKYGVEAFSDSLRRELSYFGVKVAII 204
Cdd:PRK07201 518 RF-SAYVASKAALDAFSDVAASETLSDGITFTTI 550
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 27-211 1.71e-12

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


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 65.96  E-value: 1.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDrLETVILDVTKTESivtatqwVKEHVGNRGL 106
Cdd:cd05351    5 FAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPG-IEPVCVDLSDWDA-------TEEALGSVGP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 107 W-GLVNNAGISTPSgPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP--LVRKARGRVVNVSSVMGRVSLFG-GGYCISKYG 182
Cdd:cd05351   77 VdLLVNNAAVAILQ-PFLEVTKEAFDRSFDVNVRAVIHVSQIVARgmIARGVPGSIVNVSSQASQRALTNhTVYCSTKAA 155

                        170       180
                 ....*....|....*....|....*....
gi 568967027 183 VEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:cd05351  156 LDMLTKVMALELGPHKIRVNSVNPTVVMT 184
PRK08628 PRK08628
SDR family oxidoreductase;
26-204 2.06e-12

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 66.14  E-value: 2.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  26 HLQDKYVFITGCDSGFGTLLARQLDRRG-MRVLAACLTEKG--AEELRNKTSdRLETVILDVTKTESIVTATQWVKEHVG 102
Cdd:PRK08628   4 NLKDKVVIVTGGASGIGAAISLRLAEEGaIPVIFGRSAPDDefAEELRALQP-RAEFVQVDLTDDAQCRDAVEQTVAKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 nrGLWGLVNNAG----ISTPSGPNEWMKKqdfahvLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSvmgRVSLFG----G 174
Cdd:PRK08628  83 --RIDGLVNNAGvndgVGLEAGREAFVAS------LERNLIHYYVMAHYCLPHLKASRGAIVNISS---KTALTGqggtS 151

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568967027 175 GYCISKYGVEAFSDSLRRELSYFGVKV-AII 204
Cdd:PRK08628 152 GYAAAKGAQLALTREWAVALAKDGVRVnAVI 182
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 27-236 2.37e-12

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 65.53  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVL-----AACLTEKGAEELRnKTSDRLETVILDVTKTESIVTATQWVKEHV 101
Cdd:PRK12937   3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAvnyagSAAAADELVAEIE-AAGGRAIAVQADVADAAAVTRLFDAAETAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 102 GnrGLWGLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKArGRVVNVSSVMGRVSLFGGG-YCISK 180
Cdd:PRK12937  82 G--RIDVLVNNAGV-MPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQG-GRIINLSTSVIALPLPGYGpYAASK 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568967027 181 YGVEAFSDSLRRELSYFGVKVAIIEPGffltgvtssarlCSNTQMLWDQTSSEIRE 236
Cdd:PRK12937 158 AAVEGLVHVLANELRGRGITVNAVAPG------------PVATELFFNGKSAEQID 201
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 29-216 2.39e-12

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 65.37  E-value: 2.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  29 DKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGaeelrnKTSDRLETVILDVTKTESivTATQWVKEhvgnrgLWG 108
Cdd:PRK06550   5 TKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDKP------DLSGNFHFLQLDLSDDLE--PLFDWVPS------VDI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 109 LVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSlfGGG---YCISKYGVE 184
Cdd:PRK06550  71 LCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPqMLERKSGIIINMCSIASFVA--GGGgaaYTASKHALA 148

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568967027 185 AFSDSLRRELSYFGVKVAIIEPGFFLTGVTSS 216
Cdd:PRK06550 149 GFTKQLALDYAKDGIQVFGIAPGAVKTPMTAA 180
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 30-207 3.33e-12

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: 65.18  E-value: 3.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELrnKTSDRLETVILDVTKTESIVTATQWVkEHVGNrglwgL 109
Cdd:cd05368    3 KVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKEL--ERGPGITTRVLDVTDKEQVAALAKEE-GRIDV-----L 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 110 VNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSLFGG--GYCISKYGVEAF 186
Cdd:cd05368   75 FNCAGF-VHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPkMLARKDGSIINMSSVASSIKGVPNrfVYSTTKAAVIGL 153

                        170       180
                 ....*....|....*....|.
gi 568967027 187 SDSLRRELSYFGVKVAIIEPG 207
Cdd:cd05368  154 TKSVAADFAQQGIRCNAICPG 174
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 27-217 3.35e-12

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 65.28  E-value: 3.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLaacltekgaeeLRNKTSDRLETV---ILDVTKTESIV------TAT--- 94
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVI-----------LLGRTEEKLEAVydeIEAAGGPQPAIipldllTATpqn 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  95 -----QWVKEHVGNrgLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGR 168
Cdd:PRK08945  79 yqqlaDTIEEQFGR--LDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPaASLVFTSSSVGR 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568967027 169 VS-LFGGGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSA 217
Cdd:PRK08945 157 QGrANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAMRASA 206
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 30-211 3.61e-12

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


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 65.16  E-value: 3.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVL------AACLtEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGn 103
Cdd:cd08940    3 KVALVTGSTSGIGLGIARALAAAGANIVlngfgdAAEI-EAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 rGLWGLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRV-SLFGGGYCISKY 181
Cdd:cd08940   81 -GVDILVNNAGIQH-VAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGwGRIINIASVHGLVaSANKSAYVAAKH 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 568967027 182 GVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:cd08940  159 GVVGLTKVVALETAGTGVTCNAICPGWVLT 188
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
30-222 3.64e-12

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 65.09  E-value: 3.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTE-KGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRGLWG 108
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTEnKELTKLAEQYNSNLTFHSLDLQDVHELETNFNEILSSIQEDNVSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 109 --LVNNAGISTPSGPNEWMKKQDFAHVLDVNLLgmIEVTLSMLPLVR----KARGRVVNVSSVMGRVSLFG-GGYCISKY 181
Cdd:PRK06924  82 ihLINNAGMVAPIKPIEKAESEELITNVHLNLL--APMILTSTFMKHtkdwKVDKRVINISSGAAKNPYFGwSAYCSSKA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568967027 182 GVEAFSDS--LRRELSYFGVKVAIIEPGFFLTGVTSSARLCSN 222
Cdd:PRK06924 160 GLDMFTQTvaTEQEEEEYPVKIVAFSPGVMDTNMQAQIRSSSK 202
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 30-207 4.40e-12

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: 65.18  E-value: 4.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACL----TEKGAEELRNKTSDRLETVI-LDVTKTESIVT-ATQWVKE---- 99
Cdd:cd09807    2 KTVIITGANTGIGKETARELARRGARVIMACRdmakCEEAAAEIRRDTLNHEVIVRhLDLASLKSIRAfAAEFLAEedrl 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 100 HVgnrglwgLVNNAGI-STPsgpnEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVM---GRVSL--- 171
Cdd:cd09807   82 DV-------LINNAGVmRCP----YSKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKsAPSRIVNVSSLAhkaGKINFddl 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568967027 172 -------FGGGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:cd09807  151 nseksynTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPG 193
PRK05866 PRK05866
SDR family oxidoreductase;
27-201 4.49e-12

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 65.53  E-value: 4.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDR---LETVILDVTKTESIVTATQWVKEHVGn 103
Cdd:PRK05866  38 LTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAggdAMAVPCDLSDLDAVDALVADVEKRIG- 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 rGLWGLVNNAGISTPSGPNEWMKK-QDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSS--VMGRVSLFGGGYCIS 179
Cdd:PRK05866 117 -GVDILINNAGRSIRRPLAESLDRwHDVERTMVLNYYAPLRLIRGLAPgMLERGDGHIINVATwgVLSEASPLFSVYNAS 195

                        170       180
                 ....*....|....*....|..
gi 568967027 180 KYGVEAFSDSLRRELSYFGVKV 201
Cdd:PRK05866 196 KAALSAVSRVIETEWGDRGVHS 217
PRK08251 PRK08251
SDR family oxidoreductase;
30-218 4.50e-12

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 64.96  E-value: 4.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGmRVLAAC------LTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGn 103
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKG-RDLALCarrtdrLEELKAELLARYPGIKVAVAALDVNDHDQVFEVFAEFRDELG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 rGLWGLVNNAGIST--PSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLplvRKA-RGRVVNVSSVMGRVSLFG--GGYCI 178
Cdd:PRK08251  81 -GLDRVIVNAGIGKgaRLGTGKFWANKATAETNFVAALAQCEAAMEIF---REQgSGHLVLISSVSAVRGLPGvkAAYAA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568967027 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSAR 218
Cdd:PRK08251 157 SKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNAKAK 196
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
30-207 7.66e-12

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 64.36  E-value: 7.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLE---TVILDVTKTESIVTATQWVKEHVGnrGL 106
Cdd:PRK08643   3 KVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGkaiAVKADVSDRDQVFAAVRQVVDTFG--DL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 107 WGLVNNAGIStPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR--GRVVNVSSVMGRV-----SLFGGgyciS 179
Cdd:PRK08643  81 NVVVNNAGVA-PTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGhgGKIINATSQAGVVgnpelAVYSS----T 155

                        170       180
                 ....*....|....*....|....*...
gi 568967027 180 KYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK08643 156 KFAVRGLTQTAARDLASEGITVNAYAPG 183
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 29-210 9.61e-12

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 63.90  E-value: 9.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  29 DKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTS-----DRLETVILDVTKTESIVTATQWVKEHVGN 103
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINaeygeGMAYGFGADATSEQSVLALSRGVDEIFGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 RGLwgLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMI----EVTLSMLPlvRKARGRVVNVSSVMGRV-SLFGGGYCI 178
Cdd:PRK12384  82 VDL--LVYNAGIAK-AAFITDFQLGDFDRSLQVNLVGYFlcarEFSRLMIR--DGIQGRIIQINSKSGKVgSKHNSGYSA 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568967027 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGFFL 210
Cdd:PRK12384 157 AKFGGVGLTQSLALDLAEYGITVHSLMLGNLL 188
PRK07069 PRK07069
short chain dehydrogenase; Validated
 33-213 1.27e-11

