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Conserved domains on  [gi|226510520|ref|NP_663399|]
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cis-retinol/3alpha hydroxysterol short-chain dehydrogenase-like [Mus musculus]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10176849)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase may catalyze isomerization, decarboxylation, epimerization, C=N bond reduction, dehydration, dehalogenation, enoyl-CoA reduction, and/or carbonyl-alcohol oxidoreduction; classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 30-307 3.67e-141

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: 399.73  E-value: 3.67e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEE--GAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGNRGLW 107
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKNgpGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 108 GLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEAF 187
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAAVEAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 188 SDSLRRELRYFGVKVAIIEPGFFLTGMASSARLCSNI-QMLWDQTSSEIREIYGEKYLASYLKNLNELDQRCNKDLSVVT 266
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQaKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 226510520 267 DCMEHALTACHPRTRYSAGWDAKLFFTPLSYLPTFLVDALL 307
Cdd:cd09805  241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 30-307 3.67e-141

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: 399.73  E-value: 3.67e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEE--GAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGNRGLW 107
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKNgpGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 108 GLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEAF 187
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAAVEAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 188 SDSLRRELRYFGVKVAIIEPGFFLTGMASSARLCSNI-QMLWDQTSSEIREIYGEKYLASYLKNLNELDQRCNKDLSVVT 266
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQaKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 226510520 267 DCMEHALTACHPRTRYSAGWDAKLFFTPLSYLPTFLVDALL 307
Cdd:cd09805  241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
27-307 6.08e-57

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 184.30  E-value: 6.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELR---RKTSERLETVILDVTKTENIVAATQWVKERVGn 103
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAaelRAAGARVEVVALDVTDPDAVAALAEAVLARFG- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 rGLWGLVNNAGISVPsGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKA-RGRVVNVSSILGRVSLGGSGGYCISKY 182
Cdd:COG0300   82 -PIDVLVNNAGVGGG-GPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARgRGRIVNVSSVAGLRGLPGMAAYAASKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 183 GIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSARLCSNIQMLwdqtSSEireiygekylasylknlneldqrcnkdl 262
Cdd:COG0300  160 ALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPLL----SPE---------------------------- 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 226510520 263 sVVTDCMEHALTacHPRTRYSAGWDAKLFFTPLSYLPTfLVDALL 307
Cdd:COG0300  208 -EVARAILRALE--RGRAEVYVGWDARLLARLLRLLPR-LFDRLL 248
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 30-219 1.49e-49

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 163.55  E-value: 1.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520   30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRK---TSERLETVILDVTKTENIVAATQWVKERVGnrGL 106
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKElgaLGGKALFIQGDVTDRAQVKALVEQAVERLG--RL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  107 WGLVNNAGISvPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIE 185
Cdd:pfam00106  79 DILVNNAGIT-GLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVI 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 226510520  186 AFSDSLRRELRYFGVKVAIIEPGFFLTGMASSAR 219
Cdd:pfam00106 158 GFTRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
PRK05993 PRK05993
SDR family oxidoreductase;
30-311 4.63e-44

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 152.10  E-value: 4.63e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEgaeELRRKTSERLETVILDVTKTENIVAATQWVKERVGNRgLWGL 109
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEE---DVAALEAEGLEAFQLDYAEPESIAALVAQVLELSGGR-LDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 110 VNNAGISVPSG----PNEWMKKQdfasvLDVNLLGLIEVTLSMLPLVRK-ARGRVVNVSSILGRVSLGGSGGYCISKYGI 184
Cdd:PRK05993  81 FNNGAYGQPGAvedlPTEALRAQ-----FEANFFGWHDLTRRVIPVMRKqGQGRIVQCSSILGLVPMKYRGAYNASKFAI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 185 EAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSArlCSNIQMLWDQTSSEIReiygekylASYLKNLneldQRCNKDLSV 264
Cdd:PRK05993 156 EGLSLTLRMELQGSGIHVSLIEPGPIETRFRANA--LAAFKRWIDIENSVHR--------AAYQQQM----ARLEGGGSK 221

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226510520 265 ---------VTDCMEHALTACHPRTRYSAGWDAKLFFTPLSYLPTFLVDALLYWTS 311
Cdd:PRK05993 222 srfklgpeaVYAVLLHALTAPRPRPHYRVTTPAKQGALLKRLLPARWLYRLLRKAA 277
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 32-214 3.62e-28

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: 109.22  E-value: 3.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520   32 VFITGCGSGFGNLLARQLDRRGMRVLAACR-KEEGAEELR---RKTSERLETVILDVTKTENIVAATQWVKERVGnrGLW 107
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRsSEEGAEEVVeelKALGVKALGVVLDVSDREDVKAVVEEIEEELG--TID 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  108 GLVNNAGISvPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGrvsLGGSGG---YCISKYG 183
Cdd:TIGR01830  79 ILVNNAGIT-RDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRsGRIINISSVVG---LMGNAGqanYAASKAG 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 226510520  184 IEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:TIGR01830 155 VIGFTKSLAKELASRNITVNAVAPGFIDTDM 185
 
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; ...
 30-307 3.67e-141

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: 399.73  E-value: 3.67e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEE--GAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGNRGLW 107
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKNgpGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 108 GLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEAF 187
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAAVEAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 188 SDSLRRELRYFGVKVAIIEPGFFLTGMASSARLCSNI-QMLWDQTSSEIREIYGEKYLASYLKNLNELDQRCNKDLSVVT 266
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQaKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 226510520 267 DCMEHALTACHPRTRYSAGWDAKLFFTPLSYLPTFLVDALL 307
Cdd:cd09805  241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 30-289 7.74e-67

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: 209.78  E-value: 7.74e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGnrGLWGL 109
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFG--RIDVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 110 VNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKYGIEAFS 188
Cdd:cd05374   79 VNNAGYGL-FGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGsGRIVNVSSVAGLVPTPFLGPYCASKAALEALS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 189 DSLRRELRYFGVKVAIIEPGFFLTGMAS---SARLCSNIQMLWDQTSSEIREIYGEKYLASYlknlneldqrcnkDLSVV 265
Cdd:cd05374  158 ESLRLELAPFGIKVTIIEPGPVRTGFADnaaGSALEDPEISPYAPERKEIKENAAGVGSNPG-------------DPEKV 224

                        250       260
                 ....*....|....*....|....
gi 226510520 266 TDCMEHALTACHPRTRYSAGWDAK 289
Cdd:cd05374  225 ADVIVKALTSESPPLRYFLGSDAL 248
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
27-307 6.08e-57

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 184.30  E-value: 6.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELR---RKTSERLETVILDVTKTENIVAATQWVKERVGn 103
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAaelRAAGARVEVVALDVTDPDAVAALAEAVLARFG- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 rGLWGLVNNAGISVPsGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKA-RGRVVNVSSILGRVSLGGSGGYCISKY 182
Cdd:COG0300   82 -PIDVLVNNAGVGGG-GPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARgRGRIVNVSSVAGLRGLPGMAAYAASKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 183 GIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSARLCSNIQMLwdqtSSEireiygekylasylknlneldqrcnkdl 262
Cdd:COG0300  160 ALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPLL----SPE---------------------------- 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 226510520 263 sVVTDCMEHALTacHPRTRYSAGWDAKLFFTPLSYLPTfLVDALL 307
Cdd:COG0300  208 -EVARAILRALE--RGRAEVYVGWDARLLARLLRLLPR-LFDRLL 248
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 28-219 5.77e-55

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: 178.84  E-value: 5.77e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  28 QDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGnrGLW 107
Cdd:COG4221    4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFG--RLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 108 GLVNNAGISVPsGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEA 186
Cdd:COG4221   82 VLVNNAGVALL-GPLEELDPEDWDRMIDVNVKGVLYVTRAALPaMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRG 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226510520 187 FSDSLRRELRYFGVKVAIIEPGFFLTGMASSAR 219
Cdd:COG4221  161 LSESLRAELRPTGIRVTVIEPGAVDTEFLDSVF 193
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 30-219 1.49e-49

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 163.55  E-value: 1.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520   30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRK---TSERLETVILDVTKTENIVAATQWVKERVGnrGL 106
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKElgaLGGKALFIQGDVTDRAQVKALVEQAVERLG--RL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  107 WGLVNNAGISvPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIE 185
Cdd:pfam00106  79 DILVNNAGIT-GLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVI 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 226510520  186 AFSDSLRRELRYFGVKVAIIEPGFFLTGMASSAR 219
Cdd:pfam00106 158 GFTRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
PRK05993 PRK05993
SDR family oxidoreductase;
30-311 4.63e-44

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 152.10  E-value: 4.63e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEgaeELRRKTSERLETVILDVTKTENIVAATQWVKERVGNRgLWGL 109
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEE---DVAALEAEGLEAFQLDYAEPESIAALVAQVLELSGGR-LDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 110 VNNAGISVPSG----PNEWMKKQdfasvLDVNLLGLIEVTLSMLPLVRK-ARGRVVNVSSILGRVSLGGSGGYCISKYGI 184
Cdd:PRK05993  81 FNNGAYGQPGAvedlPTEALRAQ-----FEANFFGWHDLTRRVIPVMRKqGQGRIVQCSSILGLVPMKYRGAYNASKFAI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 185 EAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSArlCSNIQMLWDQTSSEIReiygekylASYLKNLneldQRCNKDLSV 264
Cdd:PRK05993 156 EGLSLTLRMELQGSGIHVSLIEPGPIETRFRANA--LAAFKRWIDIENSVHR--------AAYQQQM----ARLEGGGSK 221

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226510520 265 ---------VTDCMEHALTACHPRTRYSAGWDAKLFFTPLSYLPTFLVDALLYWTS 311
Cdd:PRK05993 222 srfklgpeaVYAVLLHALTAPRPRPHYRVTTPAKQGALLKRLLPARWLYRLLRKAA 277
PRK08017 PRK08017
SDR family oxidoreductase;
30-309 1.30e-43

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 150.24  E-value: 1.30e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKeegAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGNRgLWGL 109
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAACRK---PDDVARMNSLGFTGILLDLDDPESVERAADEVIALTDNR-LYGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 110 VNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVR-KARGRVVNVSSILGRVSLGGSGGYCISKYGIEAFS 188
Cdd:PRK08017  79 FNNAGFGV-YGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLpHGEGRIVMTSSVMGLISTPGRGAYAASKYALEAWS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 189 DSLRRELRYFGVKVAIIEPGFFLTgmassaRLCSNIQmlwdQTSSEireiygekylaSYLKNLNeLDQRCNKDLSVVTDC 268
Cdd:PRK08017 158 DALRMELRHSGIKVSLIEPGPIRT------RFTDNVN----QTQSD-----------KPVENPG-IAARFTLGPEAVVPK 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 226510520 269 MEHALTACHPRTRYSAGWDAKLFFTPLSYLPTFLVDALLYW 309
Cdd:PRK08017 216 LRHALESPKPKLRYPVTLVTHAVMVLKRLLPGRMMDKILRG 256
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 25-219 3.68e-43

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: 148.78  E-value: 3.68e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  25 DHLQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELR---RKTSERLETVILDVTKTENIVAATQWVKERV 101
Cdd:COG1028    2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAaelRAAGGRALAVAADVTDEAAVEALVAAAVAAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 102 GnrGLWGLVNNAGISVPsGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCIS 180
Cdd:COG1028   82 G--RLDILVNNAGITPP-GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGgGRIVNISSIAGLRGSPGQAAYAAS 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 226510520 181 KYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSAR 219
Cdd:COG1028  159 KAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALL 197
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 32-219 4.18e-43

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: 148.20  E-value: 4.18e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELR--RKTSERLETVILDVTKTENIVAATQWVKERVGnrGLWGL 109
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAaiEALGGNAVAVQADVSDEEDVEALVEEALEEFG--RLDIL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 110 VNNAGISVPsGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKYGIEAFS 188
Cdd:cd05233   79 VNNAGIARP-GPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGgGRIVNISSVAGLRPLPGQAAYAASKAALEGLT 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 226510520 189 DSLRRELRYFGVKVAIIEPGFFLTGMASSAR 219
Cdd:cd05233  158 RSLALELAPYGIRVNAVAPGLVDTPMLAKLG 188
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 33-237 6.63e-43

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 148.91  E-value: 6.63e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  33 FITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGnrGLWGLVNN 112
Cdd:PRK06180   8 LITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFG--PIDVLVNN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 113 AGI----SVPSGPNEWMKKQdfasvLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKYGIEAF 187
Cdd:PRK06180  86 AGYghegAIEESPLAEMRRQ-----FEVNVFGAVAMTKAVLPGMRARRrGHIVNITSMGGLITMPGIGYYCGSKFALEGI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 226510520 188 SDSLRRELRYFGVKVAIIEPGFFLT-----GMASSARLCSNiqmlWDQTSSEIRE 237
Cdd:PRK06180 161 SESLAKEVAPFGIHVTAVEPGSFRTdwagrSMVRTPRSIAD----YDALFGPIRQ 211
PRK06914 PRK06914
SDR family oxidoreductase;
30-299 9.15e-41

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 143.24  E-value: 9.15e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELR-----RKTSERLETVILDVTKTENIVAATQWVKErVGNR 104
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLsqatqLNLQQNIKVQQLDVTDQNSIHNFQLVLKE-IGRI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 105 GLwgLVNNAGIS-------VPSGpnEWmKKQdfasvLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGG 176
Cdd:PRK06914  83 DL--LVNNAGYAnggfveeIPVE--EY-RKQ-----FETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGLSP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 177 YCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSARlcsNIQMLWDQTSSEIREIYG--EKYLASYLKNLNEL 254
Cdd:PRK06914 153 YVSSKYALEGFSESLRLELKPFGIDVALIEPGSYNTNIWEVGK---QLAENQSETTSPYKEYMKkiQKHINSGSDTFGNP 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 226510520 255 DQRCNKDLSVVtdcmehalTACHPRTRYSAGWDAKLFFTPLSYLP 299
Cdd:PRK06914 230 IDVANLIVEIA--------ESKRPKLRYPIGKGVKLMILAKKILP 266
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 27-218 1.12e-39

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: 140.03  E-value: 1.12e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRK----TSERLETVILDVTKTENIVAATQWVKERVG 102
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSEclelGAPSPHVVPLDMSDLEDAEQVVEEALKLFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 nrGLWGLVNNAGISVPSgpnEWMKK--QDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCI 179
Cdd:cd05332   81 --GLDILINNAGISMRS---LFHDTsiDVDRKIMEVNYFGPVALTKAALPhLIERSQGSIVVVSSIAGKIGVPFRTAYAA 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 226510520 180 SKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:cd05332  156 SKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNA 194
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 28-307 3.09e-39

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 139.27  E-value: 3.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  28 QDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAeelrrKTSERLETVILDVTKTENIVAATQWVKERVGNRGLw 107
Cdd:PRK06179   3 NSKVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARA-----APIPGVELLELDVTDDASVQAAVDEVIARAGRIDV- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 108 gLVNNAGISVPSGPNEWMKKQDfASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKYGIEA 186
Cdd:PRK06179  77 -LVNNAGVGLAGAAEESSIAQA-QALFDTNVFGILRMTRAVLPHMRAQGsGRIINISSVLGFLPAPYMALYAASKHAVEG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 187 FSDSLRRELRYFGVKVAIIEPGFFLTGM-ASSARLCSNIQMLwdqtsSEIREIYgEKYLASYLKNLNELDqrcnkdlsVV 265
Cdd:PRK06179 155 YSESLDHEVRQFGIRVSLVEPAYTKTNFdANAPEPDSPLAEY-----DRERAVV-SKAVAKAVKKADAPE--------VV 220

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 226510520 266 TDCMEHALTACHPRTRYSAGWDAKLFFTPLSYLPTFLVDALL 307
Cdd:PRK06179 221 ADTVVKAALGPWPKMRYTAGGQASLLSKLRRFMPAGAVDKSL 262
PRK06182 PRK06182
short chain dehydrogenase; Validated
 28-307 5.78e-39

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 138.55  E-value: 5.78e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  28 QDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELrrkTSERLETVILDVTKTENIVAATQWVKERVGNRGLw 107
Cdd:PRK06182   2 QKKVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDL---ASLGVHPLSLDVTDEASIKAAVDTIIAEEGRIDV- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 108 gLVNNAGI----SVPSGPNEWMKKQdfasvLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKY 182
Cdd:PRK06182  78 -LVNNAGYgsygAIEDVPIDEARRQ-----FEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIYTPLGAWYHATKF 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 183 GIEAFSDSLRRELRYFGVKVAIIEPGffltgmassarlcsNIQMLWDQTSSE-IREI-----YGEKYLASYLKNLNELDQ 256
Cdd:PRK06182 152 ALEGFSDALRLEVAPFGIDVVVIEPG--------------GIKTEWGDIAADhLLKTsgngaYAEQAQAVAASMRSTYGS 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 226510520 257 RCNKDLSVVTDCMEHALTACHPRTRYSAGWDAKLFFTPLSYLPTFLVDALL 307
Cdd:PRK06182 218 GRLSDPSVIADAISKAVTARRPKTRYAVGFGAKPLIFLRRILPDRAFDRLI 268
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 27-212 6.34e-38

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: 134.97  E-value: 6.34e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRK-TSE--RLETVILDVTKTENIVAATQWVKERVGn 103
Cdd:cd08934    1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADElEAEggKALVLELDVTDEQQVDAAVERTVEALG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 rGLWGLVNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVR-KARGRVVNVSSILGRVSLGGSGGYCISKY 182
Cdd:cd08934   80 -RLDILVNNAGIML-LGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLlRNKGTIVNISSVAGRVAVRNSAVYNATKF 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 226510520 183 GIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:cd08934  158 GVNAFSEGLRQEVTERGVRVVVIEPGTVDT 187
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 32-218 2.13e-37

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: 133.19  E-value: 2.13e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRG-MRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGNRGLWGLV 110
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSAATELAALGASHSRLHILELDVTDEIAESAEAVAERLGDAGLDVLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 111 NNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKA-RGRVVNVSSILGRVS---LGGSGGYCISKYGIEA 186
Cdd:cd05325   81 NNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGaRAKIINISSRVGSIGdntSGGWYSYRASKAALNM 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 226510520 187 FSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:cd05325  161 LTKSLAVELKRDGITVVSLHPGWVRTDMGGPF 192
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 27-214 4.15e-34

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 124.92  E-value: 4.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEE-GAEELRRKTSE---RLETVILDVTKTENIVAATQWVKERVG 102
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEaGAEALVAEIGAlggKALAVQGDVSDAESVERAVDEAKAEFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 nrGLWGLVNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:PRK05557  83 --GVDILVNNAGITR-DNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRsGRIINISSVVGLMGNPGQANYAASK 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:PRK05557 160 AGVIGFTKSLARELASRGITVNAVAPGFIETDM 192
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
27-214 1.02e-33

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 123.73  E-value: 1.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSE---RLETVILDVTKTENIVAATQWVKERVGn 103
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAaggEARVLVFDVSDEAAVRALIEAAVEAFG- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 rGLWGLVNNAGISvPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKY 182
Cdd:PRK05653  82 -ALDILVNNAGIT-RDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARyGRIVNISSVSGVTGNPGQTNYSAAKA 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 226510520 183 GIEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:PRK05653 160 GVIGFTKALALELASRGITVNAVAPGFIDTDM 191
PRK09291 PRK09291
SDR family oxidoreductase;
30-219 1.24e-33

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 123.95  E-value: 1.24e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSER---LETVILDVTKTENIVAATQW---Vkervgn 103
Cdd:PRK09291   3 KTILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRglaLRVEKLDLTDAIDRAQAAEWdvdV------ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 rglwgLVNNAGI----SVPSGPNEWMKKQdfasvLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYC 178
Cdd:PRK09291  77 -----LLNNAGIgeagAVVDIPVELVREL-----FETNVFGPLELTQGFVRkMVARGKGKVVFTSSMAGLITGPFTGAYC 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 226510520 179 ISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTG----MASSAR 219
Cdd:PRK09291 147 ASKHALEAIAEAMHAELKPFGIQVATVNPGPYLTGfndtMAETPK 191
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 33-217 1.96e-33

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 123.99  E-value: 1.96e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  33 FITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGNrgLWGLVNN 112
Cdd:PRK08263   7 FITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGR--LDIVVNN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 113 AGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKYGIEAFSDSL 191
Cdd:PRK08263  85 AGYGL-FGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRsGHIIQISSIGGISAFPMSGIYHASKWALEGMSEAL 163

                        170       180
                 ....*....|....*....|....*.
gi 226510520 192 RRELRYFGVKVAIIEPGFFLTGMASS 217
Cdd:PRK08263 164 AQEVAEFGIKVTLVEPGGYSTDWAGT 189
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 27-218 4.99e-33

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: 121.75  E-value: 4.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGM-RVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKErvgnrg 105
Cdd:cd05354    1 IKDKTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAAQAKD------ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 106 LWGLVNNAGISVPSGPnewMKKQDFASV---LDVNLLGLIEVTLSMLPLVRKA-RGRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:cd05354   75 VDVVINNAGVLKPATL---LEEGALEALkqeMDVNVFGLLRLAQAFAPVLKANgGGAIVNLNSVASLKNFPAMGTYSASK 151

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:cd05354  152 SAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGA 188
PRK12826 PRK12826
SDR family oxidoreductase;
27-215 1.07e-32

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 121.56  E-value: 1.07e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSE---RLETVILDVTKTENIVAATQWVKERVGn 103
Cdd:PRK12826   4 LEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAaggKARARQVDVRDRAALKAAVAAGVEDFG- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 rGLWGLVNNAGISvPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGR-VSLGGSGGYCISK 181
Cdd:PRK12826  83 -RLDILVANAGIF-PLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPaLIRAGGGRIVLTSSVAGPrVGYPGLAHYAASK 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMA 215
Cdd:PRK12826 161 AGLVGFTRALALELAARNITVNSVHPGGVDTPMA 194
PRK05650 PRK05650
SDR family oxidoreductase;
32-219 8.05e-32

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 119.76  E-value: 8.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSE---RLETVILDVTKTENIVAATQWVKERVGnrGLWG 108
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREaggDGFYQRCDVRDYSQLTALAQACEEKWG--GIDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 109 LVNNAGISVPSGPNEwMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKYGIEAF 187
Cdd:PRK05650  81 IVNNAGVASGGFFEE-LSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKsGRIVNIASMAGLMQGPAMSSYNVAKAGVVAL 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 226510520 188 SDSLRRELRYFGVKVAIIEPGFFLTGMASSAR 219
Cdd:PRK05650 160 SETLLVELADDEIGVHVVCPSFFQTNLLDSFR 191
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 30-218 1.08e-31

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


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 118.11  E-value: 1.08e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGM-RVLAACRK----EEGAEELRrktSERL--ETVILDVTKTENIVAATQWVKERVG 102
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPgTVILTARDvergQAAVEKLR---AEGLsvRFHQLDVTDDASIEAAADFVEEKYG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 nrGLWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLggsgGYCISK 181
Cdd:cd05324   78 --GLDILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPaGRIVNVSSGLGSLTS----AYGVSK 151

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:cd05324  152 AALNALTRILAKELKETGIKVNACCPGWVKTDMGGGK 188
PRK05693 PRK05693
SDR family oxidoreductase;
32-218 4.17e-31

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 117.97  E-value: 4.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELrrkTSERLETVILDVTKTENIVAATQWVKERVGnrGLWGLVN 111
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEAL---AAAGFTAVQLDVNDGAALARLAEELEAEHG--GLDVLIN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 112 NAGISV--P--SGPNEWMKKQdfasvLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEAF 187
Cdd:PRK05693  79 NAGYGAmgPllDGGVEAMRRQ-----FETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHAL 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 226510520 188 SDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:PRK05693 154 SDALRLELAPFGVQVMEVQPGAIASQFASNA 184
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 30-214 6.36e-31

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: 116.49  E-value: 6.36e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGA---EELRRKTSERLETVILDVTKTENIVAATQWVKERVGnrGL 106
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAaetVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFG--PV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAGIS----VPSgpnewMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:cd05333   79 DILVNNAGITrdnlLMR-----MSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRsGRIINISSVVGLIGNPGQANYAASK 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:cd05333  154 AGVIGFTKSLAKELASRGITVNAVAPGFIDTDM 186
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
30-219 2.50e-30

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 114.86  E-value: 2.50e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGA----EELRRKTSERLETVILDVTKTENIVAATQWVKERVGNRG 105
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCakdwFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGPVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 106 LwgLVNNAGISVPSGPNEwMKKQDFASVLDVNLLGLIEVTLSMLPLVR-KARGRVVNVSSILGRVSLGGSGGYCISKYGI 184
Cdd:PRK12824  83 I--LVNNAGITRDSVFKR-MSHQEWNDVINTNLNSVFNVTQPLFAAMCeQGYGRIINISSVNGLKGQFGQTNYSAAKAGM 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226510520 185 EAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSAR 219
Cdd:PRK12824 160 IGFTKALASEGARYGITVNCIAPGYIATPMVEQMG 194
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 30-217 3.50e-30

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: 114.14  E-value: 3.50e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGnrGLWGL 109
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFG--GLDAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 110 VNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTL-SMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEAFS 188
Cdd:cd08929   79 VNNAGVGV-MKPVEELTPEEWRLVLDTNLTGAFYCIHkAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLS 157

                        170       180
                 ....*....|....*....|....*....
gi 226510520 189 DSLRRELRYFGVKVAIIEPGFFLTGMASS 217
Cdd:cd08929  158 EAAMLDLREANIRVVNVMPGSVDTGFAGS 186
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 27-206 4.58e-30

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: 114.10  E-value: 4.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTsERLETVILDVTKTENIVAATQWVKERVGnrGL 106
Cdd:COG3967    3 LTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAAN-PGLHTIVLDVADPASIAALAEQVTAEFP--DL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAGISVP----SGPNEWmkkQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:COG3967   80 NVLINNAGIMRAedllDEAEDL---ADAEREITTNLLGPIRLTAAFLPhLKAQPEAAIVNVSSGLAFVPLAVTPTYSATK 156

                        170       180
                 ....*....|....*....|....*
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVaiIE 206
Cdd:COG3967  157 AALHSYTQSLRHQLKDTSVKV--IE 179
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 30-208 5.45e-30

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: 114.30  E-value: 5.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRK----EEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGNrg 105
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRaerlQELADELGAKFPVKVLPLQLDVSDRESIEAALENLPEEFRD-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 106 LWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISKYGI 184
Cdd:cd05346   79 IDILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPiMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAV 158

                        170       180
                 ....*....|....*....|....
gi 226510520 185 EAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:cd05346  159 RQFSLNLRKDLIGTGIRVTNIEPG 182
PRK06482 PRK06482
SDR family oxidoreductase;
33-219 9.97e-30

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 114.06  E-value: 9.97e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  33 FITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGNRGLwgLVNN 112
Cdd:PRK06482   6 FITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAALGRIDV--VVSN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 113 AGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARG-RVVNVSSILGRVSLGGSGGYCISKYGIEAFSDSL 191
Cdd:PRK06482  84 AGYGL-FGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGgRIVQVSSEGGQIAYPGFSLYHATKWGIEGFVEAV 162

                        170       180
                 ....*....|....*....|....*...
gi 226510520 192 RRELRYFGVKVAIIEPGFFLTGMASSAR 219
Cdd:PRK06482 163 AQEVAPFGIEFTIVEPGPARTNFGAGLD 190
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 30-224 1.10e-29

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: 112.84  E-value: 1.10e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKtSERLETVILDVTKTENIVAATQWVKERVGnrGLWGL 109
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS-GGDVEAVPYDARDPEDARALVDALRDRFG--RIDVL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 110 VNNAGISVPSGPNEWMKKQDfASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEAFS 188
Cdd:cd08932   78 VHNAGIGRPTTLREGSDAEL-EAHFSINVIAPAELTRALLPaLREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALA 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226510520 189 DSLRRELRYFGVKVAIIEPGFFLTGMASSARLCSNI 224
Cdd:cd08932  157 HALRQEGWDHGVRVSAVCPGFVDTPMAQGLTLVGAF 192
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 29-212 1.10e-29

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


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 113.12  E-value: 1.10e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  29 DKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKE----EGAEELRRK---TSERLETVILDVTKTENIVAATQWVKERV 101
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSEskleEAVEEIEAEanaSGQKVSYISADLSDYEEVEQAFAQAVEKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 102 GNRGLwgLVNNAGISVPsGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCIS 180
Cdd:cd08939   81 GPPDL--VVNCAGISIP-GLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRpGHIVFVSSQAALVGIYGYSAYCPS 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 226510520 181 KYGIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:cd08939  158 KFALRGLAESLRQELKPYNIRVSVVYPPDTDT 189
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 32-214 1.43e-29

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: 112.72  E-value: 1.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELR---RKTSERLETVILDVTKTENIVAATQWVKERVGNRGLwg 108
Cdd:cd05339    2 VLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETAnnvRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTI-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 109 LVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEAF 187
Cdd:cd05339   80 LINNAGV-VSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPdMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGF 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 226510520 188 SDSLRRELRYF---GVKVAIIEPGFFLTGM 214
Cdd:cd05339  159 HESLRLELKAYgkpGIKTTLVCPYFINTGM 188
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 27-219 1.87e-29

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 113.91  E-value: 1.87e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRK--TSERLETVILDVTKTENIVAATQWVKERVGnr 104
Cdd:PRK05872   7 LAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAElgGDDRVLTVVADVTDLAAMQAAAEEAVERFG-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 105 GLWGLVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISKYGI 184
Cdd:PRK05872  85 GIDVVVANAGI-ASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSLAAFAAAPGMAAYCASKAGV 163

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226510520 185 EAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSAR 219
Cdd:PRK05872 164 EAFANALRLEVAHHGVTVGSAYLSWIDTDLVRDAD 198
PRK09072 PRK09072
SDR family oxidoreductase;
26-218 2.92e-29

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 112.73  E-value: 2.92e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  26 HLQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTS--ERLETVILDVTKTENIVAATQWVKErvgN 103
Cdd:PRK09072   2 DLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPypGRHRWVVADLTSEAGREAVLARARE---M 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 RGLWGLVNNAGISVPSgpneWMKKQDFASV---LDVNLLGLIEVTLSMLPLVRKA-RGRVVNVSSILGRVSLGGSGGYCI 179
Cdd:PRK09072  79 GGINVLINNAGVNHFA----LLEDQDPEAIerlLALNLTAPMQLTRALLPLLRAQpSAMVVNVGSTFGSIGYPGYASYCA 154

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 226510520 180 SKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:PRK09072 155 SKFALRGFSEALRRELADTGVRVLYLAPRATRTAMNSEA 193
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 32-212 7.51e-29

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: 110.55  E-value: 7.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGMRVLAACRKEEG----AEELRRKTSERLeTVILDVTKTENIVAATQWVKERVGNRGLW 107
Cdd:cd05360    3 VVITGASSGIGRATALAFAERGAKVVLAARSAEAlhelAREVRELGGEAI-AVVADVADAAQVERAADTAVERFGRIDTW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 108 glVNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEA 186
Cdd:cd05360   82 --VNNAGVAV-FGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPhLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRG 158

                        170       180
                 ....*....|....*....|....*...
gi 226510520 187 FSDSLRRELRYFGVKVAI--IEPGFFLT 212
Cdd:cd05360  159 FTESLRAELAHDGAPISVtlVQPTAMNT 186
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 39-217 7.84e-29