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 63.58  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  33 FITGCDSGFGTLLARQLDRRGMRVLaacLTEKGAEELRNKTSDRLET---------VILDVTKTESIVTATQWVKEHVGn 103
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVF---LTDINDAAGLDAFAAEINAahgegvafaAVQDVTDEAQWQALLAQAADAMG- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 rGLWGLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMG-RVSLFGGGYCISKY 181
Cdd:PRK07069  79 -GLSVLVNNAGVGS-FGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQpASIVNISSVAAfKAEPDYTAYNASKA 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568967027 182 GVEAFSDSL-----RRELsyfGVKVAIIEPGFFLTGV 213
Cdd:PRK07069 157 AVASLTKSIaldcaRRGL---DVRCNSIHPTFIRTGI 190
PRK07074 PRK07074
SDR family oxidoreductase;
29-207 1.33e-11

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 63.64  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  29 DKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSD-RLETVILDVTKTESIVTAtqwVKEHVGNRGLW 107
Cdd:PRK07074   2 KRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDaRFVPVACDLTDAASLAAA---LANAAAERGPV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 108 G-LVNNAGISTP-----SGPNEWmkKQDFAHVLDVNLLGMIEVTLSMLplvRKARGRVVNVSSVMGrVSLFGG-GYCISK 180
Cdd:PRK07074  79 DvLVANAGAARAaslhdTTPASW--RADNALNLEAAYLCVEAVLEGML---KRSRGAVVNIGSVNG-MAALGHpAYSAAK 152

                        170       180
                 ....*....|....*....|....*..
gi 568967027 181 YGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK07074 153 AGLIHYTKLLAVEYGRFGIRANAVAPG 179
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 27-217 1.51e-11

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: 63.24  E-value: 1.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDR---LETVILDVTKTESIVTATQWVKEHVGN 103
Cdd:cd05329    4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKgfkVEGSVCDVSSRSERQELMDTVASHFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 RgLWGLVNNAGISTPSGPNEWMKKqDFAHVLDVNLLGMIEVTLSMLPLV-RKARGRVVNVSSVMGRVSL-FGGGYCISKY 181
Cdd:cd05329   84 K-LNILVNNAGTNIRKEAKDYTEE-DYSLIMSTNFEAAYHLSRLAHPLLkASGNGNIVFISSVAGVIAVpSGAPYGATKG 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568967027 182 GVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSA 217
Cdd:cd05329  162 ALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPV 197
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 32-217 1.53e-11

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: 63.14  E-value: 1.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRGMRVL-----AACLTEKGAEELRNKTSdRLETVILDVTKTESIVTATQWVKEHVGnrGL 106
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVVinyrkSKDAAAEVAAEIEELGG-KAVVVRADVSQPQDVEEMFAAVKERFG--RL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 107 WGLVNNAGISTPSGPNEwMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSV-MGRVSLFGGGYCISKYGVE 184
Cdd:cd05359   78 DVLVSNAAAGAFRPLSE-LTPAHWDAKMNTNLKALVHCAQQAAKLMRERGgGRIVAISSLgSIRALPNYLAVGTAKAALE 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568967027 185 AFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSA 217
Cdd:cd05359  157 ALVRYLAVELGPRGIRVNAVSPGVIDTDALAHF 189
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 27-207 1.75e-11

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: 62.99  E-value: 1.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAAC----LTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVG 102
Cdd:cd05369    1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGrkpeVLEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLKEFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 NrgLWGLVNNAGISTPSgPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP--LVRKARGRVVNVSSVMGRvslFGGGYCI-- 178
Cdd:cd05369   81 K--IDILINNAAGNFLA-PAESLSPNGFKTVIDIDLNGTFNTTKAVGKrlIEAKHGGSILNISATYAY---TGSPFQVhs 154

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568967027 179 --SKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:cd05369  155 aaAKAGVDALTRSLAVEWGPYGIRVNAIAPG 185
PRK07831 PRK07831
SDR family oxidoreductase;
27-239 2.42e-11

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 62.74  E-value: 2.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGC-DSGFGTLLARQLDRRGMRVLAACLTEK----GAEELRNKT-SDRLETVILDVTKTESIVTATQWVKEH 100
Cdd:PRK07831  15 LAGKVVLVTAAaGTGIGSATARRALEEGARVVISDIHERrlgeTADELAAELgLGRVEAVVCDVTSEAQVDALIDAAVER 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 101 VGnrGLWGLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP--LVRKARGRVVNVSSVMG-RVSLFGGGYC 177
Cdd:PRK07831  95 LG--RLDVLVNNAGLGG-QTPVVDMTDDEWSRVLDVTLTGTFRATRAALRymRARGHGGVIVNNASVLGwRAQHGQAHYA 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568967027 178 ISKYGVEAFSDSLRRELSYFGVKVAIIEPGF----FLTGVTSSARLcsntqmlwDQTSSeiREIYG 239
Cdd:PRK07831 172 AAKAGVMALTRCSALEAAEYGVRINAVAPSIamhpFLAKVTSAELL--------DELAA--REAFG 227
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-218 3.02e-11

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 62.45  E-value: 3.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAE--ELRNKTSDRLETVILDVTKTESivtATQWVKEHVGNR 104
Cdd:PRK06935  13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWDEtrRLIEKEGRKVTFVQVDLTKPES---AEKVVKEALEEF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 105 G-LWGLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGrvslFGGG-----YC 177
Cdd:PRK06935  90 GkIDILVNNAGT-IRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKvMAKQGSGKIINIASMLS----FQGGkfvpaYT 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568967027 178 ISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSAR 218
Cdd:PRK06935 165 ASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAPIR 205
PRK06124 PRK06124
SDR family oxidoreductase;
27-211 4.36e-11

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 62.04  E-value: 4.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLaacLTEKGAEELRNKTSD------RLETVILDVTKTESIVTATQWVKEH 100
Cdd:PRK06124   9 LAGQVALVTGSARGLGFEIARALAGAGAHVL---VNGRNAATLEAAVAAlraaggAAEALAFDIADEEAVAAAFARIDAE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 101 VGnrGLWGLVNNAGISTPSGPNEwMKKQDFAHVLDVNLLGMIevTLSMLPLVRKAR---GRVVNVSSVMGRVSLFGGG-Y 176
Cdd:PRK06124  86 HG--RLDILVNNVGARDRRPLAE-LDDAAIRALLETDLVAPI--LLSRLAAQRMKRqgyGRIIAITSIAGQVARAGDAvY 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568967027 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK06124 161 PAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFAT 195
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 27-218 4.74e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 62.00  E-value: 4.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRV----LAACLTEKGAEELRNKTSDrLETVILDVTKTESIVTATQWVKEHVG 102
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIvfndINQELVDKGLAAYRELGIE-AHGYVCDVTDEDGVQAMVSQIEKEVG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 NRGLwgLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVM---GRVSLfgGGYCI 178
Cdd:PRK07097  87 VIDI--LVNNAGI-IKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPsMIKKGHGKIINICSMMselGRETV--SAYAA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568967027 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSAR 218
Cdd:PRK07097 162 AKGGLKMLTKNIASEYGEANIQCNGIGPGYIATPQTAPLR 201
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 28-226 5.71e-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: 61.58  E-value: 5.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  28 QDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAE----ELRNKTSDRLETVILDVTKTESIvtATQWVKEHVGN 103
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEqlkeELTNLYKNRVIALELDITSKESI--KELIESYLEKF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 RGLWGLVNNAGIS--TPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVMGRVS----LFGGG- 175
Cdd:cd08930   79 GRIDILINNAYPSpkVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKqGKGSIINIASIYGVIApdfrIYENTq 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967027 176 ------YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSS-----ARLCSNTQML 226
Cdd:cd08930  159 myspveYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNNQPSEflekyTKKCPLKRML 220
PRK06172 PRK06172
SDR family oxidoreductase;
27-211 5.90e-11

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 61.69  E-value: 5.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEE----LRNKTSDRLeTVILDVTKTESIvtaTQWVKEHVG 102
Cdd:PRK06172   5 FSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEEtvalIREAGGEAL-FVACDVTRDAEV---KALVEQTIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 NRG-LWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGmieVTLSM---LP-LVRKARGRVVNVSSVMGRVSLFG-GGY 176
Cdd:PRK06172  81 AYGrLDYAFNNAGIEIEQGRLAEGSEAEFDAIMGVNVKG---VWLCMkyqIPlMLAQGGGAIVNTASVAGLGAAPKmSIY 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568967027 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK06172 158 AASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDT 192
PRK07023 PRK07023
SDR family oxidoreductase;
34-218 9.73e-11

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 60.80  E-value: 9.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  34 ITGCDSGFGTLLARQLDRRGMRVLaaCLTEKGAEELRNKTSDRLETVILDVTKTESivtATQWVKEHVGNRGLWG----- 108
Cdd:PRK07023   6 VTGHSRGLGAALAEQLLQPGIAVL--GVARSRHPSLAAAAGERLAEVELDLSDAAA---AAAWLAGDLLAAFVDGasrvl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 109 LVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVMGRVSLFG-GGYCISKYGVEAF 186
Cdd:PRK07023  81 LINNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDaAERRILHISSGAARNAYAGwSVYCATKAALDHH 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568967027 187 SDSLRRELSYfGVKVAIIEPGFFLTGVTSSAR 218
Cdd:PRK07023 161 ARAVALDANR-ALRIVSLAPGVVDTGMQATIR 191
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 109-208 1.24e-10

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: 59.84  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 109 LVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSL-FGGGYCISKYGVEAF 186
Cdd:cd02266   35 VVHNAAILD-DGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRlGRFILISSVAGLFGApGLGGYAASKAALDGL 113

                         90       100
                 ....*....|....*....|..
gi 568967027 187 SDSLRRELSYFGVKVAIIEPGF 208
Cdd:cd02266  114 AQQWASEGWGNGLPATAVACGT 135
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
27-206 1.73e-10

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 61.79  E-value: 1.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACL----TEKGAEELRNKtsDRLETVILDVTKTESIVTATQWVKEHVG 102
Cdd:PRK08324 420 LAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLdeeaAEAAAAELGGP--DRALGVACDVTDEAAVQAAFEEAALAFG 497

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 nrGLWGLVNNAGIStPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKA--RGRVVNVSSVMGRVSLFG-GGYCIS 179
Cdd:PRK08324 498 --GVDIVVSNAGIA-ISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQglGGSIVFIASKNAVNPGPNfGAYGAA 574

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568967027 180 KygveAFSDSLRR----ELSYFGVKVAIIEP 206
Cdd:PRK08324 575 K----AAELHLVRqlalELGPDGIRVNGVNP 601
PLN02253 PLN02253
xanthoxin dehydrogenase
 27-206 2.25e-10

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 60.22  E-value: 2.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVIL--DVTKTESIVTATQWVKEHVGNR 104
Cdd:PLN02253  16 LLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNVCFFhcDVTVEDDVSRAVDFTVDKFGTL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 105 GLwgLVNNAGISTPSGPN-EWMKKQDFAHVLDVNL----LGMIEVTLSMLPLvrkARGRVVNVSSVMGRVSLFG-GGYCI 178
Cdd:PLN02253  96 DI--MVNNAGLTGPPCPDiRNVELSEFEKVFDVNVkgvfLGMKHAARIMIPL---KKGSIVSLCSVASAIGGLGpHAYTG 170

                        170       180
                 ....*....|....*....|....*...
gi 568967027 179 SKYGVEAFSDSLRRELSYFGVKVAIIEP 206
Cdd:PLN02253 171 SKHAVLGLTRSVAAELGKHGIRVNCVSP 198
PRK06138 PRK06138
SDR family oxidoreductase;
26-207 3.14e-10

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 59.39  E-value: 3.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  26 HLQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSD--RLETVILDVTKTESIVTATQWVkehvgn 103
Cdd:PRK06138   2 RLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAggRAFARQGDVGSAEAVEALVDFV------ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 RGLWG----LVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLFG-GGYC 177
Cdd:PRK06138  76 AARWGrldvLVNNAGFGC-GGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGgGSIVNTASQLALAGGRGrAAYV 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 568967027 178 ISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK06138 155 ASKGAIASLTRAMALDHATDGIRVNAVAPG 184
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 30-217 3.71e-10

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: 59.39  E-value: 3.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACL-TEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRGLwg 108
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYrSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDT-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 109 LVNNAGISTPSGPN--------EWmkkQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSvmgrvSLFGGG---- 175
Cdd:cd05349   79 IVNNALIDFPFDPDqrktfdtiDW---EDYQQQLEGAVKGALNLLQAVLPDFKERGsGRVINIGT-----NLFQNPvvpy 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568967027 176 --YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSA 217
Cdd:cd05349  151 hdYTTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKVTDASAA 194
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 27-207 3.98e-10

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 59.25  E-value: 3.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGnrGL 106
Cdd:PRK08265   4 LAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFG--RV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 107 WGLVNNA------GIStpSGPNEWMKkqdfahVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRVSLFGGG-YCIS 179
Cdd:PRK08265  82 DILVNLActylddGLA--SSRADWLA------ALDVNLVSAAMLAQAAHPHLARGGGAIVNFTSISAKFAQTGRWlYPAS 153

                        170       180
                 ....*....|....*....|....*...
gi 568967027 180 KYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK08265 154 KAAIRQLTRSMAMDLAPDGIRVNSVSPG 181
PRK06398 PRK06398
aldose dehydrogenase; Validated
 27-183 5.57e-10

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 59.08  E-value: 5.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKgaeelRNKTSDRLEtviLDVTKTESIVTATQWVKEHVGNRGL 106
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEP-----SYNDVDYFK---VDVSNKEQVIKGIDYVISKYGRIDI 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568967027 107 wgLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGR-VSLFGGGYCISKYGV 183
Cdd:PRK06398  76 --LVNNAGIES-YGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDkGVIINIASVQSFaVTRNAAAYVTSKHAV 151
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
32-209 5.62e-10

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 59.22  E-value: 5.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCdSGF-GTLLARQLDRRGMRVLAACLTEKGAEELRNktSDRLETVILDVTKTESIVTATQWVkEHVgnrglwglV 110
Cdd:COG0451    2 ILVTGG-AGFiGSHLARRLLARGHEVVGLDRSPPGAANLAA--LPGVEFVRGDLRDPEALAAALAGV-DAV--------V 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 111 NNAGISTPSGpnewmkkQDFAHVLDVNLLGmievTLSMLPLVRKAR-GRVVNVSS--VMGRVSLF---------GGGYCI 178
Cdd:COG0451   70 HLAAPAGVGE-------EDPDETLEVNVEG----TLNLLEAARAAGvKRFVYASSssVYGDGEGPidedtplrpVSPYGA 138

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568967027 179 SKYGVEAFSDSLRRElsyFGVKVAIIEPGFF 209
Cdd:COG0451  139 SKLAAELLARAYARR---YGLPVTILRPGNV 166
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 27-214 5.69e-10

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


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 58.65  E-value: 5.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVL------AACltEKGAEELrnKTSDRLETVILDVTKTESIVTATQWVKEh 100
Cdd:cd08942    4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIisarkaEAC--ADAAEEL--SAYGECIAIPADLSSEEGIEALVARVAE- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 101 VGNRgLWGLVNNAGiSTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-----GRVVNVSSVMGRV--SLFG 173
Cdd:cd08942   79 RSDR-LDVLVNNAG-ATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAAtaenpARVINIGSIAGIVvsGLEN 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568967027 174 GGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVT 214
Cdd:cd08942  157 YSYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMT 197
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 30-249 6.35e-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: 58.56  E-value: 6.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACL----TEKGAEELRNKtsDRLETVILDVTKTESIVTATQWVKEHVGnrG 105
Cdd:cd08943    2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIdpeiAEKVAEAAQGG--PRALGVQCDVTSEAQVQSAFEQAVLEFG--G 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 106 LWGLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR--GRVVNVSSvmgRVSLFGG----GYCIS 179
Cdd:cd08943   78 LDIVVSNAGIAT-SSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGigGNIVFNAS---KNAVAPGpnaaAYSAA 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568967027 180 KygveAFSDSLRR----ELSYFGVKVAIIEP-GFFLTGVTssarlcsnTQMLWDQTSSEIREIYGEKYLA-SYLKR 249
Cdd:cd08943  154 K----AAEAHLARclalEGGEDGIRVNTVNPdAVFRGSKI--------WEGVWRAARAKAYGLLEEEYRTrNLLKR 217
PRK06953 PRK06953
SDR family oxidoreductase;
30-185 6.91e-10

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 58.16  E-value: 6.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSdrlETVILDVTKTESiVTATQWvkeHVGNRGLWGL 109
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQALGA---EALALDVADPAS-VAGLAW---KLDGEALDAA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 110 VNNAGISTP-SGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRV----SLFGGGYCISKYGVE 184
Cdd:PRK06953  75 VYVAGVYGPrTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSRMGSIgdatGTTGWLYRASKAALN 154


                 .
gi 568967027 185 A 185
Cdd:PRK06953 155 D 155
PRK12746 PRK12746
SDR family oxidoreductase;
24-215 1.43e-09

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 57.74  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  24 VSHLQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGA--EELRNKTSDRLETVIL--DVTKTESIVTATQWVKE 99
Cdd:PRK12746   1 MKNLDGKVALVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAadETIREIESNGGKAFLIeaDLNSIDGVKKLVEQLKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 100 H----VGNRGLWGLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRkARGRVVNVSSVMGRVSLFGG- 174
Cdd:PRK12746  81 ElqirVGTSEIDILVNNAGIGT-QGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLR-AEGRVINISSAEVRLGFTGSi 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568967027 175 GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTS 215
Cdd:PRK12746 159 AYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINA 199
PRK12743 PRK12743
SDR family oxidoreductase;
28-207 1.65e-09

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 57.35  E-value: 1.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  28 QDKYVFITGCDSGFGTLLARQLDRRGMRVlaaCLT----EKGA----EELRnKTSDRLETVILDVTKTESIVTATQWVKE 99
Cdd:PRK12743   1 MAQVAIVTASDSGIGKACALLLAQQGFDI---GITwhsdEEGAketaEEVR-SHGVRAEIRQLDLSDLPEGAQALDKLIQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 100 HVGnrGLWGLVNNAGistpSGPNEWMKKQDFAH---VLDVNLLGmievtlSMLPLVRKAR--------GRVVNVSSVMGR 168
Cdd:PRK12743  77 RLG--RIDVLVNNAG----AMTKAPFLDMDFDEwrkIFTVDVDG------AFLCSQIAARhmvkqgqgGRIINITSVHEH 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568967027 169 VSLFGGG-YCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK12743 145 TPLPGASaYTAAKHALGGLTKAMALELVEHGILVNAVAPG 184
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 32-167 2.08e-09

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 57.12  E-value: 2.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRGMRVLAACLTEkgAEelrnktsdrletVILDVTKTESIVTATQWVKEHVGnRGLWGLVN 111
Cdd:cd05328    2 IVITGAASGIGAATAELLEDAGHTVIGIDLRE--AD------------VIADLSTPEGRAAAIADVLARCS-GVLDGLVN 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568967027 112 NAGISTPSGPNEwmkkqdfahVLDVNLLGMIEVTLSMLPLVRKARG-RVVNVSSVMG 167
Cdd:cd05328   67 CAGVGGTTVAGL---------VLKVNYFGLRALMEALLPRLRKGHGpAAVVVSSIAG 114
PRK06101 PRK06101
SDR family oxidoreductase;
32-236 2.35e-09

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 56.80  E-value: 2.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELrNKTSDRLETVILDVTKTESIVTATQwvkehvgnrglwglvn 111
Cdd:PRK06101   4 VLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDEL-HTQSANIFTLAFDVTDHPGTKAALS---------------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 112 nagiSTPSGPNEW--------------MKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARgRVVNVSSVMGRVSL-FGGGY 176
Cdd:PRK06101  67 ----QLPFIPELWifnagdceymddgkVDATLMARVFNVNVLGVANCIEGIQPHLSCGH-RVVIVGSIASELALpRAEAY 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLCSNTQMLWDQTSSEIRE 236
Cdd:PRK06101 142 GASKAAVAYFARTLQLDLRPKGIEVVTVFPGFVATPLTDKNTFAMPMIITVEQASQEIRA 201
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 27-207 2.49e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 57.05  E-value: 2.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLetVILDVTKTESIVTATQWVKEHVGNRGL 106
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGGLF--VPTDVTDEDAVNALFDTAAETYGSVDI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 107 wgLVNNAGISTP-------SGPNEWMKkqdfahVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSS---VMG----RVSl 171
Cdd:PRK06057  83 --AFNNAGISPPeddsilnTGLDAWQR------VQDVNLTSVYLCCKAALPhMVRQGKGSIINTASfvaVMGsatsQIS- 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568967027 172 fgggYCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK06057 154 ----YTASKGGVLAMSRELGVQFARQGIRVNALCPG 185
PRK07577 PRK07577
SDR family oxidoreductase;
27-207 1.00e-08