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: 110.60  E-value: 7.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520   39 SGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVI-LDVTKTENIVAATQWVKERVGnrGLWGLVNNAGISV 117
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAEELGAAVLpCDVTDEEQVEALVAAAVEKFG--RLDILVNNAGFAP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  118 P-SGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLvRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEAFSDSLRRELR 196
Cdd:pfam13561  84 KlKGPFLDTSREDFDRALDVNLYSLFLLAKAALPL-MKEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELG 162

                         170       180
                  ....*....|....*....|.
gi 226510520  197 YFGVKVAIIEPGFFLTGMASS 217
Cdd:pfam13561 163 PRGIRVNAISPGPIKTLAASG 183
PRK08264 PRK08264
SDR family oxidoreductase;
26-218 3.02e-28

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 109.21  E-value: 3.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  26 HLQDKYVFITGCGSGFGNLLARQLDRRG-MRVLAACRKEEGAEELrrktSERLETVILDVTKTENIVAATqwvkERVGNR 104
Cdd:PRK08264   3 DIKGKVVLVTGANRGIGRAFVEQLLARGaAKVYAAARDPESVTDL----GPRVVPLQLDVTDPASVAAAA----EAASDV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 105 GLwgLVNNAGISVPSGPnewMKKQDFASV---LDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCIS 180
Cdd:PRK08264  75 TI--LVNNAGIFRTGSL---LLEGDEDALraeMETNYFGPLAMARAFAPvLAANGGGAIVNVLSVLSWVNFPNLGTYSAS 149

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 226510520 181 KYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:PRK08264 150 KAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAAGL 187
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 32-214 3.62e-28

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: 109.22  E-value: 3.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520   32 VFITGCGSGFGNLLARQLDRRGMRVLAACR-KEEGAEELR---RKTSERLETVILDVTKTENIVAATQWVKERVGnrGLW 107
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRsSEEGAEEVVeelKALGVKALGVVLDVSDREDVKAVVEEIEEELG--TID 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  108 GLVNNAGISvPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGrvsLGGSGG---YCISKYG 183
Cdd:TIGR01830  79 ILVNNAGIT-RDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRsGRIINISSVVG---LMGNAGqanYAASKAG 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 226510520  184 IEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:TIGR01830 155 VIGFTKSLAKELASRNITVNAVAPGFIDTDM 185
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 27-207 5.23e-28

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 110.78  E-value: 5.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEG----AEELRRKTSERLeTVILDVTKTENIVAATQWVKERVG 102
Cdd:PRK07109   6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGlealAAEIRAAGGEAL-AVVADVADAEAVQAAADRAEEELG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 NRGLWglVNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:PRK07109  85 PIDTW--VNNAMVTV-FGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRhMRPRDRGAIIQVGSALAYRSIPLQSAYCAAK 161

                        170       180
                 ....*....|....*....|....*...
gi 226510520 182 YGIEAFSDSLRRELRYFG--VKVAIIEP 207
Cdd:PRK07109 162 HAIRGFTDSLRCELLHDGspVSVTMVQP 189
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 27-219 9.33e-28

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: 107.78  E-value: 9.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSErLETVILDVTKTENIVAATQWVKERvgNRGL 106
Cdd:cd05370    3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN-IHTIVLDVGDAESVEALAEALLSE--YPNL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAGISVP---SGPNEWMkkQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISKY 182
Cdd:cd05370   80 DILINNAGIQRPidlRDPASDL--DKADTEIDTNLIGPIRLIKAFLPhLKKQPEATIVNVSSGLAFVPMAANPVYCATKA 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226510520 183 GIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSAR 219
Cdd:cd05370  158 ALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERR 194
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 25-216 6.00e-27

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 106.56  E-value: 6.00e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  25 DHLQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEElrrkTSERLETVI---LDVTKTENIVAATQWVkerv 101
Cdd:PRK07825   1 DDLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKE----TAAELGLVVggpLDVTDPASFAAFLDAV---- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 102 gnRGLWG----LVNNAGIsVPSGPnewMKKQDFASV---LDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGG 173
Cdd:PRK07825  73 --EADLGpidvLVNNAGV-MPVGP---FLDEPDAVTrriLDVNVYGVILGSKLAAPrMVPRGRGHVVNVASLAGKIPVPG 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 226510520 174 SGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMAS 216
Cdd:PRK07825 147 MATYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELIA 189
PRK07326 PRK07326
SDR family oxidoreductase;
27-208 6.58e-27

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 105.48  E-value: 6.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVIL--DVTKTENIVAATQWVKERVGnr 104
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGNVLGLaaDVRDEADVQRAVDAIVAAFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 105 GLWGLVNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISKYGI 184
Cdd:PRK07326  82 GLDVLIANAGVGH-FAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGTNFFAGGAAYNASKFGL 160

                        170       180
                 ....*....|....*....|....
gi 226510520 185 EAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:PRK07326 161 VGFSEAAMLDLRQYGIKVSTIMPG 184
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 30-282 3.87e-26

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: 104.08  E-value: 3.87e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDR---RGMRVLAACR----KEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVG 102
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLASdpsKRFKVYATMRdlkkKGRLWEAAGALAGGTLETLQLDVCDSKSVAAAVERVTERHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 NRglwgLVNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:cd09806   81 DV----LVCNAGVGL-LGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGsGRILVTSSVGGLQGLPFNDVYCASK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSArLCSNIQMLWDQTSSEIREIYGEKYLASYLKNLNELDQRCNKd 261
Cdd:cd09806  156 FALEGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKV-LGSPEEVLDRTADDITTFHFFYQYLAHSKQVFREAAQNPEE- 233

                        250       260
                 ....*....|....*....|.
gi 226510520 262 lsvVTDCMEHALTACHPRTRY 282
Cdd:cd09806  234 ---VAEVFLTAIRAPKPPLRY 251
PRK07832 PRK07832
SDR family oxidoreductase;
30-220 5.33e-26

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 103.97  E-value: 5.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEG----AEELRRKTSERLETVILDVTKTENIVAATQWVKERVGNRG 105
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGlaqtVADARALGGTVPEHRALDISDYDAVAAFAADIHAAHGSMD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 106 LwgLVNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGR-VVNVSSILGRVSLGGSGGYCISKYG 183
Cdd:PRK07832  81 V--VMNIAGISA-WGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPpMVAAGRGGhLVNVSSAAGLVALPWHAAYSASKFG 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226510520 184 IEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSARL 220
Cdd:PRK07832 158 LRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVNTVEI 194
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 20-208 6.31e-26

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 103.60  E-value: 6.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  20 ERQVVDHLQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLET-VILDVTKTENIVAATQWVK 98
Cdd:PRK12829   2 AIDLLKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPGAKVTaTVADVADPAQVERVFDTAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  99 ERVGnrGLWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKA-RGRVV-NVSSILGRVSLGGSGG 176
Cdd:PRK12829  82 ERFG--GLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASgHGGVIiALSSVAGRLGYPGRTP 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 226510520 177 YCISKYGIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:PRK12829 160 YAASKWAVVGLVKSLAIELGPLGIRVNAILPG 191
PRK07024 PRK07024
SDR family oxidoreductase;
32-214 8.83e-26

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 103.09  E-value: 8.83e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRK--TSERLETVILDVTKTENIVAATQWVKERVGNRGLwgL 109
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARlpKAARVSVYAADVRDADALAAAAADFIAAHGLPDV--V 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 110 VNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSML-PLVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEAFS 188
Cdd:PRK07024  83 IANAGISVGTLTEEREDLAVFREVMDTNYFGMVATFQPFIaPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIKYL 162

                        170       180
                 ....*....|....*....|....*.
gi 226510520 189 DSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:PRK07024 163 ESLRVELRPAGVRVVTIAPGYIRTPM 188
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-218 9.19e-26

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 103.02  E-value: 9.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRK-EEGAEELRRK---TSERLETVILDVTKTENIVAATQWVKERVG 102
Cdd:PRK12825   4 LMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSdEEAAEELVEAveaLGRRAQAVQADVTDKAALEAAVAAAVERFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 nrGLWGLVNNAGISvPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:PRK12825  84 --RIDILVNNAGIF-EDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRgGRIVNISSVAGLPGWPGRSNYAAAK 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:PRK12825 161 AGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEAT 197
PRK06181 PRK06181
SDR family oxidoreductase;
29-212 1.60e-25

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 102.75  E-value: 1.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  29 DKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEG----AEELRRKTSERLeTVILDVTKTENIVAATQWVKERVGnr 104
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRlaslAQELADHGGEAL-VVPTDVSDAEACERLIEAAVARFG-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 105 GLWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISKYGI 184
Cdd:PRK06181  78 GIDILVNNAGITMWSRFDELTDLSVFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTRSGYAASKHAL 157

                        170       180
                 ....*....|....*....|....*...
gi 226510520 185 EAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:PRK06181 158 HGFFDSLRIELADDGVAVTVVCPGFVAT 185
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 27-218 4.89e-25

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: 100.95  E-value: 4.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRK------TSERLETVILDVTKTENIVAATQWVKER 100
Cdd:cd05364    1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSclqagvSEKKILLVVADLTEEEGQDRIISTTLAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 101 VGNRGLwgLVNNAGISVPsGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCIS 180
Cdd:cd05364   81 FGRLDI--LVNNAGILAK-GGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGRSFPGVLYYCIS 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 226510520 181 KYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:cd05364  158 KAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRM 195
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 27-214 7.13e-25

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: 100.54  E-value: 7.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGnrGL 106
Cdd:cd05341    3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFG--RL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAGISVPsGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKA-RGRVVNVSSILGRVSLGGSGGYCISKYGIE 185
Cdd:cd05341   81 DVLVNNAGILTG-GTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAgGGSIINMSSIEGLVGDPALAAYNASKGAVR 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 226510520 186 AFSDSLRRELR--YFGVKVAIIEPGFFLTGM 214
Cdd:cd05341  160 GLTKSAALECAtqGYGIRVNSVHPGYIYTPM 190
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 27-215 1.14e-24

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: 99.74  E-value: 1.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSE---RLETVILDVTKTENIVAATQWVKERVGN 103
Cdd:cd05347    3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKegvEATAFTCDVSDEEAIKAAVEAIEEDFGK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 RGLwgLVNNAGISVPSgPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISKY 182
Cdd:cd05347   83 IDI--LVNNAGIIRRH-PAEEFPEAEWRDVIDVNLNGVFFVSQAVARhMIKQGHGKIINICSLLSELGGPPVPAYAASKG 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226510520 183 GIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMA 215
Cdd:cd05347  160 GVAGLTKALATEWARHGIQVNAIAPGYFATEMT 192
FabG-like PRK07231
SDR family oxidoreductase;
27-247 2.41e-24

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 99.13  E-value: 2.41e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEElrrkTSERLET------VILDVTKTENIVAATQWVKER 100
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAER----VAAEILAggraiaVAADVSDEADVEAAVAAALER 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 101 VGnrGLWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCI 179
Cdd:PRK07231  79 FG--SVDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGgGAIVNVASTAGLRPRPGLGWYNA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226510520 180 SKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSarlcsniqmLWDQTSSEIReiygEKYLASY 247
Cdd:PRK07231 157 SKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEA---------FMGEPTPENR----AKFLATI 211
PRK06484 PRK06484
short chain dehydrogenase; Validated
 32-223 2.72e-24

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 102.62  E-value: 2.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGNRGLwgLVN 111
Cdd:PRK06484 272 VAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRLDV--LVN 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 112 NAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKArGRVVNVSSILGRVSLGGSGGYCISKYGIEAFSDSL 191
Cdd:PRK06484 350 NAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG-GVIVNLGSIASLLALPPRNAYCASKAAVTMLSRSL 428

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226510520 192 RRELRYFGVKVAIIEPGFFLT----GMASSARLCSN 223
Cdd:PRK06484 429 ACEWAPAGIRVNTVAPGYIETpavlALKASGRADFD 464
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 30-223 3.78e-24

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: 97.91  E-value: 3.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKT-SERLETVILDVTKTENIVAATQWVKERVGNRgLWG 108
Cdd:cd08931    1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELgAENVVAGALDVTDRAAWAAALADFAAATGGR-LDA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 109 LVNNAGISvPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARG-RVVNVSSILGRVSLGGSGGYCISKYGIEAF 187
Cdd:cd08931   80 LFNNAGVG-RGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGaRVINTASSSAIYGQPDLAVYSATKFAVRGL 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226510520 188 SDSLRRELRYFGVKVAIIEPGFFLTGMASSARLCSN 223
Cdd:cd08931  159 TEALDVEWARHGIRVADVWPWFVDTPILTKGETGAA 194
PRK08219 PRK08219
SDR family oxidoreductase;
34-214 1.38e-23

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 96.54  E-value: 1.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  34 ITGCGSGFGNLLARQLDRRgMRVLAACRKEEGAEELRrKTSERLETVILDVTKTENIVAATQWVkERVGNrglwgLVNNA 113
Cdd:PRK08219   8 ITGASRGIGAAIARELAPT-HTLLLGGRPAERLDELA-AELPGATPFPVDLTDPEAIAAAVEQL-GRLDV-----LVHNA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 114 GISVPsGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEAFSDSLRR 193
Cdd:PRK08219  80 GVADL-GPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRANPGWGSYAASKFALRALADALRE 158

                        170       180
                 ....*....|....*....|.
gi 226510520 194 ELRYfGVKVAIIEPGFFLTGM 214
Cdd:PRK08219 159 EEPG-NVRVTSVHPGRTDTDM 178
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 30-219 3.19e-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: 95.83  E-value: 3.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKE--EGAEELRRKTSE-RLETVILDVTKTENIVAATQWVKERVGnrGL 106
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNEnpGAAAELQAINPKvKATFVQCDVTSWEQLAAAFKKAIEKFG--RV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAGISVPSGPNEWMK-KQDFASVLDVNLLGLIEVTLSMLPLVRKAR----GRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:cd05323   79 DILINNAGILDEKSYLFAGKlPPPWEKTIDVNLTGVINTTYLALHYMDKNKggkgGVIVNIGSVAGLYPAPQFPVYSASK 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 226510520 182 YGIEAFSDSLRRELRY-FGVKVAIIEPGFFLTGMASSAR 219
Cdd:cd05323  159 HGVVGFTRSLADLLEYkTGVRVNAICPGFTNTPLLPDLV 197
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 32-215 8.53e-23

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: 94.70  E-value: 8.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSE---RLETVILDVTKTENIVAATQWVKERVGnrGLWG 108
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNpnpSVEVEILDVTDEERNQLVIAELEAELG--GLDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 109 LVNNAGISVPSgPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEAF 187
Cdd:cd05350   79 VIINAGVGKGT-SLGDLSFKAFRETIDTNLLGAAAILEAALPqFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSL 157

                        170       180
                 ....*....|....*....|....*...
gi 226510520 188 SDSLRRELRYFGVKVAIIEPGFFLTGMA 215
Cdd:cd05350  158 AESLRYDVKKRGIRVTVINPGFIDTPLT 185
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 27-218 2.07e-22

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: 93.71  E-value: 2.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGnrGL 106
Cdd:cd08944    1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFG--GL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVR-KARGRVVNVSSILGRVSLGGSGGYCISKYGIE 185
Cdd:cd08944   79 DLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIaRGGGSIVNLSSIAGQSGDPGYGAYGASKAAIR 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226510520 186 AFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:cd08944  159 NLTRTLAAELRHAGIRCNALAPGLIDTPLLLAK 191
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 27-212 3.62e-22