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 54.73  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACltekgaeelRNKTSD---RLETVIL-DVTKTESIVTATqwvkehVG 102
Cdd:PRK07577   1 MSSRTVLVTGATKGIGLALSLRLANLGHQVIGIA---------RSAIDDfpgELFACDLaDIEQTAATLAQI------NE 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 NRGLWGLVNNAGISTPsgpnEWMKKQDFAH---VLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSvmgrVSLFGG---- 174
Cdd:PRK07577  66 IHPVDAIVNNVGIALP----QPLGKIDLAAlqdVYDLNVRAAVQVTQAFLEGMKLREqGRIVNICS----RAIFGAldrt 137

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568967027 175 GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK07577 138 SYSAAKSALVGCTRTWALELAEYGITVNAVAPG 170
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 27-196 1.49e-08

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


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 54.67  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTAtqwVKEHVGNRG- 105
Cdd:cd05348    2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERA---VARCVERFGk 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 106 LWGLVNNAGI-----STPSGPNEWMKKQdFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRVSlfGGG---YC 177
Cdd:cd05348   79 LDCFIGNAGIwdystSLVDIPEEKLDEA-FDELFHINVKGYILGAKAALPALYATEGSVIFTVSNAGFYP--GGGgplYT 155

                        170
                 ....*....|....*....
gi 568967027 178 ISKYGVEAfsdsLRRELSY 196
Cdd:cd05348  156 ASKHAVVG----LVKQLAY 170
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 27-207 1.95e-08

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: 54.16  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGnrGL 106
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWG--SI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 107 WGLVNNAGISTPSgPNEWMKKQDFAHVLDVNLLGMievtLSMLPLVRKAR------GRVVNVSSVMGRV-SLFGGGYCIS 179
Cdd:cd05363   79 DILVNNAALFDLA-PIVDITRESYDRLFAINVSGT----LFMMQAVARAMiaqgrgGKIINMASQAGRRgEALVGVYCAT 153

                        170       180
                 ....*....|....*....|....*...
gi 568967027 180 KYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:cd05363  154 KAAVISLTQSAGLNLIRHGINVNAIAPG 181
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 30-215 2.03e-08

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 54.70  E-value: 2.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFG-----TLLARQLDRRGMRVLAACLTEKGAEELRNKTSD-------RLETVILDVTKTESIVTATQWV 97
Cdd:cd08941    2 KVVLVTGANSGLGlaiceRLLAEDDENPELTLILACRNLQRAEAACRALLAshpdarvVFDYVLVDLSNMVSVFAAAKEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  98 KEHVgnRGLWGLVNNAGIstpsGPNE---W-------------------MKKQ--------------DFAHVLDVNLLGM 141
Cdd:cd08941   82 KKRY--PRLDYLYLNAGI----MPNPgidWigaikevltnplfavtnptYKIQaegllsqgdkatedGLGEVFQTNVFGH 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 142 IEVTLSMLPLVRKAR--GRVVNVSSVMGRVSLFG----------GGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFF 209
Cdd:cd08941  156 YYLIRELEPLLCRSDggSQIIWTSSLNASPKYFSlediqhlkgpAPYSSSKYLVDLLSLALNRKFNKLGVYSYVVHPGIC 235


                 ....*.
gi 568967027 210 LTGVTS 215
Cdd:cd08941  236 TTNLTY 241
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 34-217 2.25e-08

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: 54.01  E-value: 2.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  34 ITGCDSGFGTLLARQLDRRGMRVL------AACLTEKGAEELR-NKTSDRLETVILDVTKTESIVTATQwvkEHVGnrGL 106
Cdd:cd05337    6 VTGASRGIGRAIATELAARGFDIAindlpdDDQATEVVAEVLAaGRRAIYFQADIGELSDHEALLDQAW---EDFG--RL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 107 WGLVNNAGISTPsgpnewmKKQD--------FAHVLDVNLLGMI----EVTLSML--PLVRKA-RGRVVNVSSV-MGRVS 170
Cdd:cd05337   81 DCLVNNAGIAVR-------PRGDlldltedsFDRLIAINLRGPFfltqAVARRMVeqPDRFDGpHRSIIFVTSInAYLVS 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568967027 171 LFGGGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSA 217
Cdd:cd05337  154 PNRGEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPV 200
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 27-258 2.97e-08

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


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 53.69  E-value: 2.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGaEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRG- 105
Cdd:cd08937    2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELV-HEVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 106 LWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRvSLFGGGYCISKYGVE 184
Cdd:cd08937   81 VDVLINNVGGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPhMLERQQGVIVNVSSIATR-GIYRIPYSAAKGGVN 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568967027 185 AFSDSLRRELSYFGVKVAIIEPGffltGVTSSAR-LCSNTQMLWDQTSSEIREIYGEKYLASYLKRLNKLDKRCN 258
Cdd:cd08937  160 ALTASLAFEHARDGIRVNAVAPG----GTEAPPRkIPRNAAPMSEQEKVWYQRIVDQTLDSSLMGRYGTIDEQVR 230
PRK06500 PRK06500
SDR family oxidoreductase;
25-207 3.02e-08

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 53.81  E-value: 3.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  25 SHLQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGnr 104
Cdd:PRK06500   2 SRLQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAAQKALAQALAEAFG-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 105 GLWGLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNvSSVMGRVSLFGGG-YCISKYGV 183
Cdd:PRK06500  80 RLDAVFINAGVAK-FAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPASIVLN-GSINAHIGMPNSSvYAASKAAL 157

                        170       180
                 ....*....|....*....|....
gi 568967027 184 EAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK06500 158 LSLAKTLSGELLPRGIRVNAVSPG 181
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 32-212 3.75e-08

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


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 52.91  E-value: 3.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRGMRVLaacLTEKGAEELRNKTSDRLE-TVILDVTkTESIVTATQwvkEHVGNRGLWglV 110
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLL---LSGRDAGALAGLAAEVGAlARPADVA-AELEVWALA---QELGPLDLL--V 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 111 NNAGISTPSgPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVrKARGRVVNVSSVMGRVSLFG-GGYCISKYGVEAFSDS 189
Cdd:cd11730   72 YAAGAILGK-PLARTKPAAWRRILDANLTGAALVLKHALALL-AAGARLVFLGAYPELVMLPGlSAYAAAKAALEAYVEV 149

                        170       180
                 ....*....|....*....|...
gi 568967027 190 LRRELSyfGVKVAIIEPGFFLTG 212
Cdd:cd11730  150 ARKEVR--GLRLTLVRPPAVDTG 170
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-217 5.06e-08

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 53.17  E-value: 5.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACL-TEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGnRG 105
Cdd:PRK08642   3 ISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHqSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEHFG-KP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 106 LWGLVNNA-------GISTPSGPN-EWmkkQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSvmgrvSLFGG-- 174
Cdd:PRK08642  82 ITTVVNNAladfsfdGDARKKADDiTW---EDFQQQLEGSVKGALNTIQAALPGMREQGfGRIINIGT-----NLFQNpv 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568967027 175 ----GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSA 217
Cdd:PRK08642 154 vpyhDYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTTDASAA 200
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 27-207 5.35e-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: 52.71  E-value: 5.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLteKGAEELRNKTSDRLETVILDVTK--------TESIVTATQWVK 98
Cdd:cd05353    3 FDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDL--GGDRKGSGKSSSAADKVVDEIKAaggkavanYDSVEDGEKIVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  99 EHVGNRG-LWGLVNNAGI----STPSgpnewMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLF 172
Cdd:cd05353   81 TAIDAFGrVDILVNNAGIlrdrSFAK-----MSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKfGRIINTSSAAGLYGNF 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568967027 173 G-GGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:cd05353  156 GqANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA 191
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-218 7.29e-08

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 52.57  E-value: 7.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTE-KGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRG 105
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEpTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEFGHID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 106 LwgLVNNAGISTPSGPNEWmKKQDFAHVLDVNllgmIEVTLSMLPLVRKA------RGRVVNVSSVMGrvslFGGG---- 175
Cdd:PRK08993  88 I--LVNNAGLIRREDAIEF-SEKDWDDVMNLN----IKSVFFMSQAAAKHfiaqgnGGKIINIASMLS----FQGGirvp 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568967027 176 -YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSAR 218
Cdd:PRK08993 157 sYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLR 200
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 25-184 7.46e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 52.70  E-value: 7.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  25 SHLQDKYVFITGCDSGFGTLLARQLDRRGMRVLAAC--LTEKG---AEELRnKTSDRLETVILDVTKTESIVTATQWVKE 99
Cdd:PRK06198   2 GRLDGKVALVTGGTQGLGAAIARAFAERGAAGLVICgrNAEKGeaqAAELE-ALGAKAVFVQADLSDVEDCRRVVAAADE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 100 HVGnrGLWGLVNNAGIST-----PSGPnewmkkQDFAHVLDVNLLG----MIEVTLSMLPlvRKARGRVVNVSSV--MGR 168
Cdd:PRK06198  81 AFG--RLDALVNAAGLTDrgtilDTSP------ELFDRHFAVNVRApfflMQEAIKLMRR--RKAEGTIVNIGSMsaHGG 150

                        170
                 ....*....|....*.
gi 568967027 169 VSlFGGGYCISKYGVE 184
Cdd:PRK06198 151 QP-FLAAYCASKGALA 165
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 33-215 1.31e-07