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 93.11  E-value: 3.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSE---RLETVILDVTKTENIVAATQWVKERVGn 103
Cdd:PRK12939   5 LAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAaggRAHAIAADLADPASVQRFFDAAAAALG- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 rGLWGLVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVR-KARGRVVNVSSILGRVSLGGSGGYCISKY 182
Cdd:PRK12939  84 -GLDGLVNNAGI-TNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRdSGRGRIVNLASDTALWGAPKLGAYVASKG 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 226510520 183 GIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:PRK12939 162 AVIGMTRSLARELGGRGITVNAIAPGLTAT 191
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-220 7.45e-22

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 92.06  E-value: 7.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEG----AEELRrKTSERLETVILDVTKTENIVAATQWVKERVG 102
Cdd:PRK07666   5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENlkavAEEVE-AYGVKVVIATADVSDYEEVTAAIEQLKNELG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 NRGLwgLVNNAGISVPSG-----PNEWMKkqdfasVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGG 176
Cdd:PRK07666  84 SIDI--LINNAGISKFGKfleldPAEWEK------IIQVNLMGVYYATRAVLPsMIERQSGDIINISSTAGQKGAAVTSA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 226510520 177 YCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSARL 220
Cdd:PRK07666 156 YSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDLGL 199
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 30-218 8.23e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 92.09  E-value: 8.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSErlETVILDVTKTENIVAAtqwvkerVGNRGLW-G 108
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGC--EPLRLDVGDDAAIRAA-------LAAAGAFdG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 109 LVNNAGISVPSGPNEwMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKAR-GRVVNVSSILGRVSLGGSGGYCISKYGIEA 186
Cdd:PRK07060  81 LVNCAGIASLESALD-MTAEGFDRVMAVNARGAALVARHVARaMIAAGRgGSIVNVSSQAALVGLPDHLAYCASKAALDA 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 226510520 187 FSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:PRK07060 160 ITRVLCVELGPHGIRVNSVNPTVTLTPMAAEA 191
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 27-218 9.63e-22

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: 92.20  E-value: 9.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSE-----RLETVILDVTKTENIVAATQWVKERV 101
Cdd:cd05330    1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEiapdaEVLLIKADVSDEAQVEAYVDATVEQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 102 GNrgLWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCIS 180
Cdd:cd05330   81 GR--IDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGsGMIVNTASVGGIRGVGNQSGYAAA 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 226510520 181 KYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:cd05330  159 KHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGS 196
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 26-219 3.52e-21

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 90.40  E-value: 3.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  26 HLQDKYVFITGCGSGFGNLLARQLDRRGMRV----LAACRKEEGAEELRRKTSErLETVILDVTKTENIVAATQWVKERV 101
Cdd:PRK08217   2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAKLalidLNQEKLEEAVAECGALGTE-VRGYAANVTDEEDVEATFAQIAEDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 102 GnrGLWGLVNNAGI-------SVPSGP-NEWMKKQDFASVLDVNLLGLI----EVTLSMLPLVRKarGRVVNVSSIlgrv 169
Cdd:PRK08217  81 G--QLNGLINNAGIlrdgllvKAKDGKvTSKMSLEQFQSVIDVNLTGVFlcgrEAAAKMIESGSK--GVIINISSI---- 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 226510520 170 SLGGSGG---YCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSAR 219
Cdd:PRK08217 153 ARAGNMGqtnYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMK 205
PRK07454 PRK07454
SDR family oxidoreductase;
32-208 3.78e-21

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 90.02  E-value: 3.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELR---RKTSERLETVILDVTKTENIVAATQWVKERVGNRGLwg 108
Cdd:PRK07454   9 ALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAaelRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDV-- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 109 LVNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKYGIEAF 187
Cdd:PRK07454  87 LINNAGMAY-TGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGgGLIINVSSIAARNAFPQWGAYCVSKAALAAF 165

                        170       180
                 ....*....|....*....|.
gi 226510520 188 SDSLRRELRYFGVKVAIIEPG 208
Cdd:PRK07454 166 TKCLAEEERSHGIRVCTITLG 186
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-217 4.11e-21

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 90.29  E-value: 4.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRK-EEGAEELRRKTSERLETVIL---DVTKTENIVAATQWVKERVG 102
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDInEEAAQELLEEIKEEGGDAIAvkaDVSSEEDVENLVEQIVEKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 nrGLWGLVNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVslGGSGG--YCI 179
Cdd:PRK05565  83 --KIDILVNNAGISN-FGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPyMIKRKSGVIVNISSIWGLI--GASCEvlYSA 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 226510520 180 SKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASS 217
Cdd:PRK05565 158 SKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSS 195
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 32-208 4.12e-21

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 90.20  E-value: 4.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGNRGLwgLVN 111
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDV--LVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 112 NAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEAFSDS 190
Cdd:PRK10538  81 NAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPgMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLN 160

                        170
                 ....*....|....*...
gi 226510520 191 LRRELRYFGVKVAIIEPG 208
Cdd:PRK10538 161 LRTDLHGTAVRVTDIEPG 178
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 29-214 1.36e-20

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


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 89.21  E-value: 1.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  29 DKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAE----ELRRKT-SERLETVILDVTKTENIVAATQWVKERVgn 103
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEeaaaEIKKETgNAKVEVIQLDLSSLASVRQFAEEFLARF-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 RGLWGLVNNAGISVPSgpnEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRV------------- 169
Cdd:cd05327   79 PRLDILINNAGIMAPP---RRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASApSRIVNVSSIAHRAgpidfndldlenn 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 226510520 170 -SLGGSGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:cd05327  156 kEYSPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTEL 201
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 33-242 2.22e-20

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: 88.36  E-value: 2.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  33 FITGCGSGFGNLLARQLDRRGMRVLAACRKEEG-AEELRRKTSERLET--VILDVTKTENIVAATQWVKERVGNRGLwgL 109
Cdd:cd08945    7 LVTGATSGIGLAIARRLGKEGLRVFVCARGEEGlATTVKELREAGVEAdgRTCDVRSVPEIEALVAAAVARYGPIDV--L 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 110 VNNAGISvPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP---LVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEA 186
Cdd:cd08945   85 VNNAGRS-GGGATAELADELWLDVVETNLTGVFRVTKEVLKaggMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVVG 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226510520 187 FSDSLRRELRYFGVKVAIIEPGFFLTGMASSARlcSNIQMLWDQTSSEIREIYGEK 242
Cdd:cd08945  164 FTKALGLELARTGITVNAVCPGFVETPMAASVR--EHYADIWEVSTEEAFDRITAR 217
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 27-214 3.40e-20

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 87.66  E-value: 3.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGnrGL 106
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEADLE--GV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAGISvPSGPNEWMKKQDFASVLDVNLLGLIEVTLSML-PLVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIE 185
Cdd:PRK12936  82 DILVNNAGIT-KDGLFVRMSDEDWDSVLEVNLTATFRLTRELThPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGMI 160

                        170       180
                 ....*....|....*....|....*....
gi 226510520 186 AFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:PRK12936 161 GFSKSLAQEIATRNVTVNCVAPGFIESAM 189
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 28-214 4.37e-20

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: 87.59  E-value: 4.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  28 QDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRK--TSERLETVIL--DVTKTENIVAATQWVKERVGN 103
Cdd:cd08933    8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESElnRAGPGSCKFVpcDVTKEEDIKTLISVTVERFGR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 rgLWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISKYG 183
Cdd:cd08933   88 --IDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIGQKQAAPYVATKGA 165

                        170       180       190
                 ....*....|....*....|....*....|.
gi 226510520 184 IEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:cd08933  166 ITAMTKALAVDESRYGVRVNCISPGNIWTPL 196
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 27-209 5.00e-20

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 87.32  E-value: 5.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRK---TSERLETVILDVTKTENIVAATQWVKERVGn 103
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEiddLGRRALAVPTDITDEDQCANLVALALERFG- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 rGLWGLVNNAgISVPS-GPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISKY 182
Cdd:PRK07890  82 -RVDALVNNA-FRVPSmKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMINSMVLRHSQPKYGAYKMAKG 159

                        170       180
                 ....*....|....*....|....*..
gi 226510520 183 GIEAFSDSLRRELRYFGVKVAIIEPGF 209
Cdd:PRK07890 160 ALLAASQSLATELGPQGIRVNSVAPGY 186
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 27-218 5.05e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 87.41  E-value: 5.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGNRGL 106
Cdd:PRK06841  13 LSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRIDI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 wgLVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIE 185
Cdd:PRK06841  93 --LVNSAGV-ALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRhMIAAGGGKIVNLASQAGVVALERHVAYCASKAGVV 169

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226510520 186 AFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:PRK06841 170 GMTKVLALEWGPYGITVNAISPTVVLTELGKKA 202
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 31-219 1.46e-19

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


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 85.80  E-value: 1.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  31 YVFITGCGSGFGNLLARQLDRRG--MRVLAACRKEEGAEELRRKTSE--RLETVILDVTKTEN---IVAATQWV-KERVG 102
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGspSVVVLLARSEEPLQELKEELRPglRVTTVKADLSDAAGveqLLEAIRKLdGERDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 nrglwgLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR--GRVVNVSSILGRVSLGGSGGYCIS 180
Cdd:cd05367   81 ------LINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGlkKTVVNVSSGAAVNPFKGWGLYCSS 154

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 226510520 181 KYGIEAFSDSLRRELRyfGVKVAIIEPGFFLTGMASSAR 219
Cdd:cd05367  155 KAARDMFFRVLAAEEP--DVRVLSYAPGVVDTDMQREIR 191
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 27-214 1.52e-19

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: 85.99  E-value: 1.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSErLETVILDVtktenivAATQWVKERVGNRGL 106
Cdd:cd05351    5 FAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPG-IEPVCVDL-------SDWDATEEALGSVGP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 W-GLVNNAGISVPSgPNEWMKKQDFASVLDVNLLGLIEVTLSMLP--LVRKARGRVVNVSSILGRVSLGGSGGYCISKYG 183
Cdd:cd05351   77 VdLLVNNAAVAILQ-PFLEVTKEAFDRSFDVNVRAVIHVSQIVARgmIARGVPGSIVNVSSQASQRALTNHTVYCSTKAA 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 226510520 184 IEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:cd05351  156 LDMLTKVMALELGPHKIRVNSVNPTVVMTDM 186
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
27-219 1.55e-19

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 85.83  E-value: 1.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACrkeeGAEELRR-KTSERLETVILDVTKTENIVA-------ATQWVK 98
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAGC----GPNSPRRvKWLEDQKALGFDFIASEGNVGdwdstkaAFDKVK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  99 ERVGNRGLwgLVNNAGISVPSGPNEwMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGY 177
Cdd:PRK12938  77 AEVGEIDV--LVNNAGITRDVVFRK-MTREDWTAVIDTNLTSLFNVTKQVIDgMVERGWGRIINISSVNGQKGQFGQTNY 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 226510520 178 CISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSAR 219
Cdd:PRK12938 154 STAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIR 195
PRK05855 PRK05855
SDR family oxidoreductase;
29-219 2.06e-19

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 88.50  E-value: 2.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  29 DKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEE---LRRKTSERLETVILDVTKTENIVAATQWVKERVGNRG 105
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERtaeLIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPD 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 106 LwgLVNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKAR-GRVVNVSSILGRVSLGGSGGYCISKYG 183
Cdd:PRK05855 395 I--VVNNAGIGM-AGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRqMVERGTgGHIVNVASAAAYAPSRSLPAYATSKAA 471

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226510520 184 IEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSAR 219
Cdd:PRK05855 472 VLMLSECLRAELAAAGIGVTAICPGFVDTNIVATTR 507
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-214 2.35e-19

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 85.61  E-value: 2.35e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRV-LAACRKEEGAEELRRKTSErleTVILDVTKTENIVAATQWVKERVGNRG 105
Cdd:PRK06463   5 FKGKVALITGGTRGIGRAIAEAFLREGAKVaVLYNSAENEAKELREKGVF---TIKCDVGNRDQVKKSKEVVEKEFGRVD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 106 LwgLVNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILG-RVSLGGSGGYCISKYG 183
Cdd:PRK06463  82 V--LVNNAGIMY-LMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKnGAIVNIASNAGiGTAAEGTTFYAITKAG 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 226510520 184 IEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:PRK06463 159 IIILTRRLAFELGKYGIRVNAVAPGWVETDM 189
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 24-216 2.40e-19

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: 85.64  E-value: 2.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  24 VDHLQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRK-TSERLETVI---LDVTKTENIVAATQWVKE 99
Cdd:cd05343    1 MERWRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAEcQSAGYPTLFpyqCDLSNEEQILSMFSAIRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 100 RVGnrGLWGLVNNAGISVP----SGPNEWMKKqdfasVLDVNLLGLIEVT---LSMLPLVRKARGRVVNVSSILG-RVSL 171
Cdd:cd05343   81 QHQ--GVDVCINNAGLARPepllSGKTEGWKE-----MFDVNVLALSICTreaYQSMKERNVDDGHIININSMSGhRVPP 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 226510520 172 GGSGG-YCISKYGIEAFSDSLRRELRYF--GVKVAIIEPGFFLTGMAS 216
Cdd:cd05343  154 VSVFHfYAATKHAVTALTEGLRQELREAktHIRATSISPGLVETEFAF 201
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 27-239 2.90e-19

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: 84.94  E-value: 2.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEG----AEELRRKTSERLETVILDVTK--TENIVAATQWVKER 100
Cdd:cd05340    2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKlrqvADHINEEGGRQPQWFILDLLTctSENCQQLAQRIAVN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 101 VGNrgLWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCI 179
Cdd:cd05340   82 YPR--LDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQGRANWGAYAV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 180 SKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSARLCSNIQMLwdQTSSEIREIY 239
Cdd:cd05340  160 SKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRASAFPTEDPQKL--KTPADIMPLY 217
PRK08267 PRK08267
SDR family oxidoreductase;
30-215 3.94e-19

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 84.99  E-value: 3.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRK-TSERLETVILDVTKtenivaATQWvKERVGNRGLWG 108
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAElGAGNAWTGALDVTD------RAAW-DAALADFAAAT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 109 ------LVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARG-RVVNVSSILGrvsLGGSGG---YC 178
Cdd:PRK08267  75 ggrldvLFNNAGI-LRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGaRVINTSSASA---IYGQPGlavYS 150

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226510520 179 ISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMA 215
Cdd:PRK08267 151 ATKFAVRGLTEALDLEWRRHGIRVADVMPLFVDTAML 187
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 27-217 8.24e-19

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 83.90  E-value: 8.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRK-EEGAEELRRKTSERLETVIL---DVTKTENivaATQWVKERVG 102
Cdd:PRK12935   4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSsKEAAENLVNELGKEGHDVYAvqaDVSKVED---ANRLVEEAVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 NRG-LWGLVNNAGISVPSGPNEwMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCIS 180
Cdd:PRK12935  81 HFGkVDILVNNAGITRDRTFKK-LNREDWERVIDVNLSSVFNTTSAVLPYITEAEeGRIISISSIIGQAGGFGQTNYSAA 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226510520 181 KYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASS 217
Cdd:PRK12935 160 KAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAE 196
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 29-213 1.26e-18

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: 83.48  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  29 DKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEG---AEELRRKTSERLETVILDVTKTENIVAATQWVKERVGnrG 105
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENlerAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFG--R 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 106 LWGLVNNAGiSVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRV---SLGGSGgycISK 181
Cdd:cd05344   79 VDILVNNAG-GPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLTVKEpepNLVLSN---VAR 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPGFFLTG 213
Cdd:cd05344  155 AGLIGLVKTLSRELAPDGVTVNSVLPGYIDTE 186
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 27-208 1.40e-18

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: 83.20  E-value: 1.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACR-KEEGAEELRR-KTSERLETVIL--DVTKTENIVAATQWVKERVG 102
Cdd:cd05358    1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRsKEDAAEEVVEeIKAVGGKAIAVqaDVSKEEDVVALFQSAIKEFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 NRGLWglVNNAGISVPSGPNEwMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR--GRVVNVSSILGRVSLGGSGGYCIS 180
Cdd:cd05358   81 TLDIL--VNNAGLQGDASSHE-MTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKikGKIINMSSVHEKIPWPGHVNYAAS 157

                        170       180
                 ....*....|....*....|....*...
gi 226510520 181 KYGIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:cd05358  158 KGGVKMMTKTLAQEYAPKGIRVNAIAPG 185
PRK06194 PRK06194
hypothetical protein; Provisional
 27-219 2.52e-18

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 83.14  E-value: 2.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMR-VLAACRK---EEGAEELRRKTSERLeTVILDVTKTENIVAATQWVKERVG 102
Cdd:PRK06194   4 FAGKVAVITGAASGFGLAFARIGAALGMKlVLADVQQdalDRAVAELRAQGAEVL-GVRTDVSDAAQVEALADAALERFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 NRGLwgLVNNAGisVPSGPNEW-MKKQDFASVLDVNLLGLIEVTLSMLPLVRKA-------RGRVVNVSSILGRVSLGGS 174
Cdd:PRK06194  83 AVHL--LFNNAG--VGAGGLVWeNSLADWEWVLGVNLWGVIHGVRAFTPLMLAAaekdpayEGHIVNTASMAGLLAPPAM 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 226510520 175 GGYCISKYGIEAFSDSLRRELRYFG--VKVAIIEPGFFLTGMASSAR 219
Cdd:PRK06194 159 GIYNVSKHAVVSLTETLYQDLSLVTdqVGASVLCPYFVPTGIWQSER 205
PRK08628 PRK08628
SDR family oxidoreductase;
26-205 3.08e-18

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 82.70  E-value: 3.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  26 HLQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEG---AEELRRKTSeRLETVILDVTKTENIVAATQWVKERVG 102
Cdd:PRK08628   4 NLKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDdefAEELRALQP-RAEFVQVDLTDDAQCRDAVEQTVAKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 nrGLWGLVNNAG----ISVPSGPnewmkkQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYC 178
Cdd:PRK08628  83 --RIDGLVNNAGvndgVGLEAGR------EAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISSKTALTGQGGTSGYA 154

                        170       180
                 ....*....|....*....|....*...
gi 226510520 179 ISKYGIEAFSDSLRRELRYFGVKV-AII 205
Cdd:PRK08628 155 AAKGAQLALTREWAVALAKDGVRVnAVI 182
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 27-220 3.44e-18

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: 82.12  E-value: 3.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVI-LDVTKTENIVAATQWVKERVGNrg 105
Cdd:cd05326    2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFVhCDVTVEADVRAAVDTAVARFGR-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 106 LWGLVNNAGI-SVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKYG 183
Cdd:cd05326   80 LDIMFNNAGVlGAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKkGSIVSVASVAGVVGGLGPHAYTASKHA 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226510520 184 IEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSARL 220
Cdd:cd05326  160 VLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFG 196
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 30-242 3.53e-18

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: 82.42  E-value: 3.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRV-LAACRKEEGAEELRRKTSE---RLETVILDVTKTENIVAATQWVKERVGnrG 105
Cdd:cd05366    3 KVAIITGAAQGIGRAIAERLAADGFNIvLADLNLEEAAKSTIQEISEagyNAVAVGADVTDKDDVEALIDQAVEKFG--S 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 106 LWGLVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGlieVTLSMLPLVRK-----ARGRVVNVSSILGRVSLGGSGGYCIS 180
Cdd:cd05366   81 FDVMVNNAGI-APITPLLTITEEDLKKVYAVNVFG---VLFGIQAAARQfkklgHGGKIINASSIAGVQGFPNLGAYSAS 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226510520 181 KYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMassarlcsniqmlWDQTSSEIREIYGEK 242
Cdd:cd05366  157 KFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEM-------------WDYIDEEVGEIAGKP 205
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 27-215 4.90e-18

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 81.92  E-value: 4.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRK-TSERLETVIL--DVTKTENIVAATQWVKERVGN 103
Cdd:PRK08213  10 LSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHlEALGIDALWIaaDVADEADIERLAEETLERFGH 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 RGLwgLVNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVT-----LSMLPlvRKArGRVVNVSSILGrvsLGGSG--- 175
Cdd:PRK08213  90 VDI--LVNNAGATW-GAPAEDHPVEAWDKVMNLNVRGLFLLSqavakRSMIP--RGY-GRIINVASVAG---LGGNPpev 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 226510520 176 ----GYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMA 215
Cdd:PRK08213 161 mdtiAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMT 204
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 27-212 4.97e-18

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 81.86  E-value: 4.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGA---EELRRKTSERLETVILDVTKTENIVAATQWVKERVGn 103
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAaaaAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 rGLWGLVNNAGISVPSgPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKY 182
Cdd:PRK12429  81 -GVDILVNNAGIQHVA-PIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGgGRIINMASVHGLVGSAGKAAYVSAKH 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 226510520 183 GIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:PRK12429 159 GLIGLTKVVALEGATHGVTVNAICPGYVDT 188
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 27-214 6.17e-18

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


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 81.55  E-value: 6.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRV-LAACRKEEGAEELR---RKTSERLETVILDVTKTENIVAATQWVKERVG 102
Cdd:cd05362    1 LAGKVALVTGASRGIGRAIAKRLARDGASVvVNYASSKAAAEEVVaeiEAAGGKAIAVQADVSDPSQVARLFDAAEKAFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 nrGLWGLVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRkARGRVVNVSSILGRVSLGGSGGYCISKY 182
Cdd:cd05362   81 --GVDILVNNAGV-MLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLR-DGGRIINISSSLTAAYTPNYGAYAGSKA 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 226510520 183 GIEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:cd05362  157 AVEAFTRVLAKELGGRGITVNAVAPGPVDTDM 188
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 29-214 1.03e-17

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


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 80.73  E-value: 1.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  29 DKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEG----AEELRRKTSERLETVILDVTKTENIVAAtqwVKERVGNR 104
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKldavAKEIEEKYGVETKTIAADFSAGDDIYER---IEKELEGL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 105 GLWGLVNNAGISvPSGPNEWMKKQD--FASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:cd05356   78 DIGILVNNVGIS-HSIPEYFLETPEdeLQDIINVNVMATLKMTRLILPgMVKRKKGAIVNISSFAGLIPTPLLATYSASK 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:cd05356  157 AFLDFFSRALYEEYKSQGIDVQSLLPYLVATKM 189
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 27-225 1.20e-17

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 80.53  E-value: 1.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRV----LAACRKEEGAEELRRKTSE---RLETVILDVTKTENIVAATQWVKE 99
Cdd:PRK12827   4 LDSRRVLITGGSGGLGRAIAVRLAADGADVivldIHPMRGRAEADAVAAGIEAaggKALGLAFDVRDFAATRAALDAGVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 100 RVGnrGLWGLVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR--GRVVNVSSILGRVSLGGSGGY 177
Cdd:PRK12827  84 EFG--RLDILVNNAGI-ATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARrgGRIVNIASVAGVRGNRGQVNY 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 226510520 178 CISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSARLCSNIQ 225
Cdd:PRK12827 161 AASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADNAAPTEHLL 208
PRK06114 PRK06114
SDR family oxidoreductase;
27-231 1.64e-17

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 80.60  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEElrrKTSERLET-------VILDVTKTENIVAATQWVKE 99
Cdd:PRK06114   6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLA---ETAEHIEAagrraiqIAADVTSKADLRAAVARTEA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 100 RVGNRGLwgLVNNAGISvPSGPNEWMKKQDFASVLDVNLLGlieVTLS-------MLPlvrKARGRVVNVSSILGRVSLG 172
Cdd:PRK06114  83 ELGALTL--AVNAAGIA-NANPAEEMEEEQWQTVMDINLTG---VFLScqaearaMLE---NGGGSIVNIASMSGIIVNR 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226510520 173 G--SGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSARLCSNIQMLWDQT 231
Cdd:PRK06114 154 GllQAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTRPEMVHQTKLFEEQT 214
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 26-218 4.67e-17

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 79.07  E-value: 4.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  26 HLQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACR-KEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGnr 104
Cdd:PRK12828   4 SLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRgAAPLSQTLPGVPADALRIGGIDLVDPQAARRAVDEVNRQFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 105 GLWGLVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISKYG 183
Cdd:PRK12828  82 RLDALVNIAGA-FVWGTIADGDADTWDRMYGVNVKTTLNASKAALPaLTASGGGRIVNIGAGAALKAGPGMGAYAAAKAG 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226510520 184 IEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:PRK12828 161 VARLTEALAAELLDRGITVNAVLPSIIDTPPNRAD 195
PRK06484 PRK06484
short chain dehydrogenase; Validated
 28-214 6.03e-17

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 81.05  E-value: 6.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  28 QDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGNRGLw 107
Cdd:PRK06484   4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDV- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 108 gLVNNAGISVPS-GPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR--GRVVNVSSILGRVSLGGSGGYCISKYGI 184
Cdd:PRK06484  83 -LVNNAGVTDPTmTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGhgAAIVNVASGAGLVALPKRTAYSASKAAV 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 226510520 185 EAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:PRK06484 162 ISLTRSLACEWAAKGIRVNAVLPGYVRTQM 191
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 27-212 1.37e-16

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 78.01  E-value: 1.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAE---ELRRKTSERLETVILDVTKTENIVAATQWVKERVGN 103
Cdd:PRK13394   5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANavaDEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 RGLwgLVNNAGISVPSgPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR--GRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:PRK13394  85 VDI--LVSNAGIQIVN-PIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHSHEASPLKSAYVTAK 161

                        170       180       190
                 ....*....|....*....|....*....|.
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:PRK13394 162 HGLLGLARVLAKEGAKHNVRSHVVCPGFVRT 192
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 27-218 1.40e-16

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 78.13  E-value: 1.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVlAACRKEEGAEElrrktSERLETVILDVTKTENIVAATQWVKERVGnrGL 106
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANV-VNADIHGGDGQ-----HENYQFVPTDVSSAEEVNHTVAEIIEKFG--RI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAGISVP---------SGPNEwMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGrvsLGGSGG 176
Cdd:PRK06171  79 DGLVNNAGINIPrllvdekdpAGKYE-LNEAAFDKMFNINQKGVFLMSQAVARqMVKQHDGVIVNMSSEAG---LEGSEG 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 226510520 177 ---YCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFF-LTGMASSA 218
Cdd:PRK06171 155 qscYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILeATGLRTPE 200
PRK07063 PRK07063
SDR family oxidoreductase;
27-212 1.53e-16

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 77.78  E-value: 1.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRK----EEGAEELRRK-TSERLETVILDVTKTENIVAATQWVKERV 101
Cdd:PRK07063   5 LAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDaalaERAAAAIARDvAGARVLAVPADVTDAASVAAAVAAAEEAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 102 GnrGLWGLVNNAGISVPSGPNEwMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCIS 180
Cdd:PRK07063  85 G--PLDVLVNNAGINVFADPLA-MTDEDWRRCFAVDLDGAWNGCRAVLPgMVERGRGSIVNIASTHAFKIIPGCFPYPVA 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 226510520 181 KYGIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:PRK07063 162 KHGLLGLTRALGIEYAARNVRVNAIAPGYIET 193
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 34-217 3.18e-16

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: 76.94  E-value: 3.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  34 ITGCGSGFGNLLARQLDRRGMRV-LAACRKEEGAEELrrKTSERLETVILDVTKTENIVAATQWVKERVGNrgLWGLVNN 112
Cdd:cd05371    7 VTGGASGLGLATVERLLAQGAKVvILDLPNSPGETVA--KLGDNCRFVPVDVTSEKDVKAALALAKAKFGR--LDIVVNC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 113 AGISV-----------PSGPNEWMKkqdfasVLDVNLLGlievTLSMLPLVRKA-----------RGRVVNVSSILGRVS 170
Cdd:cd05371   83 AGIAVaaktynkkgqqPHSLELFQR------VINVNLIG----TFNVIRLAAGAmgknepdqggeRGVIINTASVAAFEG 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 226510520 171 LGGSGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASS 217
Cdd:cd05371  153 QIGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAG 199
PRK09242 PRK09242
SDR family oxidoreductase;
27-217 3.53e-16

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 76.71  E-value: 3.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAE----ELRRKTSER-LETVILDVTKTENIVAATQWVKERV 101
Cdd:PRK09242   7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAqardELAEEFPEReVHGLAADVSDDEDRRAILDWVEDHW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 102 GnrGLWGLVNNAGISVPSGPNEWmKKQDFASVLDVNLLGLIEVTLSMLPLVRK-ARGRVVNVSSILGRVSLGGSGGYCIS 180
Cdd:PRK09242  87 D--GLHILVNNAGGNIRKAAIDY-TEDEWRGIFETNLFSAFELSRYAHPLLKQhASSAIVNIGSVSGLTHVRSGAPYGMT 163

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226510520 181 KYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASS 217
Cdd:PRK09242 164 KAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSG 200
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 27-212 3.62e-16

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: 77.11  E-value: 3.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVI---LDVTKTENIVAATQWVKERVGN 103
Cdd:cd08935    3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIalaADVLDRASLERAREEIVAQFGT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 RGLwgLVNNAGISVPSG--PNEW-----------MKKQDFASVLDVNLLGliEVTLSML---PLVRKARGRVVNVSSILG 167
Cdd:cd08935   83 VDI--LINGAGGNHPDAttDPEHyepeteqnffdLDEEGWEFVFDLNLNG--SFLPSQVfgkDMLEQKGGSIINISSMNA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 226510520 168 RVSLGGSGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:cd08935  159 FSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVT 203
PRK06138 PRK06138
SDR family oxidoreductase;
26-214 4.71e-16

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 76.34  E-value: 4.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  26 HLQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEEL--RRKTSERLETVILDVTKTENIVAATQWVKERVGn 103
Cdd:PRK06138   2 RLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVaaAIAAGGRAFARQGDVGSAEAVEALVDFVAARWG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 rGLWGLVNNAGIS-----VPSGPNEWmkkqdfASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGY 177
Cdd:PRK06138  81 -RLDVLVNNAGFGcggtvVTTDEADW------DAVMRVNVGGVFLWAKYAIPIMQRQGgGSIVNTASQLALAGGRGRAAY 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226510520 178 CISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:PRK06138 154 VASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPY 190
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 32-240 4.76e-16

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: 75.97  E-value: 4.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKtserLETVILDVTKTENIVAATQWVKERVGnrGLWGLVN 111
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYGDP----LRLTPLDVADAAAVREVCSRLLAEHG--PIDALVN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 112 NAGISVPsGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKYGIEAFSDS 190
Cdd:cd05331   75 CAGVLRP-GATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRtGAIVTVASNAAHVPRISMAAYGASKAALASLSKC 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 226510520 191 LRRELRYFGVKVAIIEPGFFLTGMassarlcsnIQMLWDQTSSEIREIYG 240
Cdd:cd05331  154 LGLELAPYGVRCNVVSPGSTDTAM---------QRTLWHDEDGAAQVIAG 194
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 27-208 6.36e-16

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: 75.70  E-value: 6.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRK----EEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVG 102
Cdd:cd05369    1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKpevlEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLKEFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 NrgLWGLVNNAGISVPSgPNEWMKKQDFASVLDVNLLGLIEVTLSMLP--LVRKARGRVVNVSSILGRVSLGGSGGYCIS 180
Cdd:cd05369   81 K--IDILINNAAGNFLA-PAESLSPNGFKTVIDIDLNGTFNTTKAVGKrlIEAKHGGSILNISATYAYTGSPFQVHSAAA 157