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 51.89  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  33 FITGCDSGFGTLLARQLDRRGMRVLAACLTEkgAEELRnKTSDRLET-------VILDVTKTESIVTATQWVKEHVGnrG 105
Cdd:PRK12745   6 LVTGGRRGIGLGIARALAAAGFDLAINDRPD--DEELA-ATQQELRAlgvevifFPADVADLSAHEAMLDAAQAAWG--R 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 106 LWGLVNNAGISTPS-GPNEWMKKQDFAHVLDVNLLGMIEVT-------LSMLPLVRKARGRVVNVSSV-MGRVSLFGGGY 176
Cdd:PRK12745  81 IDCLVNNAGVGVKVrGDLLDLTPESFDRVLAINLRGPFFLTqavakrmLAQPEPEELPHRSIVFVSSVnAIMVSPNRGEY 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568967027 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTS 215
Cdd:PRK12745 161 CISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTA 199
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 28-210 1.77e-07

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: 51.31  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  28 QDKYVFITGCDSGFGTLLARQLDRRGMRVLAACL----TEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGN 103
Cdd:cd05322    1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADInsenAEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 RGLwgLVNNAGISTpSGPNEWMKKQDFAHVLDVNLLG--MIEVTLSMLPLVRKARGRVVNVSSVMGRV-SLFGGGYCISK 180
Cdd:cd05322   81 VDL--LVYSAGIAK-SAKITDFELGDFDRSLQVNLVGyfLCAREFSKLMIRDGIQGRIIQINSKSGKVgSKHNSGYSAAK 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 568967027 181 YGVEAFSDSLRRELSYFGVKVAIIEPGFFL 210
Cdd:cd05322  158 FGGVGLTQSLALDLAEHGITVNSLMLGNLL 187
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 27-196 2.18e-07

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 51.11  E-value: 2.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTAtqwVKEHVGNRG- 105
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRA---VDQTVDAFGk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 106 LWGLVNNAGISTPSGPNEWMKKQD----FAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRVSlfGGG---YCI 178
Cdd:PRK06200  81 LDCFVGNAGIWDYNTSLVDIPAETldtaFDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLSNSSFYP--GGGgplYTA 158

                        170
                 ....*....|....*...
gi 568967027 179 SKYGVEAfsdsLRRELSY 196
Cdd:PRK06200 159 SKHAVVG----LVRQLAY 172
PRK06123 PRK06123
SDR family oxidoreductase;
29-216 4.52e-07

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 50.16  E-value: 4.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  29 DKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEK-GAEELRNKTSDRLETVIL---DVTKTESIVTATQWVKEHVGNr 104
Cdd:PRK06123   2 RKVMIITGASRGIGAATALLAAERGYAVCLNYLRNRdAAEAVVQAIRRQGGEALAvaaDVADEADVLRLFEAVDRELGR- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 105 gLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMI----EVTLSMLPLVRKARGRVVNVSSVMGRVSLFGG--GYCI 178
Cdd:PRK06123  81 -LDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSFlcarEAVKRMSTRHGGRGGAIVNVSSMAARLGSPGEyiDYAA 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568967027 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSS 216
Cdd:PRK06123 160 SKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHAS 197
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-214 4.58e-07

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 50.99  E-value: 4.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLaaCLTEKGAEELRNKTSDRL--ETVILDVTKTESIVTATQWVKEHVGnr 104
Cdd:PRK08261 208 LAGKVALVTGAARGIGAAIAEVLARDGAHVV--CLDVPAAGEALAAVANRVggTALALDITAPDAPARIAEHLAERHG-- 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 105 GLWGLVNNAGIS--------TPSgpnEWmkkqdfAHVLDVNLLGMIEVTLSML-PLVRKARGRVVNVSSVMGRVSLFG-G 174
Cdd:PRK08261 284 GLDIVVHNAGITrdktlanmDEA---RW------DSVLAVNLLAPLRITEALLaAGALGDGGRIVGVSSISGIAGNRGqT 354

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568967027 175 GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVT 214
Cdd:PRK08261 355 NYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQMT 394
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 30-211 4.82e-07

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


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 49.89  E-value: 4.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGnrGLWGL 109
Cdd:cd09761    2 KVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLG--RIDVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 110 VNNAGISTPsGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRVSLFGG-GYCISKYGVEAFSD 188
Cdd:cd09761   80 VNNAARGSK-GILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAFQSEPDSeAYAASKGGLVALTH 158

                        170       180
                 ....*....|....*....|...
gi 568967027 189 SLRRELSYFgVKVAIIEPGFFLT 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 ...
 32-217 4.86e-07

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


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 49.88  E-value: 4.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAeelrNKTSDRLET-------VILDVTKTESIVtatQWVKEHVGNR 104
Cdd:cd05365    2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGA----EAVAAAIQQaggqaigLECNVTSEQDLE---AVVKATVSQF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 105 G-LWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSVMGRVSLFG-GGYCISKY 181
Cdd:cd05365   75 GgITILVNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGgGAILNISSMSSENKNVRiAAYGSSKA 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568967027 182 GVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSA 217
Cdd:cd05365  155 AVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDALASV 190
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 27-207 5.41e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 50.03  E-value: 5.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKG-AEElrnkTSDRLE-------TVILDVTKTESIVTATQWVK 98
Cdd:PRK06701  44 LKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEdANE----TKQRVEkegvkclLIPGDVSDEAFCKDAVEETV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  99 EHVGnrGLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVrKARGRVVNVSSVMGrvsLFGGG--- 175
Cdd:PRK06701 120 RELG--RLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL-KQGSAIINTGSITG---YEGNEtli 193

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568967027 176 -YCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK06701 194 dYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPG 226
PRK08278 PRK08278
SDR family oxidoreductase;
27-201 5.63e-07

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 49.90  E-value: 5.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMR-VLAACLTEK----------GAEELRNKTSDRLeTVILDVTKTESIVTATQ 95
Cdd:PRK08278   4 LSGKTLFITGASRGIGLAIALRAARDGANiVIAAKTAEPhpklpgtihtAAEEIEAAGGQAL-PLVGDVRDEDQVAAAVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  96 WVKEHVGnrGLWGLVNNAG-ISTPSGPNEWMKKQDFAHvlDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSS--VMGRvSL 171
Cdd:PRK08278  83 KAVERFG--GIDICVNNASaINLTGTEDTPMKRFDLMQ--QINVRGTFLVSQACLPHLKKSEnPHILTLSPplNLDP-KW 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568967027 172 FGG--GYCISKYGVEAFSDSLRRELSYFGVKV 201
Cdd:PRK08278 158 FAPhtAYTMAKYGMSLCTLGLAEEFRDDGIAV 189
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 28-254 6.08e-07

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 49.94  E-value: 6.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  28 QDKYVFITGCDSGFGTLLARQLDRRGMRVLA---ACLTEKGAEELRNKTSDRLeTVILDVTKTESIVTATQWVKEHVGnr 104
Cdd:PRK12823   7 AGKVVVVTGAAQGIGRGVALRAAAEGARVVLvdrSELVHEVAAELRAAGGEAL-ALTADLETYAGAQAAMAAAVEAFG-- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 105 GLWGLVNNAGISTpsgpneWMKKqdFAHVLDVNLLGmiEVTLSMLP-----------LVRKARGRVVNVSSVMGRvSLFG 173
Cdd:PRK12823  84 RIDVLINNVGGTI------WAKP--FEEYEEEQIEA--EIRRSLFPtlwccravlphMLAQGGGAIVNVSSIATR-GINR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 174 GGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGffltGVTSSARLCS-NTQMLWDQTSSEIREIYGEKYLASYLKRLNK 252
Cdd:PRK12823 153 VPYSAAKGGVNALTASLAFEYAEHGIRVNAVAPG----GTEAPPRRVPrNAAPQSEQEKAWYQQIVDQTLDSSLMKRYGT 228


                 ..
gi 568967027 253 LD 254
Cdd:PRK12823 229 ID 230
PRK07814 PRK07814
SDR family oxidoreductase;
27-211 6.70e-07

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 49.78  E-value: 6.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSD---RLETVILDVTKTESIVTATQWVKEHVGN 103
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAagrRAHVVAADLAHPEATAGLAGQAVEAFGR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 RGLwgLVNNAGISTPSgPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRK--ARGRVVNVSSVMGRVSLFG-GGYCISK 180
Cdd:PRK07814  88 LDI--VVNNVGGTMPN-PLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEhsGGGSVINISSTMGRLAGRGfAAYGTAK 164

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568967027 181 YGVEAFSDSLRRELSYfGVKVAIIEPGFFLT 211
Cdd:PRK07814 165 AALAHYTRLAALDLCP-RIRVNAIAPGSILT 194
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-218 6.89e-07

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 49.52  E-value: 6.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAacLTEKGAEELRNK---TSDRLETVILDVTKTESIVTATQWVKEHVGN 103
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVG--VGVAEAPETQAQveaLGRKFHFITADLIQQKDIDSIVSQAVEVMGH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 104 RGLwgLVNNAGISTPSGPNEWmKKQDFAHVLDVNLLGMIEVTLSMLPLVRKAR--GRVVNVSSVMGrvslFGGG-----Y 176
Cdd:PRK12481  84 IDI--LINNAGIIRRQDLLEF-GNKDWDDVININQKTVFFLSQAVAKQFVKQGngGKIINIASMLS----FQGGirvpsY 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568967027 177 CISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSAR 218
Cdd:PRK12481 157 TASKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAALR 198
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 27-207 7.55e-07

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


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 49.60  E-value: 7.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKgaEELRNKTSDRLET-----VIL--DVTKTESivtATQWVKE 99
Cdd:cd05355   24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEE--EDDAEETKKLIEEegrkcLLIpgDLGDESF---CRDLVKE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 100 HVGNRG-LWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKArGRVVNVSSVM---GRVSLFggG 175
Cdd:cd05355   99 VVKEFGkLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKKG-SSIINTTSVTaykGSPHLL--D 175

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568967027 176 YCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:cd05355  176 YAATKGAIVAFTRGLSLQLAEKGIRVNAVAPG 207
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 27-211 7.56e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 49.80  E-value: 7.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRV---------LAACLTEKGAeeLRNKTSDRLETVilDVTKTESIVTATQWV 97
Cdd:PRK05875   5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVmivgrnpdkLAAAAEEIEA--LKGAGAVRYEPA--DVTDEDQVARAVDAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  98 KEHVGnrGLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLG-MIEVTLSMLPLVRKARGRVVNVSSVMG-RVSLFGGG 175
Cdd:PRK05875  81 TAWHG--RLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGtMYVLKHAARELVRGGGGSFVGISSIAAsNTHRWFGA 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568967027 176 YCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK05875 159 YGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRT 194
PRK07102 PRK07102
SDR family oxidoreductase;
30-229 1.69e-06

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 48.38  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRV-LAACLTEK---GAEELRNKTSDRLETVILDVTKTESIVTATQwvkehvgnrG 105
Cdd:PRK07102   2 KKILIIGATSDIARACARRYAAAGARLyLAARDVERlerLADDLRARGAVAVSTHELDILDTASHAAFLD---------S 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 106 LWGLVNNAGISTPSGPNEWMKKQDFAH---VLDVNLLGmievTLSMLPLVRK---ARGR--VVNVSSVM---GRVS--LF 172
Cdd:PRK07102  73 LPALPDIVLIAVGTLGDQAACEADPALalrEFRTNFEG----PIALLTLLANrfeARGSgtIVGISSVAgdrGRASnyVY 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568967027 173 GGGycisKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLcsnTQMLWDQ 229
Cdd:PRK07102 149 GSA----KAALTAFLSGLRNRLFKSGVHVLTVKPGFVRTPMTAGLKL---PGPLTAQ 198
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 26-211 1.80e-06

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 48.30  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  26 HLQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVI---LDVTKTESIVTATQWVKEHVG 102
Cdd:PRK06113   8 RLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFacrCDITSEQELSALADFALSKLG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 nrGLWGLVNNAGistPSGPNEW-MKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVV-NVSSVMG-----RVSLFGGg 175
Cdd:PRK06113  88 --KVDILVNNAG---GGGPKPFdMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVIlTITSMAAenkniNMTSYAS- 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568967027 176 yciSKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK06113 162 ---SKAAASHLVRNMAFDLGEKNIRVNGIAPGAILT 194
PRK05854 PRK05854
SDR family oxidoreductase;
27-168 2.95e-06

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 48.14  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTE-KG---AEELRNKTSD-RLETVILDVTKTESIVTATQWVKEHv 101
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRaKGeaaVAAIRTAVPDaKLSLRALDLSSLASVAALGEQLRAE- 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568967027 102 gNRGLWGLVNNAGISTPsgPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGR 168
Cdd:PRK05854  91 -GRPIHLLINNAGVMTP--PERQTTADGFELQFGTNHLGHFALTAHLLPLLRAGRARVTSQSSIAAR 154
DUF1776 pfam08643
Fungal family of unknown function (DUF1776); This is a fungal family of unknown function. One ...
 44-303 2.96e-06

Fungal family of unknown function (DUF1776); This is a fungal family of unknown function. One of the proteins in this family Swiss:P32792 has been localized to the mitochondria.


Pssm-ID: 370028  Cd Length: 295  Bit Score: 47.81  E-value: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027   44 LLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTA----------TQW----VKEHVGNrgLWGL 109
Cdd:pfam08643  19 AIALDLERRGFIVFVTVTSAKDYKTVESEQRPDIRPLSLDDTAPSSIEASleeflqlletPHVpfpgAKPHVLR--LRGV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  110 VNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVR----KARGRVVNVSSVmgrVSL---FGGGYCISKYG 182
Cdd:pfam08643  97 ILVPSLSYPTGPIENIPPSSWASEFNSRLLNYYLTLQGLLPLLRsrsqKAQIIVFNPSIS---SSLnlpYHAPEALVSSA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  183 VEAFSDSLRRELSYFGVKVAIIEPGFF--LTGVTSSARLCSNTQMLWDQTSSEIREIYGEKYLASYLKRLNKLDKRCN-- 258
Cdd:pfam08643 174 LSTLFTTLKRELRPHGIDVTQIKLGNLdlSNGSASNYKYLNIAGSEVLSWSEIMRALYGPNYVSIQSKAIGIRSTRGSsl 253

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 568967027  259 -KDLSGVTDCMEHALTachPRTRYsAGWDAKLFYLPLSYLPTFLVD 303
Cdd:pfam08643 254 rELHNALFDLLYGSSP---KPVVY-CGKGARLYSWVGKWLPEWLLS 295
PRK08177 PRK08177
SDR family oxidoreductase;
30-211 3.24e-06

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 47.33  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETviLDVTKTESIVTATQWVKEHVGNRglwgL 109
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIEK--LDMNDPASLDQLLQRLQGQRFDL----L 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 110 VNNAGISTPsgpnewmKKQDFAHV--------LDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRVSLFGGG----YC 177
Cdd:PRK08177  76 FVNAGISGP-------AHQSAADAtaaeigqlFLTNAIAPIRLARRLLGQVRPGQGVLAFMSSQLGSVELPDGGemplYK 148

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568967027 178 ISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK08177 149 ASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKT 182
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 30-211 3.71e-06

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 47.49  E-value: 3.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKtesiVTATQWVKEHVGNRGLW-G 108
Cdd:cd08951    8 KRIFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSS----LAETRKLADQVNAIGRFdA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 109 LVNNAGIStpSGPNEWMKKQDFAHVLDVNLLGMIEVTlsmlPLVRKARgRVVNVSSVM---GRVSLFG-----------G 174
Cdd:cd08951   84 VIHNAGIL--SGPNRKTPDTGIPAMVAVNVLAPYVLT----ALIRRPK-RLIYLSSGMhrgGNASLDDidwfnrgendsP 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568967027 175 GYCISKYGVEAFSDSLRRelSYFGVKVAIIEPGFFLT 211
Cdd:cd08951  157 AYSDSKLHVLTLAAAVAR--RWKDVSSNAVHPGWVPT 191
PRK09135 PRK09135
pteridine reductase; Provisional
 28-207 4.46e-06

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 47.23  E-value: 4.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  28 QDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLT-----EKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVG 102
Cdd:PRK09135   5 SAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRsaaeaDALAAELNALRPGSAAALQADLLDPDALPELVAACVAAFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 103 nrGLWGLVNNAG--ISTPSG---PNEWmkkQDfahVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSV-----MGRVSLf 172
Cdd:PRK09135  85 --RLDALVNNASsfYPTPLGsitEAQW---DD---LFASNLKAPFFLSQAAAPQLRKQRGAIVNITDIhaerpLKGYPV- 155

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568967027 173 gggYCISKYGVEAFSDSLRRELSYfGVKVAIIEPG 207
Cdd:PRK09135 156 ---YCAAKAALEMLTRSLALELAP-EVRVNAVAPG 186
PRK07035 PRK07035
SDR family oxidoreductase;
27-245 4.48e-06

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 47.32  E-value: 4.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRV------LAACltEKGAEELRNKtSDRLETVILDVTKTESIVTATQWVKEH 100
Cdd:PRK07035   6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVivssrkLDGC--QAVADAIVAA-GGKAEALACHIGEMEQIDALFAHIRER 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 101 VGNrgLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVMG-RVSLFGGGYCI 178
Cdd:PRK07035  83 HGR--LDILVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEqGGGSIVNVASVNGvSPGDFQGIYSI 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568967027 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGffLTGVTSSARLCSNTQMLwDQTSSEI--------REIYGEK-YLAS 245
Cdd:PRK07035 161 TKAAVISMTKAFAKECAPFGIRVNALLPG--LTDTKFASALFKNDAIL-KQALAHIplrrhaepSEMAGAVlYLAS 233
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 1-218 4.99e-06

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 47.55  E-value: 4.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027   1 MWLYLVALVGLWTLLRFF--RVRQV-VSHLQ-----DKY---VFITGCDSGFGTLLARQLDRRGMR-VLAACLTEK---G 65
Cdd:PLN02780  14 LWLLVLFVLGSLSILKFFftILNWVyVYFLRpaknlKKYgswALVTGPTDGIGKGFAFQLARKGLNlVLVARNPDKlkdV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  66 AEELRNKTSD-RLETVILDVTKteSIVTATQWVKEHVGNRGLWGLVNNAGISTPSGpnEWMKKQD---FAHVLDVNLLGM 141
Cdd:PLN02780  94 SDSIQSKYSKtQIKTVVVDFSG--DIDEGVKRIKETIEGLDVGVLINNVGVSYPYA--RFFHEVDeelLKNLIKVNVEGT 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 142 IEVTLSMLP-LVRKARGRVVNVSSVMGRV---SLFGGGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSA 217
Cdd:PLN02780 170 TKVTQAVLPgMLKRKKGAIINIGSGAAIVipsDPLYAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMASIR 249


                 .
gi 568967027 218 R 218
Cdd:PLN02780 250 R 250
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 32-202 6.63e-06

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


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 46.61  E-value: 6.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVIL----DVTKTESIVTATQWVKEHVGNRGLw 107
Cdd:cd05373    2 AAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKavptDARDEDEVIALFDLIEEEIGPLEV- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 108 gLVNNAGISTPSGPNEwMKKQDFAHVLDVNLLGMI----EVTLSMLPlvrKARGRVV---NVSSVMGRVSL--FGGGyci 178
Cdd:cd05373   81 -LVYNAGANVWFPILE-TTPRVFEKVWEMAAFGGFlaarEAAKRMLA---RGRGTIIftgATASLRGRAGFaaFAGA--- 152

                        170       180
                 ....*....|....*....|....
gi 568967027 179 sKYGVEAFSDSLRRELSYFGVKVA 202
Cdd:cd05373  153 -KFALRALAQSMARELGPKGIHVA 175
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 27-207 8.42e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 46.46  E-value: 8.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLaacLTEKGAEELrnktsDRL---------ETVIL--DVTKTESIVTATQ 95
Cdd:PRK07478   4 LNGKVAIITGASSGIGRAAAKLFAREGAKVV---VGARRQAEL-----DQLvaeiraeggEAVALagDVRDEAYAKALVA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  96 WVKEHVGnrGLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMGRVSLFGG 174
Cdd:PRK07478  76 LAVERFG--GLDIAFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPaMLARGGGSLIFTSTFVGHTAGFPG 153

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568967027 175 --GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK07478 154 maAYAASKAGLIGLTQVLAAEYGAQGIRVNALLPG 188
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 27-225 9.72e-06