                        170       180
                 ....*....|....*....|....*...
gi 226510520 181 KYGIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:cd05369  158 KAGVDALTRSLAVEWGPYGIRVNAIAPG 185
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 32-218 7.42e-16

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


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 75.47  E-value: 7.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGMRVLAACRK-EEGAEELRRKTSERLETVIL---DVTKTENIVAATQWVKERVGnrGLW 107
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVVINYRKsKDAAAEVAAEIEELGGKAVVvraDVSQPQDVEEMFAAVKERFG--RLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 108 GLVNNAGISVPSGPNEwMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKYGIEA 186
Cdd:cd05359   79 VLVSNAAAGAFRPLSE-LTPAHWDAKMNTNLKALVHCAQQAAKLMRERGgGRIVAISSLGSIRALPNYLAVGTAKAALEA 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 226510520 187 FSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:cd05359  158 LVRYLAVELGPRGIRVNAVSPGVIDTDALAHF 189
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
27-208 1.22e-15

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 75.06  E-value: 1.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGnrGL 106
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFG--GI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGLI----EVTLSMLPlvRKARGRVVNVSSILGRVSLGGSGGYCISKY 182
Cdd:PRK07067  82 DILFNNAAL-FDMAPILDISRDSYDRLFAVNVKGLFflmqAVARHMVE--QGRGGKIINMASQAGRRGEALVSHYCATKA 158

                        170       180
                 ....*....|....*....|....*.
gi 226510520 183 GIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:PRK07067 159 AVISYTQSAALALIRHGINVNAIAPG 184
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 27-230 1.84e-15

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: 74.68  E-value: 1.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRV----LAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVG 102
Cdd:cd05352    6 LKGKVAIVTGGSRGIGLAIARALAEAGADVaiiyNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 NrgLWGLVNNAGISVPSgPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRK-ARGRVVNVSSILGRVSL--GGSGGYCI 179
Cdd:cd05352   86 K--IDILIANAGITVHK-PALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKqGKGSLIITASMSGTIVNrpQPQAAYNA 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 226510520 180 SKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSARlcSNIQMLWDQ 230
Cdd:cd05352  163 SKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVD--KELRKKWES 211
PRK06949 PRK06949
SDR family oxidoreductase;
27-214 2.11e-15

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 74.41  E-value: 2.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRrktsERLE-------TVILDVTKTENIVAATQWVKE 99
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELR----AEIEaeggaahVVSLDVTDYQSIKAAVAHAET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 100 RVGNRGLwgLVNNAGISVPSGPNEwMKKQDFASVLDVNLLGLI----EVTLSMLPLVR-----KARGRVVNVSSILGRVS 170
Cdd:PRK06949  83 EAGTIDI--LVNNSGVSTTQKLVD-VTPADFDFVFDTNTRGAFfvaqEVAKRMIARAKgagntKPGGRIINIASVAGLRV 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 226510520 171 LGGSGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:PRK06949 160 LPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEI 203
PRK07775 PRK07775
SDR family oxidoreductase;
32-217 3.06e-15

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 74.41  E-value: 3.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRK-TSERLETVI--LDVTKTENIVAATQWVKERVGNRGLwg 108
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKiRADGGEAVAfpLDVTDPDSVKSFVAQAEEALGEIEV-- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 109 LVNNAGISVPSGPNEwMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEAF 187
Cdd:PRK07775  91 LVSGAGDTYFGKLHE-ISTEQFESQVQIHLVGANRLATAVLPgMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEAM 169

                        170       180       190
                 ....*....|....*....|....*....|
gi 226510520 188 SDSLRRELRYFGVKVAIIEPGFFLTGMASS 217
Cdd:PRK07775 170 VTNLQMELEGTGVRASIVHPGPTLTGMGWS 199
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 27-217 3.42e-15

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


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 73.96  E-value: 3.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGnrGL 106
Cdd:cd05345    3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFG--RL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRV-VNVSSILGRVSLGGSGGYCISKYGIE 185
Cdd:cd05345   81 DILVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGViINIASTAGLRPRPGLTWYNASKGWVV 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 226510520 186 AFSDSLRRELRYFGVKVAIIEPGFFLTGMASS 217
Cdd:cd05345  161 TATKAMAVELAPRNIRVNCLCPVAGETPLLSM 192
PRK06947 PRK06947
SDR family oxidoreductase;
30-217 4.79e-15

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 73.30  E-value: 4.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRV-LAACRKEEGAEE---LRRKTSERLETVILDVTKTENIVAATQWVKERVGnrG 105
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVgINYARDAAAAEEtadAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFG--R 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 106 LWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR----GRVVNVSSILGRVslgGSGG----Y 177
Cdd:PRK06947  81 LDALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRggrgGAIVNVSSIASRL---GSPNeyvdY 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 226510520 178 CISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASS 217
Cdd:PRK06947 158 AGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHAS 197
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 27-212 4.83e-15

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 73.78  E-value: 4.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGcGSG-FGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVIL---DVTKTENIVAATQWVKERVG 102
Cdd:PRK08277   8 LKGKVAVITG-GGGvLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAvkaDVLDKESLEQARQQILEDFG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 NRGLwgLVNNAGISVPSG--PNEW------------MKKQDFASVLDVNLLGlievtlSMLP-------LVRKARGRVVN 161
Cdd:PRK08277  87 PCDI--LINGAGGNHPKAttDNEFhelieptktffdLDEEGFEFVFDLNLLG------TLLPtqvfakdMVGRKGGNIIN 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226510520 162 VSSI-----LGRVSlggsgGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:PRK08277 159 ISSMnaftpLTKVP-----AYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLT 209
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 27-240 6.02e-15

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 72.99  E-value: 6.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRrktserLETVILDVTKTENIVAATQWVKERVGnrGL 106
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDYP------FATFVLDVSDAAAVAQVCQRLLAETG--PL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIE 185
Cdd:PRK08220  78 DVLVNAAGI-LRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPqFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKAALT 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 226510520 186 AFSDSLRRELRYFGVKVAIIEPGFFLTGMAssarlcsniQMLWDQTSSEIREIYG 240
Cdd:PRK08220 157 SLAKCVGLELAPYGVRCNVVSPGSTDTDMQ---------RTLWVDEDGEQQVIAG 202
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 30-208 7.87e-15

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: 73.27  E-value: 7.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRK----EEGAEELRRKTSERLETVI-LDVTKTENIVA-ATQWVKERvgn 103
Cdd:cd09807    2 KTVIITGANTGIGKETARELARRGARVIMACRDmakcEEAAAEIRRDTLNHEVIVRhLDLASLKSIRAfAAEFLAEE--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 RGLWGLVNNAGI-SVPsgpnEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRK-ARGRVVNVSSIL---GRV--------- 169
Cdd:cd09807   79 DRLDVLINNAGVmRCP----YSKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKsAPSRIVNVSSLAhkaGKInfddlnsek 154

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 226510520 170 SLGGSGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:cd09807  155 SYNTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPG 193
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
30-214 8.42e-15

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 72.84  E-value: 8.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLE---TVILDVTKTENIVAATQWVKERVGnrGL 106
Cdd:PRK08643   3 KVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGkaiAVKADVSDRDQVFAAVRQVVDTFG--DL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAGISvPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR--GRVVNVSSILGRVSLGGSGGYCISKYGI 184
Cdd:PRK08643  81 NVVVNNAGVA-PTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGhgGKIINATSQAGVVGNPELAVYSSTKFAV 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 226510520 185 EAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:PRK08643 160 RGLTQTAARDLASEGITVNAYAPGIVKTPM 189
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 25-218 9.58e-15

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 72.60  E-value: 9.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  25 DHLQDKYVFITGCGSGFGNLLARQLDRRGMRVLaacrkeegaeeLRRKTSERLETV---------------ILD---VTK 86
Cdd:PRK08945   8 DLLKDRIILVTGAGDGIGREAALTYARHGATVI-----------LLGRTEEKLEAVydeieaaggpqpaiiPLDlltATP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  87 TENI-VAATqwVKERVGNrgLWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSS 164
Cdd:PRK08945  77 QNYQqLADT--IEEQFGR--LDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPaASLVFTSS 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 226510520 165 ILGRVSLGGSGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:PRK08945 153 SVGRQGRANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAMRASA 206
PRK06124 PRK06124
SDR family oxidoreductase;
27-212 1.10e-14

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 72.44  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLA----ACRKEEGAEELRRKTSeRLETVILDVTKTENIVAATQWVKERVG 102
Cdd:PRK06124   9 LAGQVALVTGSARGLGFEIARALAGAGAHVLVngrnAATLEAAVAALRAAGG-AAEALAFDIADEEAVAAAFARIDAEHG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 nrGLWGLVNNAGISVPSGPNEwMKKQDFASVLDVNLLGLIevTLSMLPLVRKAR---GRVVNVSSILGRVSLGGSGGYCI 179
Cdd:PRK06124  88 --RLDILVNNVGARDRRPLAE-LDDAAIRALLETDLVAPI--LLSRLAAQRMKRqgyGRIIAITSIAGQVARAGDAVYPA 162

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226510520 180 SKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:PRK06124 163 AKQGLTGLMRALAAEFGPHGITSNAIAPGYFAT 195
PRK06172 PRK06172
SDR family oxidoreductase;
27-218 1.11e-14

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 72.48  E-value: 1.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEE---LRRKTSERLETVILDVTKTENIvaaTQWVKERVGN 103
Cdd:PRK06172   5 FSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEEtvaLIREAGGEALFVACDVTRDAEV---KALVEQTIAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 RG-LWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGlieVTLSM---LP-LVRKARGRVVNVSSILGRVSLGGSGGYC 178
Cdd:PRK06172  82 YGrLDYAFNNAGIEIEQGRLAEGSEAEFDAIMGVNVKG---VWLCMkyqIPlMLAQGGGAIVNTASVAGLGAAPKMSIYA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 226510520 179 ISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:PRK06172 159 ASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRA 198
PRK07201 PRK07201
SDR family oxidoreductase;
18-189 1.20e-14

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 74.22  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  18 FRERQVVDHLQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVIL---DVTKTENIVAAT 94
Cdd:PRK07201 360 ARRRDLRGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAytcDLTDSAAVDHTV 439

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  95 QWVKERVGNRGLwgLVNNAGISV-PSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSIlG----- 167
Cdd:PRK07201 440 KDILAEHGHVDY--LVNNAGRSIrRSVENSTDRFHDYERTMAVNYFGAVRLILGLLPHMRERRfGHVVNVSSI-Gvqtna 516

                        170       180
                 ....*....|....*....|...
gi 226510520 168 -RVSlggsgGYCISKYGIEAFSD 189
Cdd:PRK07201 517 pRFS-----AYVASKAALDAFSD 534
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 27-214 1.84e-14

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: 71.74  E-value: 1.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVIL--DVTKTENIVAATQWVKERvgNR 104
Cdd:cd08942    4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYGECIAIpaDLSSEEGIEALVARVAER--SD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 105 GLWGLVNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-----GRVVNVSSILGRVSLGGSG-GYC 178
Cdd:cd08942   82 RLDVLVNNAGATW-GAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAAtaenpARVINIGSIAGIVVSGLENySYG 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226510520 179 ISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:cd08942  161 ASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKM 196
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 27-214 2.01e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 71.71  E-value: 2.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVL----AACRKEEGAEELRRKtSERLETVILDVTKTENIVAATQWVKERVG 102
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIindiTAERAELAVAKLRQE-GIKAHAAPFNVTHKQEVEAAIEHIEKDIG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 nrGLWGLVNNAGISVPSGPNEWmKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSI---LGRVSLggsGGYC 178
Cdd:PRK08085  86 --PIDVLINNAGIQRRHPFTEF-PEQEWNDVIAVNQTAVFLVSQAVARyMVKRQAGKIINICSMqseLGRDTI---TPYA 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226510520 179 ISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:PRK08085 160 ASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEM 195
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 34-223 3.23e-14

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 71.53  E-value: 3.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  34 ITGCGSGFGNLLARQLDRRGMR-VLAACRK---EEGAEELRRKTSErLETVILDVTKTENIVAATQWVKERVGNRGLwgL 109
Cdd:PRK05876  11 ITGGASGIGLATGTEFARRGARvVLGDVDKpglRQAVNHLRAEGFD-VHGVMCDVRHREEVTHLADEAFRLLGHVDV--V 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 110 VNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP--LVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEAF 187
Cdd:PRK05876  88 FSNAGIVV-GGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPrlLEQGTGGHVVFTASFAGLVPNAGLGAYGVAKYGVVGL 166

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226510520 188 SDSLRRELRYFGVKVAIIEPgffltgMASSARLCSN 223
Cdd:PRK05876 167 AETLAREVTADGIGVSVLCP------MVVETNLVAN 196
PRK07023 PRK07023
SDR family oxidoreductase;
34-219 3.31e-14

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 70.81  E-value: 3.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  34 ITGCGSGFGNLLARQLDRRGMRVLAACRKEEgaEELRRKTSERLETVILDVTKTEnivAATQWVKERVGNRGLWG----- 108
Cdd:PRK07023   6 VTGHSRGLGAALAEQLLQPGIAVLGVARSRH--PSLAAAAGERLAEVELDLSDAA---AAAAWLAGDLLAAFVDGasrvl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 109 LVNNAGISVPSGPNEwmkKQDFASV---LDVNLLGLIEVTLSMLPLVRK-ARGRVVNVSSILGRVSLGGSGGYCISKYGI 184
Cdd:PRK07023  81 LINNAGTVEPIGPLA---TLDAAAIaraVGLNVAAPLMLTAALAQAASDaAERRILHISSGAARNAYAGWSVYCATKAAL 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226510520 185 EAFSDSLRRELRYfGVKVAIIEPGFFLTGMASSAR 219
Cdd:PRK07023 158 DHHARAVALDANR-ALRIVSLAPGVVDTGMQATIR 191
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 32-216 5.23e-14

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: 69.08  E-value: 5.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGM-RVLAACRkeegaeelrrktserletviLDVtktenivaatqwvkervgnrglwgLV 110
Cdd:cd02266    1 VLVTGGSGGIGGAIARWLASRGSpKVLVVSR--------------------RDV------------------------VV 36

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 111 NNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKYGIEAFSD 189
Cdd:cd02266   37 HNAAILD-DGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRlGRFILISSVAGLFGAPGLGGYAASKAALDGLAQ 115

                        170       180
                 ....*....|....*....|....*...
gi 226510520 190 SLRRELRYFGVKVAIIEPGFFL-TGMAS 216
Cdd:cd02266  116 QWASEGWGNGLPATAVACGTWAgSGMAK 143
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 27-208 6.34e-14

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 70.16  E-value: 6.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRV-LAACRKEEGAEELRRKTSE---RLETVILDVTKTENIVAATQWVKERVG 102
Cdd:PRK12937   3 LSNKVAIVTGASRGIGAAIARRLAADGFAVaVNYAGSAAAADELVAEIEAaggRAIAVQADVADAAAVTRLFDAAETAFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 nrGLWGLVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKArGRVVNVSSILGRVSLGGSGGYCISKY 182
Cdd:PRK12937  83 --RIDVLVNNAGV-MPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQG-GRIINLSTSVIALPLPGYGPYAASKA 158

                        170       180
                 ....*....|....*....|....*.
gi 226510520 183 GIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:PRK12937 159 AVEGLVHVLANELRGRGITVNAVAPG 184
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 27-218 9.83e-14

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: 69.78  E-value: 9.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSER---LETVILDVTKTENIVAATQWVKERVGN 103
Cdd:cd05329    4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKgfkVEGSVCDVSSRSERQELMDTVASHFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 RgLWGLVNNAGISVPSGPNEWMKKqDFASVLDVNLLGLIEVTLSMLPLV-RKARGRVVNVSSILGRVSLGGSGGYCISKY 182
Cdd:cd05329   84 K-LNILVNNAGTNIRKEAKDYTEE-DYSLIMSTNFEAAYHLSRLAHPLLkASGNGNIVFISSVAGVIAVPSGAPYGATKG 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226510520 183 GIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:cd05329  162 ALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPV 197
PRK06139 PRK06139
SDR family oxidoreductase;
27-212 1.25e-13