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 46.22  E-value: 9.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLA--ACLTEKGAEELRNKTSD-----RLETVILDVTKTESIVTA-TQWVK 98
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIhyGNRKEEAEETVYEIQSNggsafSIGANLESLHGVEALYSSlDNELQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  99 EHVGNRGLWGLVNNAGIStPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKaRGRVVNVSSVMGRVSLFGG-GYC 177
Cdd:PRK12747  82 NRTGSTKFDILINNAGIG-PGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRD-NSRIINISSAATRISLPDFiAYS 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568967027 178 ISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVtsSARLCSNTQM 225
Cdd:PRK12747 160 MTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDM--NAELLSDPMM 205
PRK09186 PRK09186
flagellin modification protein A; Provisional
 27-167 1.01e-05

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 46.14  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEEL-----RNKTSDRLETVILDVTKTESIVTATQWVKEHV 101
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELleslgKEFKSKKLSLVELDITDQESLEEFLSKSAEKY 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967027 102 GNrgLWGLVNNAgisTPSGPNeWMKK------QDFAHVLDVNLLGMIEVTLSMLP-LVRKARGRVVNVSSVMG 167
Cdd:PRK09186  82 GK--IDGAVNCA---YPRNKD-YGKKffdvslDDFNENLSLHLGSSFLFSQQFAKyFKKQGGGNLVNISSIYG 148
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 27-211 1.24e-05

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 45.91  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVL-----AACLtEKGAEELRNKTSDrLETVILDVTKTESIVTATQWVKEHV 101
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVIlngrdPAKL-AAAAESLKGQGLS-AHALAFDVTDHDAVRAAIDAFEAEI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 102 GNRGLwgLVNNAGISTPSgPNEWMKKQDFAHVLDVNLLGMIEVTLSML-PLVRKARGRVVNVSSV---MGRVSLfgGGYC 177
Cdd:PRK07523  86 GPIDI--LVNNAGMQFRT-PLEDFPADAFERLLRTNISSVFYVGQAVArHMIARGAGKIINIASVqsaLARPGI--APYT 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568967027 178 ISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK07523 161 ATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDT 194
PRK07062 PRK07062
SDR family oxidoreductase;
27-168 1.50e-05

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 45.80  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVlAACLTE----KGAE-ELRNKTSD-RLETVILDVTKTESIVTATQWVKEH 100
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASV-AICGRDeerlASAEaRLREKFPGaRLLAARCDVLDEADVAAFAAAVEAR 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568967027 101 VGnrGLWGLVNNAGISTPSgPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKA-RGRVVNVSSVMGR 168
Cdd:PRK07062  85 FG--GVDMLVNNAGQGRVS-TFADTTDDAWRDELELKYFSVINPTRAFLPLLRASaAASIVCVNSLLAL 150
PRK06128 PRK06128
SDR family oxidoreductase;
27-211 1.72e-05

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 45.62  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACL--TEKGAEELRN--KTSDRLETVILDVTKTESIvtATQWV-KEHV 101
Cdd:PRK06128  53 LQGRKALITGADSGIGRATAIAFAREGADIALNYLpeEEQDAAEVVQliQAEGRKAVALPGDLKDEAF--CRQLVeRAVK 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 102 GNRGLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVrKARGRVVNVSSVMG---RVSLFggGYCI 178
Cdd:PRK06128 131 ELGGLDILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHL-PPGASIINTGSIQSyqpSPTLL--DYAS 207

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568967027 179 SKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK06128 208 TKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWT 240
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 27-211 1.87e-05

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: 45.52  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVL----AACLTEKG-AEELRnKTSDRLETVILDVTKTESIVTATQWVKEHV 101
Cdd:cd09763    1 LSGKIALVTGASRGIGRGIALQLGEAGATVYitgrTILPQLPGtAEEIE-ARGGKCIPVRCDHSDDDEVEALFERVAREQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 102 GNRgLWGLVNNA------GISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKA-RGRVVNVSSVMGRVSLFGG 174
Cdd:cd09763   80 QGR-LDILVNNAyaavqlILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAgKGLIVIISSTGGLEYLFNV 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568967027 175 GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:cd09763  159 AYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRT 195
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-206 2.03e-05

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 45.54  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVL-----AACLTEKGAEELRNKTSdRLETVILDVTKTEsivTATQWVKEHV 101
Cdd:PRK07792  10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVvndvaSALDASDVLDEIRAAGA-KAVAVAGDISQRA---TADELVATAV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 102 GNRGLWGLVNNAGIsTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVR-KAR-------GRVVNVSSVMGRVSLFG 173
Cdd:PRK07792  86 GLGGLDIVVNNAGI-TRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRaKAKaaggpvyGRIVNTSSEAGLVGPVG 164

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568967027 174 -GGYCISKYGVEAFSDSLRRELSYFGVKVAIIEP 206
Cdd:PRK07792 165 qANYGAAKAGITALTLSAARALGRYGVRANAICP 198
PRK05867 PRK05867
SDR family oxidoreductase;
27-211 2.72e-05

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 44.64  E-value: 2.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAAClteKGAEELRnKTSDRLE-------TVILDVTKTESIVTATQWVKE 99
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAA---RHLDALE-KLADEIGtsggkvvPVCCDVSQHQQVTSMLDQVTA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 100 HVGnrGLWGLVNNAGISTPSGPNEwMKKQDFAHVLDVNLLGM-IEVTLSMLPLVRKARG-RVVNVSSVMGR---VSLFGG 174
Cdd:PRK05867  83 ELG--GIDIAVCNAGIITVTPMLD-MPLEEFQRLQNTNVTGVfLTAQAAAKAMVKQGQGgVIINTASMSGHiinVPQQVS 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568967027 175 GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK05867 160 HYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILT 196
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 32-174 4.38e-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: 44.43  E-value: 4.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCDSGFGTLLARQLDRRGM-RVLAACLTEKGAEELRNKT---SDRLETVILDVTKTESIvtaTQWVKEHVGN-RGL 106
Cdd:cd09810    4 VVITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQEVgmpKDSYSVLHCDLASLDSV---RQFVDNFRRTgRPL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967027 107 WGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARG---RVVNVSSVMGRVSLFGG 174
Cdd:cd09810   81 DALVCNAAVYLPTAKEPRFTADGFELTVGVNHLGHFLLTNLLLEDLQRSENaspRIVIVGSITHNPNTLAG 151
PRK09730 PRK09730
SDR family oxidoreductase;
34-216 4.99e-05

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 44.07  E-value: 4.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  34 ITGCDSGFGTLLARQLDRRGMRVLAACL-TEKGAEELRNK---TSDRLETVILDVTKTESIVTATQWVKEHVGNrgLWGL 109
Cdd:PRK09730   6 VTGGSRGIGRATALLLAQEGYTVAVNYQqNLHAAQEVVNLitqAGGKAFVLQADISDENQVVAMFTAIDQHDEP--LAAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 110 VNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMI----EVTLSMLPLVRKARGRVVNVSSVMGRVSLFGG--GYCISKYGV 183
Cdd:PRK09730  84 VNNAGILFTQCTVENLTAERINRVLSTNVTGYFlccrEAVKRMALKHGGSGGAIVNVSSAASRLGAPGEyvDYAASKGAI 163

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568967027 184 EAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSS 216
Cdd:PRK09730 164 DTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHAS 196
PRK07985 PRK07985
SDR family oxidoreductase;
27-207 8.17e-05

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 43.44  E-value: 8.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACL--TEKGAEELRNKTSDRLETVIL---DVTKTESIVTATQWVKEHV 101
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISYLpvEEEDAQDVKKIIEECGRKAVLlpgDLSDEKFARSLVHEAHKAL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 102 GNRGLWGLVNNAGISTPSGPNewMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKArGRVVNVSSVMG-RVSLFGGGYCISK 180
Cdd:PRK07985 127 GGLDIMALVAGKQVAIPDIAD--LTSEQFQKTFAINVFALFWLTQEAIPLLPKG-ASIITTSSIQAyQPSPHLLDYAATK 203

                        170       180
                 ....*....|....*....|....*..
gi 568967027 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 9.25e-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: 43.35  E-value: 9.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  34 ITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRN---KTSDRLETV--ILDVTKTESIVTATQWVKEHvgNRGLWG 108
Cdd:cd09808    6 ITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKeieTESGNQNIFlhIVDMSDPKQVWEFVEEFKEE--GKKLHV 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568967027 109 LVNNAG-ISTPSGPNEWMKKQDFAhvldVNLLGMIEVTLSMLPLVRKARG-RVVNVSS 164
Cdd:cd09808   84 LINNAGcMVNKRELTEDGLEKNFA----TNTLGTYILTTHLIPVLEKEEDpRVITVSS 137
PRK05717 PRK05717
SDR family oxidoreductase;
30-208 1.75e-04

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 42.18  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIvtaTQWVKEHVGNRG-LWG 108
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFIAMDVADEAQV---AAGVAEVLGQFGrLDA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 109 LVNNAGISTPSgpNEWMKKQDFAH---VLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRVSLFGG-GYCISKYGVE 184
Cdd:PRK05717  88 LVCNAAIADPH--NTTLESLSLAHwnrVLAVNLTGPMLLAKHCAPYLRAHNGAIVNLASTRARQSEPDTeAYAASKGGLL 165

                        170       180
                 ....*....|....*....|....
gi 568967027 185 AFSDSLRRELSYfGVKVAIIEPGF 208
Cdd:PRK05717 166 ALTHALAISLGP-EIRVNAVSPGW 188
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
27-211 2.31e-04

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 42.01  E-value: 2.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGA-----EELRnKTSDRLETVILDVTKTESIVTATQWVKEHV 101
Cdd:PRK08063   2 FSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAaeetaEEIE-ALGRKALAVKANVGDVEKIKEMFAQIDEEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 102 GnrGLWGLVNNAGistpSGPNEWMKKQDFAH---VLDVNLLGMIEVTLSMLPLVRKAR-GRVVNVSSV-MGRV---SLFG 173
Cdd:PRK08063  81 G--RLDVFVNNAA----SGVLRPAMELEESHwdwTMNINAKALLFCAQEAAKLMEKVGgGKIISLSSLgSIRYlenYTTV 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568967027 174 GgycISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLT 211
Cdd:PRK08063 155 G---VSKAALEALTRYLAVELAPKGIAVNAVSGGAVDT 189
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 34-165 2.64e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 41.93  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  34 ITGCDSGFGTLLARQLDRRGMRV-LAACLTEKG---AEELRNKTSDRLETVI-LDVTKTESIVTATQWVKEHVGNRGLwg 108
Cdd:PRK06197  21 VTGANTGLGYETAAALAAKGAHVvLAVRNLDKGkaaAARITAATPGADVTLQeLDLTSLASVRAAADALRAAYPRIDL-- 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568967027 109 LVNNAGISTPsgPNEwMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARG-RVVNVSSV 165
Cdd:PRK06197  99 LINNAGVMYT--PKQ-TTADGFELQFGTNHLGHFALTGLLLDRLLPVPGsRVVTVSSG 153
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 25-207 3.45e-04