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 70.52  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEG----AEELRRKTSERLeTVILDVTKTENIVAATQWVKERVG 102
Cdd:PRK06139   5 LHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEAlqavAEECRALGAEVL-VVPTDVTDADQVKALATQAASFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 NRGLWglVNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRK-ARGRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:PRK06139  84 RIDVW--VNNVGVGA-VGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKqGHGIFINMISLGGFAAQPYAAAYSASK 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 226510520 182 YGIEAFSDSLRRELRYF-GVKVAIIEPGFFLT 212
Cdd:PRK06139 161 FGLRGFSEALRGELADHpDIHVCDVYPAFMDT 192
PRK08589 PRK08589
SDR family oxidoreductase;
27-208 1.32e-13

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 69.81  E-value: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELR--RKTSERLETVILDVTKTENIVAATQWVKERVGNR 104
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDkiKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 105 GLwgLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISKYGI 184
Cdd:PRK08589  84 DV--LFNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAADLYRSGYNAAKGAV 161

                        170       180
                 ....*....|....*....|....
gi 226510520 185 EAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:PRK08589 162 INFTKSIAIEYGRDGIRANAIAPG 185
PRK06101 PRK06101
SDR family oxidoreductase;
32-237 1.67e-13

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 68.74  E-value: 1.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRrKTSERLETVILDVTKTENIVAATQwvkervgnrglwglvn 111
Cdd:PRK06101   4 VLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDELH-TQSANIFTLAFDVTDHPGTKAALS---------------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 112 nagiSVPSGPNEW--------------MKKQDFASVLDVNLLGLIEVTLSMLPLVRKARgRVVNVSSILGRVSLGGSGGY 177
Cdd:PRK06101  67 ----QLPFIPELWifnagdceymddgkVDATLMARVFNVNVLGVANCIEGIQPHLSCGH-RVVIVGSIASELALPRAEAY 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 178 CISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSARLCSNIQMLWDQTSSEIRE 237
Cdd:PRK06101 142 GASKAAVAYFARTLQLDLRPKGIEVVTVFPGFVATPLTDKNTFAMPMIITVEQASQEIRA 201
PRK05866 PRK05866
SDR family oxidoreductase;
21-202 1.99e-13

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 69.39  E-value: 1.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  21 RQVVDhLQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSER---LETVILDVTKTENIVAATQWV 97
Cdd:PRK05866  33 RQPVD-LTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAggdAMAVPCDLSDLDAVDALVADV 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  98 KERVGnrGLWGLVNNAGISVPSGPNEWMKK-QDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSilGRVSLGGS- 174
Cdd:PRK05866 112 EKRIG--GVDILINNAGRSIRRPLAESLDRwHDVERTMVLNYYAPLRLIRGLAPgMLERGDGHIINVAT--WGVLSEASp 187

                        170       180       190
                 ....*....|....*....|....*....|
gi 226510520 175 --GGYCISKYGIEAFSDSLRRELRYFGVKV 202
Cdd:PRK05866 188 lfSVYNASKAALSAVSRVIETEWGDRGVHS 217
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
30-223 2.09e-13

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 68.94  E-value: 2.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKE-EGAEELRRKTSERLETVILDVTkteNIVAATQWVKE-----RVGN 103
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTEnKELTKLAEQYNSNLTFHSLDLQ---DVHELETNFNEilssiQEDN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 RGLWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLG---LIEVTLSMLPLvRKARGRVVNVSSILGRVSLGGSGGYCIS 180
Cdd:PRK06924  79 VSSIHLINNAGMVAPIKPIEKAESEELITNVHLNLLApmiLTSTFMKHTKD-WKVDKRVINISSGAAKNPYFGWSAYCSS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 226510520 181 KYGIEAFSDS--LRRELRYFGVKVAIIEPGFFLTGMASSARLCSN 223
Cdd:PRK06924 158 KAGLDMFTQTvaTEQEEEEYPVKIVAFSPGVMDTNMQAQIRSSSK 202
PRK07774 PRK07774
SDR family oxidoreductase;
27-208 2.34e-13

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 68.62  E-value: 2.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVI---LDVTKTENIVAATQWVKERVGn 103
Cdd:PRK07774   4 FDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIavqVDVSDPDSAKAMADATVSAFG- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 rGLWGLVNNAGISVPSGPNEWMKK--QDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSlggSGGYCIS 180
Cdd:PRK07774  83 -GIDYLVNNAAIYGGMKLDLLITVpwDYYKKFMSVNLDGALVCTRAVYKHMAKRGgGAIVNQSSTAAWLY---SNFYGLA 158

                        170       180
                 ....*....|....*....|....*...
gi 226510520 181 KYGIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:PRK07774 159 KVGLNGLTQQLARELGGMNIRVNAIAPG 186
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 27-208 2.87e-13

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 68.60  E-value: 2.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRK-EEGAEELR---RKTSERLETVILDVTKTENIVAATQWVKERVG 102
Cdd:PRK08936   5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSdEEEANDVAeeiKKAGGEAIAVKGDVTVESDVVNLIQTAVKEFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 NRGLWglVNNAGISVPSgPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRK--ARGRVVNVSSILGRVSLGGSGGYCIS 180
Cdd:PRK08936  85 TLDVM--INNAGIENAV-PSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEhdIKGNIINMSSVHEQIPWPLFVHYAAS 161

                        170       180
                 ....*....|....*....|....*...
gi 226510520 181 KYGIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:PRK08936 162 KGGVKLMTETLAMEYAPKGIRVNNIGPG 189
PRK07831 PRK07831
SDR family oxidoreductase;
27-240 3.71e-13

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 68.14  E-value: 3.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGC-GSGFGNLLARQLDRRGMRVLA----ACRKEEGAEELRRKTSE-RLETVILDVTKTENIVAATQWVKER 100
Cdd:PRK07831  15 LAGKVVLVTAAaGTGIGSATARRALEEGARVVIsdihERRLGETADELAAELGLgRVEAVVCDVTSEAQVDALIDAAVER 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 101 VGnrGLWGLVNNAGIS-----VPSGPNEWMKkqdfasVLDVNLLGLIEVTLSMLP--LVRKARGRVVNVSSILGRVSLGG 173
Cdd:PRK07831  95 LG--RLDVLVNNAGLGgqtpvVDMTDDEWSR------VLDVTLTGTFRATRAALRymRARGHGGVIVNNASVLGWRAQHG 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226510520 174 SGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGF----FLTGMASSARLcsniqmlwDQTSSeiREIYG 240
Cdd:PRK07831 167 QAHYAAAKAGVMALTRCSALEAAEYGVRINAVAPSIamhpFLAKVTSAELL--------DELAA--REAFG 227
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 30-218 4.60e-13

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: 67.87  E-value: 4.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRK-EEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGNRGLwg 108
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYRsTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDT-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 109 LVNNAGISVPSGPN--------EWmkkQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCI 179
Cdd:cd05349   79 IVNNALIDFPFDPDqrktfdtiDW---EDYQQQLEGAVKGALNLLQAVLPDFKERGsGRVINIGTNLFQNPVVPYHDYTT 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 226510520 180 SKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:cd05349  156 AKAALLGFTRNMAKELGPYGITVNMVSGGLLKVTDASAA 194
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 30-217 5.55e-13

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


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 67.49  E-value: 5.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRktSERLETVILDVTKTENIVAATQWVkERVGNrglwgL 109
Cdd:cd05368    3 KVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELER--GPGITTRVLDVTDKEQVAALAKEE-GRIDV-----L 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 110 VNNAGIsVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRV-SLGGSGGYCISKYGIEAF 187
Cdd:cd05368   75 FNCAGF-VHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPkMLARKDGSIINMSSVASSIkGVPNRFVYSTTKAAVIGL 153

                        170       180       190
                 ....*....|....*....|....*....|
gi 226510520 188 SDSLRRELRYFGVKVAIIEPGFFLTGMASS 217
Cdd:cd05368  154 TKSVAADFAQQGIRCNAICPGTVDTPSLEE 183
PRK08251 PRK08251
SDR family oxidoreductase;
30-219 6.58e-13

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 67.27  E-value: 6.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGmRVLAAC-RKEEGAEELR-----RKTSERLETVILDVTKTENIVAATQWVKERVGn 103
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKG-RDLALCaRRTDRLEELKaellaRYPGIKVAVAALDVNDHDQVFEVFAEFRDELG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 rGLWGLVNNAGI----SVPSGpNEWMKKQdfasVLDVNLLGL---IEVTLSMLplvRKA-RGRVVNVSSILGRVSLGGS- 174
Cdd:PRK08251  81 -GLDRVIVNAGIgkgaRLGTG-KFWANKA----TAETNFVAAlaqCEAAMEIF---REQgSGHLVLISSVSAVRGLPGVk 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 226510520 175 GGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSAR 219
Cdd:PRK08251 152 AAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNAKAK 196
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 32-214 1.01e-12

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: 66.01  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLetVILDVTKTENIVAATQwvkeRVGNRGLWglVN 111
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALA--RPADVAAELEVWALAQ----ELGPLDLL--VY 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 112 NAGISVPSgPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVrKARGRVVNVSSILGRVSLGGSGGYCISKYGIEAFSDSL 191
Cdd:cd11730   73 AAGAILGK-PLARTKPAAWRRILDANLTGAALVLKHALALL-AAGARLVFLGAYPELVMLPGLSAYAAAKAALEAYVEVA 150

                        170       180
                 ....*....|....*....|...
gi 226510520 192 RRELRyfGVKVAIIEPGFFLTGM 214
Cdd:cd11730  151 RKEVR--GLRLTLVRPPAVDTGL 171
PRK07074 PRK07074
SDR family oxidoreductase;
29-225 1.60e-12

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 66.33  E-value: 1.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  29 DKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTS-ERLETVILDVTKTENIVAAtqwVKERVGNRGLW 107
Cdd:PRK07074   2 KRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGdARFVPVACDLTDAASLAAA---LANAAAERGPV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 108 G-LVNNAGISVP-----SGPNEWmkKQDFASVLDVNLLGLIEVTLSMLplvRKARGRVVNVSSILGrVSLGGSGGYCISK 181
Cdd:PRK07074  79 DvLVANAGAARAaslhdTTPASW--RADNALNLEAAYLCVEAVLEGML---KRSRGAVVNIGSVNG-MAALGHPAYSAAK 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPGFFLTgMASSARLCSNIQ 225
Cdd:PRK07074 153 AGLIHYTKLLAVEYGRFGIRANAVAPGTVKT-QAWEARVAANPQ 195
PRK12743 PRK12743
SDR family oxidoreductase;
28-214 1.93e-12

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 66.21  E-value: 1.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  28 QDKYVFITGCGSGFGNLLARQLDRRGMRV-LAACRKEEGAE---ELRRKTSERLETVILDVTKTENIVAATQWVKERVGn 103
Cdd:PRK12743   1 MAQVAIVTASDSGIGKACALLLAQQGFDIgITWHSDEEGAKetaEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 rGLWGLVNNAGisvpSGPNEWMKKQDFA---SVLDVNLLGlievtlSMLPLVRKAR--------GRVVNVSSILGRVSLG 172
Cdd:PRK12743  80 -RIDVLVNNAG----AMTKAPFLDMDFDewrKIFTVDVDG------AFLCSQIAARhmvkqgqgGRIINITSVHEHTPLP 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 226510520 173 GSGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:PRK12743 149 GASAYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIATPM 190
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 27-219 2.23e-12

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: 65.84  E-value: 2.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGNrgL 106
Cdd:cd05348    2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGK--L 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAGI-----SVPSGPNEWMKKQdFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:cd05348   80 DCFIGNAGIwdystSLVDIPEEKLDEA-FDELFHINVKGYILGAKAALPALYATEGSVIFTVSNAGFYPGGGGPLYTASK 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 226510520 182 YGIEAfsdsLRRELRY-FG--VKVAIIEPGffltGMASSAR 219
Cdd:cd05348  159 HAVVG----LVKQLAYeLAphIRVNGVAPG----GMVTDLR 191
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 32-167 2.28e-12

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: 65.59  E-value: 2.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGMRVLAACRKEegAEelrrktserletVILDVTKTENIVAATQWVKERVGnRGLWGLVN 111
Cdd:cd05328    2 IVITGAASGIGAATAELLEDAGHTVIGIDLRE--AD------------VIADLSTPEGRAAAIADVLARCS-GVLDGLVN 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 226510520 112 NAGISVPSGPNewmkkqdfaSVLDVNLLGLIEVTLSMLPLVRKARG-RVVNVSSILG 167
Cdd:cd05328   67 CAGVGGTTVAG---------LVLKVNYFGLRALMEALLPRLRKGHGpAAVVVSSIAG 114
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 29-211 2.63e-12

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 65.83  E-value: 2.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  29 DKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLE-----TVILDVTKTENIVAATQWVKERVGN 103
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGegmayGFGADATSEQSVLALSRGVDEIFGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 RGLwgLVNNAGISVpSGPNEWMKKQDFASVLDVNLLGLI----EVTLSMLPlvRKARGRVVNVSSILGRVSLGGSGGYCI 179
Cdd:PRK12384  82 VDL--LVYNAGIAK-AAFITDFQLGDFDRSLQVNLVGYFlcarEFSRLMIR--DGIQGRIIQINSKSGKVGSKHNSGYSA 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 226510520 180 SKYGIEAFSDSLRRELRYFGVKVAIIEPGFFL 211
Cdd:PRK12384 157 AKFGGVGLTQSLALDLAEYGITVHSLMLGNLL 188
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 27-208 2.66e-12

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 65.80  E-value: 2.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGnrGL 106
Cdd:PRK08265   4 LAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFG--RV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAGISV----PSGPNEWMKkqdfasVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISKY 182
Cdd:PRK08265  82 DILVNLACTYLddglASSRADWLA------ALDVNLVSAAMLAQAAHPHLARGGGAIVNFTSISAKFAQTGRWLYPASKA 155

                        170       180
                 ....*....|....*....|....*.
gi 226510520 183 GIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:PRK08265 156 AIRQLTRSMAMDLAPDGIRVNSVSPG 181
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 30-212 2.76e-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: 65.55  E-value: 2.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVIL-----DVTKTENIVAATQWVKERVGnr 104
Cdd:cd08940    3 KVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGLAAKHGVKVlyhgaDLSKPAAIEDMVAYAQRQFG-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 105 GLWGLVNNAGISvPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKYG 183
Cdd:cd08940   81 GVDILVNNAGIQ-HVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGwGRIINIASVHGLVASANKSAYVAAKHG 159

                        170       180
                 ....*....|....*....|....*....
gi 226510520 184 IEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:cd08940  160 VVGLTKVVALETAGTGVTCNAICPGWVLT 188
PRK07069 PRK07069
short chain dehydrogenase; Validated
 33-214 3.68e-12

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 65.12  E-value: 3.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  33 FITGCGSGFGNLLARQLDRRGMRV-LAACRKEEGAEELRRKTSERLET-----VILDVTKTENIVAATQWVKERVGnrGL 106
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVfLTDINDAAGLDAFAAEINAAHGEgvafaAVQDVTDEAQWQALLAQAADAMG--GL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKYGIE 185
Cdd:PRK07069  81 SVLVNNAGVGS-FGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQpASIVNISSVAAFKAEPDYTAYNASKAAVA 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 226510520 186 AFSDSL-----RRELRyfgVKVAIIEPGFFLTGM 214
Cdd:PRK07069 160 SLTKSIaldcaRRGLD---VRCNSIHPTFIRTGI 190
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 29-214 9.62e-12