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 41.60  E-value: 3.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  25 SHLQDKYVFITGCD--SGFGTLLARQLDRRGMRVLAACLTEKGAE--------------ELRNKTSDRLETVILDVTKTE 88
Cdd:PRK12748   1 LPLMKKIALVTGASrlNGIGAAVCRRLAAKGIDIFFTYWSPYDKTmpwgmhdkepvllkEEIESYGVRCEHMEIDLSQPY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  89 SIVTATQWVKEHVGNRGLwgLVNNAGISTPSGPNEwmkkqdfahvLDVNLLG---MIEVTLSMLpLVR--------KARG 157
Cdd:PRK12748  81 APNRVFYAVSERLGDPSI--LINNAAYSTHTRLEE----------LTAEQLDkhyAVNVRATML-LSSafakqydgKAGG 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568967027 158 RVVNVSS------VMGRVSlfgggYCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK12748 148 RIINLTSgqslgpMPDELA-----YAATKGAIEAFTKSLAPELAEKGITVNAVNPG 198
PRK07856 PRK07856
SDR family oxidoreductase;
27-211 8.08e-04

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 40.30  E-value: 8.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNktsdrLETVILDVTKTESIVTATQWVKEHVGnrGL 106
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETVDGRP-----AEFHAADVRDPDQVAALVDAIVERHG--RL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 107 WGLVNNAGIStPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRK--ARGRVVNVSSVMG-RVSLFGGGYCISKYGV 183
Cdd:PRK07856  77 DVLVNNAGGS-PYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQqpGGGSIVNIGSVSGrRPSPGTAAYGAAKAGL 155

                        170       180
                 ....*....|....*....|....*...
gi 568967027 184 EAFSDSLRRELSYfGVKVAIIEPGFFLT 211
Cdd:PRK07856 156 LNLTRSLAVEWAP-KVRVNAVVVGLVRT 182
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 66-212 1.09e-03

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 39.77  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  66 AEELRnKTSDRLETVILDVTKTESIVTATQWVKEHVGNRGLwgLVNNAGISTPSGPNEWMKKQDFAHVLdVNLLGMIEVT 145
Cdd:PRK12859  60 QEELL-KNGVKVSSMELDLTQNDAPKELLNKVTEQLGYPHI--LVNNAAYSTNNDFSNLTAEELDKHYM-VNVRATTLLS 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568967027 146 LSMLPLVRKARG-RVVNVSSVMGRVSLFGG-GYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTG 212
Cdd:PRK12859 136 SQFARGFDKKSGgRIINMTSGQFQGPMVGElAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTG 204
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 30-210 1.14e-03

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: 39.57  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  30 KYVFITGCDSGFGTLLARQLDRRGMRVLAACLT-EKGAEELR---NKTSDRLETVILDVTKTESIVTATQWVKEHVGNRG 105
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRsEAEAQRLKdelNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 106 LwgLVNNAGI--STPSGPNEWmkkQDFAHVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSSVMGRVSLFGG-GYCISKY 181
Cdd:cd05357   81 V--LVNNASAfyPTPLGQGSE---DAWAELFGINLKAPYLLIQAFARRLAGsRNGSIINIIDAMTDRPLTGYfAYCMSKA 155

                        170       180
                 ....*....|....*....|....*....
gi 568967027 182 GVEAFSDSLRRELSYFgVKVAIIEPGFFL 210
Cdd:cd05357  156 ALEGLTRSAALELAPN-IRVNGIAPGLIL 183
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 27-207 1.23e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 39.94  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRV------------LAACLTEKGAEELrnktsdrleTVILDVTKTESIVTAT 94
Cdd:PRK07576   7 FAGKNVVVVGGTSGINLGIAQAFARAGANVavasrsqekvdaAVAQLQQAGPEGL---------GVSADVRDYAAVEAAF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  95 QWVKEHVGNRGLwgLVNNAGISTPSgPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRV-SLFG 173
Cdd:PRK07576  78 AQIADEFGPIDV--LVSGAAGNFPA-PAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPGASIIQISAPQAFVpMPMQ 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568967027 174 GGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPG 207
Cdd:PRK07576 155 AHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVPG 188
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 27-182 1.83e-03

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: 39.35  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEK-----------GAEELRNKTSDRLeTVILDVTKTESIVTATQ 95
Cdd:cd09762    1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEphpklpgtiytAAEEIEAAGGKAL-PCIVDIRDEDQVRAAVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  96 WVKEHVGnrGLWGLVNNA-GISTPSGPNEWMKKQDFAHvlDVNLLGMIEVTLSMLPLVRKARG-RVVNVSSVMG-RVSLF 172
Cdd:cd09762   80 KAVEKFG--GIDILVNNAsAISLTGTLDTPMKRYDLMM--GVNTRGTYLCSKACLPYLKKSKNpHILNLSPPLNlNPKWF 155

                        170
                 ....*....|..
gi 568967027 173 GG--GYCISKYG 182
Cdd:cd09762  156 KNhtAYTMAKYG 167
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 29-164 2.46e-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: 39.12  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  29 DKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEE-----LRNKTSDRLETVILDVTKTESIVTATQWVKEHvgN 103
Cdd:cd09809    1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAavsriLEEWHKARVEAMTLDLASLRSVQRFAEAFKAK--N 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967027 104 RGLWGLVNNAGISTPSgpneWMKKQD-FAHVLDVNLLGMIEVTLSMLPLVRK-ARGRVVNVSS 164
Cdd:cd09809   79 SPLHVLVCNAAVFALP----WTLTEDgLETTFQVNHLGHFYLVQLLEDVLRRsAPARVIVVSS 137
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 32-217 2.47e-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: 38.67  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  32 VFITGCdSGF-GTLLARQLDRRGMRVLAACLTEKGAEELRNktsDRLETVILDVTKTESIVTATQwvkehvgnrGLWGLV 110
Cdd:COG0702    2 ILVTGA-TGFiGRRVVRALLARGHPVRALVRDPEKAAALAA---AGVEVVQGDLDDPESLAAALA---------GVDAVF 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 111 NNAGISTpsgpnewmkKQDFAHVLDvnllgmievtlSMLPLVRKAR----GRVVNVSSvMGRVSLFGGGYCISKYGVE-A 185
Cdd:COG0702   69 LLVPSGP---------GGDFAVDVE-----------GARNLADAAKaagvKRIVYLSA-LGADRDSPSPYLRAKAAVEeA 127

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568967027 186 FSDSlrrelsyfGVKVAIIEPGFFLTGVTSSA 217
Cdd:COG0702  128 LRAS--------GLPYTILRPGWFMGNLLGFF 151
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
 32-227 2.51e-03

thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.


Pssm-ID: 273787 [Multi-domain]  Cd Length: 367  Bit Score: 39.32  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027   32 VFITGCdSGF-GTLLARQLDRRGMRVLAACLT-----EKGAEELR-----------NKTSDRLETVILDVTKTESIVTAT 94
Cdd:TIGR01746   2 VLLTGA-TGFlGAYLLEELLRRSTRAKVICLVradseEHAMERLRealrsyrlwheNLAMERIEVVAGDLSKPRLGLSDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027   95 QWVK--EHVGNrglwgLVNNAGISTPSGPNEWMKKqdfahvldVNLLGMIEV----------------TLSMLPLVRKAR 156
Cdd:TIGR01746  81 EWERlaENVDT-----IVHNGALVNHVYPYSELRG--------ANVLGTVEVlrlaasgrakplhyvsTISVGAAIDLST 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967027  157 GRVVNVSSVMGRVSLfGGGYCISKYgveaFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLCSNtqMLW 227
Cdd:TIGR01746 148 GVTEDDATVTPYPGL-AGGYTQSKW----VAELLVREASDRGLPVTIVRPGRILGDSYTGAWNSSD--ILW 211
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-211 2.90e-03

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 38.55  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAAclTEKGAEE-------LRNKTSDRLeTVILDVTKTESIVTAtqwVKE 99
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVN--AKKRAEEmnetlkmVKENGGEGI-GVLADVSTREGCETL---AKA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027 100 HVGN-RGLWGLVNNAGISTPS----GPNEWMKKQdfahvLDVNLLGMIEVTLSMLPLVRKArGRVVNVSSVMGRVSLFG- 173
Cdd:PRK06077  78 TIDRyGVADILVNNAGLGLFSpflnVDDKLIDKH-----ISTDFKSVIYCSQELAKEMREG-GAIVNIASVAGIRPAYGl 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568967027 174 GGYCISKYGVEAFSDSLRRELSYfGVKVAIIEPGFFLT 211
Cdd:PRK06077 152 SIYGAMKAAVINLTKYLALELAP-KIRVNAIAPGFVKT 188
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 27-174 6.31e-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: 37.75  E-value: 6.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967027  27 LQDKYVFITGCDSGFGTLLARQLDRRGMRVLAAC------LTEKGAEELRNKTSDRLETVILDVTKTESiVTATqwVKEH 100
Cdd:cd05274  148 GLDGTYLITGGLGGLGLLVARWLAARGARHLVLLsrrgpaPRAAARAALLRAGGARVSVVRCDVTDPAA-LAAL--LAEL 224

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568967027 101 VGNRGLWGLVNNAGISTPsGPNEWMKKQDFAHVLDVNLLGmievTLSMLPLVRKARG-RVVNVSSVMgrvSLFGG 174
Cdd:cd05274  225 AAGGPLAGVIHAAGVLRD-ALLAELTPAAFAAVLAAKVAG----ALNLHELTPDLPLdFFVLFSSVA---ALLGG 291
 
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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