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 63.83  E-value: 9.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  29 DKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGaeelrrKTSERLETVILDVTktENIVAATQWVKErvgnrgLWG 108
Cdd:PRK06550   5 TKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDKP------DLSGNFHFLQLDLS--DDLEPLFDWVPS------VDI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 109 LVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEAF 187
Cdd:PRK06550  71 LCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPqMLERKSGIIINMCSIASFVAGGGGAAYTASKHALAGF 150

                        170       180
                 ....*....|....*....|....*..
gi 226510520 188 SDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:PRK06550 151 TKQLALDYAKDGIQVFGIAPGAVKTPM 177
PRK06953 PRK06953
SDR family oxidoreductase;
30-214 1.61e-11

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 62.78  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSerlETVILDVTKTENiVAATQWvkeRVGNRGLWGL 109
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQALGA---EALALDVADPAS-VAGLAW---KLDGEALDAA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 110 VNNAGISVP-SGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVS-LGGSGG--YCISKygiE 185
Cdd:PRK06953  75 VYVAGVYGPrTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSRMGSIGdATGTTGwlYRASK---A 151

                        170       180       190
                 ....*....|....*....|....*....|
gi 226510520 186 AFSDSLR-RELRYFGVKVAIIEPGFFLTGM 214
Cdd:PRK06953 152 ALNDALRaASLQARHATCIALHPGWVRTDM 181
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
27-207 1.70e-11

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 64.87  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRK--TSERLETVILDVTKTENIVAATQWVKERVGnr 104
Cdd:PRK08324 420 LAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAElgGPDRALGVACDVTDEAAVQAAFEEAALAFG-- 497

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 105 GLWGLVNNAGISvPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKA--RGRVVNVSSILGRVSLGGSGGYCISKy 182
Cdd:PRK08324 498 GVDIVVSNAGIA-ISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQglGGSIVFIASKNAVNPGPNFGAYGAAK- 575

                        170       180
                 ....*....|....*....|....*....
gi 226510520 183 gieAFSDSLRR----ELRYFGVKVAIIEP 207
Cdd:PRK08324 576 ---AAELHLVRqlalELGPDGIRVNGVNP 601
PRK12746 PRK12746
SDR family oxidoreductase;
26-212 2.06e-11

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 63.13  E-value: 2.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  26 HLQDKYVFITGCGSGFGNLLARQLDRRGMRV-LAACRKEEGAEELRRKTSERLETVIL---DVTKTENIVAATQWVKE-- 99
Cdd:PRK12746   3 NLDGKVALVTGASRGIGRAIAMRLANDGALVaIHYGRNKQAADETIREIESNGGKAFLieaDLNSIDGVKKLVEQLKNel 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 100 --RVGNRGLWGLVNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRkARGRVVNVSSILGRVSLGGSGGY 177
Cdd:PRK12746  83 qiRVGTSEIDILVNNAGIGT-QGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLR-AEGRVINISSAEVRLGFTGSIAY 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226510520 178 CISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:PRK12746 161 GLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKT 195
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 28-227 4.90e-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: 61.97  E-value: 4.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  28 QDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAE----ELRRKTSERLETVILDVTKTENIVAATQWVKERVGN 103
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEqlkeELTNLYKNRVIALELDITSKESIKELIESYLEKFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 rgLWGLVNNAGISV--PSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRK-ARGRVVNVSSILGRVS-----LGGSG 175
Cdd:cd08930   81 --IDILINNAYPSPkvWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKqGKGSIINIASIYGVIApdfriYENTQ 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226510520 176 -----GYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASS-----ARLCSNIQML 227
Cdd:cd08930  159 myspvEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNNQPSEflekyTKKCPLKRML 220
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 30-217 5.25e-11

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: 62.12  E-value: 5.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKteniVAATQWVKERVGNRGLW-G 108
Cdd:cd08951    8 KRIFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSS----LAETRKLADQVNAIGRFdA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 109 LVNNAGISvpSGPNEWMKKQDFASVLDVNLLGLIEVTlsmlPLVRKARgRVVNVSSIL---GRVSL----------GGSG 175
Cdd:cd08951   84 VIHNAGIL--SGPNRKTPDTGIPAMVAVNVLAPYVLT----ALIRRPK-RLIYLSSGMhrgGNASLddidwfnrgeNDSP 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 226510520 176 GYCISKYGIEAFSDSLRRelRYFGVKVAIIEPGFFLTGMASS 217
Cdd:cd08951  157 AYSDSKLHVLTLAAAVAR--RWKDVSSNAVHPGWVPTKMGGA 196
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-218 7.78e-11

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 61.26  E-value: 7.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRK-EEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGnRG 105
Cdd:PRK08642   3 ISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQsEDAAEALADELGDRAIALQADVTDREQVQAMFATATEHFG-KP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 106 LWGLVNNAGISVPSGPN--------EWmkkQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGG 176
Cdd:PRK08642  82 ITTVVNNALADFSFDGDarkkaddiTW---EDFQQQLEGSVKGALNTIQAALPGMREQGfGRIINIGTNLFQNPVVPYHD 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 226510520 177 YCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:PRK08642 159 YTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTTDASAA 200
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 27-208 8.02e-11

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


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 61.18  E-value: 8.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRV----LAACRKEEGA---------EELRRKTSERletvildVTKTENIVAA 93
Cdd:cd05353    3 FDGRVVLVTGAGGGLGRAYALAFAERGAKVvvndLGGDRKGSGKsssaadkvvDEIKAAGGKA-------VANYDSVEDG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  94 TQWVKERVGNRG-LWGLVNNAGI----SVPSgpnewMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILG 167
Cdd:cd05353   76 EKIVKTAIDAFGrVDILVNNAGIlrdrSFAK-----MSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKfGRIINTSSAAG 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 226510520 168 RVSLGGSGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:cd05353  151 LYGNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA 191
PRK06398 PRK06398
aldose dehydrogenase; Validated
 27-184 1.09e-10

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 61.00  E-value: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEgaeelRRKTSERLEtviLDVTKTENIVAATQWVKERVGNRGL 106
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEP-----SYNDVDYFK---VDVSNKEQVIKGIDYVISKYGRIDI 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226510520 107 wgLVNNAGISVpSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKYGI 184
Cdd:PRK06398  76 --LVNNAGIES-YGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDkGVIINIASVQSFAVTRNAAAYVTSKHAV 151
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
32-210 1.27e-10

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 61.15  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGcGSGF-GNLLARQLDRRGMRVLAACRKEEGAEELRRktSERLETVILDVTKTENIVAATQWVkERVgnrglwglV 110
Cdd:COG0451    2 ILVTG-GAGFiGSHLARRLLARGHEVVGLDRSPPGAANLAA--LPGVEFVRGDLRDPEALAAALAGV-DAV--------V 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 111 NNAGISVPSGpnewmkkQDFASVLDVNLLGlievTLSMLPLVRKAR-GRVVNVSSI--LGRVS--------LGGSGGYCI 179
Cdd:COG0451   70 HLAAPAGVGE-------EDPDETLEVNVEG----TLNLLEAARAAGvKRFVYASSSsvYGDGEgpidedtpLRPVSPYGA 138

                        170       180       190
                 ....*....|....*....|....*....|.
gi 226510520 180 SKYGIEAFSDSLRRElryFGVKVAIIEPGFF 210
Cdd:COG0451  139 SKLAAELLARAYARR---YGLPVTILRPGNV 166
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 34-218 1.51e-10

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: 60.55  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  34 ITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLET----VILDVTKTENIVAATQWVKERVGnrGLWGL 109
Cdd:cd05337    6 VTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAGRraiyFQADIGELSDHEALLDQAWEDFG--RLDCL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 110 VNNAGISVPsgpnewmKKQD--------FASVLDVNLLGLI----EVTLSML--PLVRKA-RGRVVNVSSILGRVSLGGS 174
Cdd:cd05337   84 VNNAGIAVR-------PRGDlldltedsFDRLIAINLRGPFfltqAVARRMVeqPDRFDGpHRSIIFVTSINAYLVSPNR 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 226510520 175 GGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:cd05337  157 GEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPV 200
PRK06500 PRK06500
SDR family oxidoreductase;
27-208 2.15e-10

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 59.97  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKteniVAATQWVKERVGNRG- 105
Cdd:PRK06500   4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGD----VAAQKALAQALAEAFg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 106 -LWGLVNNAGISVpSGPNEWMKKQDFASVLDVNLLG---LIEvtlSMLPLVRKARGRVVNvSSILGRVSLGGSGGYCISK 181
Cdd:PRK06500  80 rLDAVFINAGVAK-FAPLEDWDEAMFDRSFNTNVKGpyfLIQ---ALLPLLANPASIVLN-GSINAHIGMPNSSVYAASK 154

                        170       180
                 ....*....|....*....|....*..
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:PRK06500 155 AALLSLAKTLSGELLPRGIRVNAVSPG 181
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 30-216 2.48e-10

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: 60.09  E-value: 2.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFG-----NLLARQLDRRGMRVLAACRKEEGAEELRRKTSE-------RLETVILDVTKTENIVAATQWV 97
Cdd:cd08941    2 KVVLVTGANSGLGlaiceRLLAEDDENPELTLILACRNLQRAEAACRALLAshpdarvVFDYVLVDLSNMVSVFAAAKEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  98 KERVgnRGLWGLVNNAGISVPSGPNeW-------------------MKKQ--------------DFASVLDVNLLG---L 141
Cdd:cd08941   82 KKRY--PRLDYLYLNAGIMPNPGID-WigaikevltnplfavtnptYKIQaegllsqgdkatedGLGEVFQTNVFGhyyL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 142 IEVTLSMLPLvRKARGRVVNVSSILGRVS---------LGGSGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:cd08941  159 IRELEPLLCR-SDGGSQIIWTSSLNASPKyfslediqhLKGPAPYSSSKYLVDLLSLALNRKFNKLGVYSYVVHPGICTT 237


                 ....
gi 226510520 213 GMAS 216
Cdd:cd08941  238 NLTY 241
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-212 3.11e-10

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 59.75  E-value: 3.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAE--ELRRKTSERLETVILDVTKTEnivAATQWVKERVGNR 104
Cdd:PRK06935  13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWDEtrRLIEKEGRKVTFVQVDLTKPE---SAEKVVKEALEEF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 105 G-LWGLVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRvslggSGG-----Y 177
Cdd:PRK06935  90 GkIDILVNNAGT-IRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKvMAKQGSGKIINIASMLSF-----QGGkfvpaY 163

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226510520 178 CISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:PRK06935 164 TASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKT 198
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 27-226 3.94e-10

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 59.32  E-value: 3.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLA--ACRKEEGAEELRRKTSE-----RLETVILDVTKTENIVAA-TQWVK 98
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIhyGNRKEEAEETVYEIQSNggsafSIGANLESLHGVEALYSSlDNELQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  99 ERVGNRGLWGLVNNAGISvPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKaRGRVVNVSSILGRVSLGGSGGYC 178
Cdd:PRK12747  82 NRTGSTKFDILINNAGIG-PGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRD-NSRIINISSAATRISLPDFIAYS 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 226510520 179 ISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMasSARLCSNIQM 226
Cdd:PRK12747 160 MTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDM--NAELLSDPMM 205
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 30-245 3.99e-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: 59.33  E-value: 3.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTS--ERLETVILDVTKTENIVAATQWVKERVGnrGLW 107
Cdd:cd08943    2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQggPRALGVQCDVTSEAQVQSAFEQAVLEFG--GLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 108 GLVNNAGISvPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR--GRVVNVSSILGRVSLGGSGGYCISKygie 185
Cdd:cd08943   80 IVVSNAGIA-TSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGigGNIVFNASKNAVAPGPNAAAYSAAK---- 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226510520 186 AFSDSLRR----ELRYFGVKVAIIEPGFFLTGMASSArlcsniqMLWDQTSSEIREIYGEKYLA 245
Cdd:cd08943  155 AAEAHLARclalEGGEDGIRVNTVNPDAVFRGSKIWE-------GVWRAARAKAYGLLEEEYRT 211
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 27-214 5.42e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 59.05  E-value: 5.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEE----GAEELRRKTSE-RLETVILDVTKTENIVAATQWVKERV 101
Cdd:PRK05875   5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDklaaAAEEIEALKGAgAVRYEPADVTDEDQVARAVDAATAWH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 102 GnrGLWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEV-TLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCIS 180
Cdd:PRK05875  85 G--RLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVlKHAARELVRGGGGSFVGISSIAASNTHRWFGAYGVT 162

                        170       180       190
                 ....*....|....*....|....*....|....
gi 226510520 181 KYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:PRK05875 163 KSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDL 196
PRK06123 PRK06123
SDR family oxidoreductase;
29-235 8.10e-10

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 58.25  E-value: 8.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  29 DKYVFITGCGSGFGNLLARQLDRRGMRV-LAACRKEEGAEELR---RKTSERLETVILDVTKTENIVAATQWVKERVGNr 104
Cdd:PRK06123   2 RKVMIITGASRGIGAATALLAAERGYAVcLNYLRNRDAAEAVVqaiRRQGGEALAVAADVADEADVLRLFEAVDRELGR- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 105 gLWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLI----EVTLSMLPLVRKARGRVVNVSSILGRvsLGGSG---GY 177
Cdd:PRK06123  81 -LDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSFlcarEAVKRMSTRHGGRGGAIVNVSSMAAR--LGSPGeyiDY 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226510520 178 CISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA-------RLCSNIQMLWDQTSSEI 235
Cdd:PRK06123 158 AASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASGgepgrvdRVKAGIPMGRGGTAEEV 222
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 32-218 9.92e-10

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: 57.96  E-value: 9.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAE----ELRRKTSERLeTVILDVTKTENIVAATQWVKERVGnrGLW 107
Cdd:cd05365    2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEavaaAIQQAGGQAI-GLECNVTSEQDLEAVVKATVSQFG--GIT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 108 GLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKYGIEA 186
Cdd:cd05365   79 ILVNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGgGAILNISSMSSENKNVRIAAYGSSKAAVNH 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 226510520 187 FSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:cd05365  159 MTRNLAFDLGPKGIRVNAVAPGAVKTDALASV 190
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 27-208 1.01e-09

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: 58.01  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGnrGL 106
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWG--SI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGlievTLSMLPLVRKAR------GRVVNVSSILGRVSLGGSGGYCIS 180
Cdd:cd05363   79 DILVNNAAL-FDLAPIVDITRESYDRLFAINVSG----TLFMMQAVARAMiaqgrgGKIINMASQAGRRGEALVGVYCAT 153

                        170       180
                 ....*....|....*....|....*...
gi 226510520 181 KYGIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:cd05363  154 KAAVISLTQSAGLNLIRHGINVNAIAPG 181
PRK07035 PRK07035
SDR family oxidoreductase;
27-216 1.19e-09

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 57.72  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEG----AEELRRKTSeRLETVILDVTKTENIVAATQWVKERVG 102
Cdd:PRK07035   6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGcqavADAIVAAGG-KAEALACHIGEMEQIDALFAHIRERHG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 NrgLWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRK-ARGRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:PRK07035  85 R--LDILVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEqGGGSIVNVASVNGVSPGDFQGIYSITK 162

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMAS 216
Cdd:PRK07035 163 AAVISMTKAFAKECAPFGIRVNALLPGLTDTKFAS 197
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 27-212 1.21e-09

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 58.15  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEE---GAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGN 103
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQElvdKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVGV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 RGLwgLVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSI---LGRVSLggsGGYCI 179
Cdd:PRK07097  88 IDI--LVNNAGI-IKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPsMIKKGHGKIINICSMmseLGRETV---SAYAA 161

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226510520 180 SKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:PRK07097 162 AKGGLKMLTKNIASEYGEANIQCNGIGPGYIAT 194
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 27-208 1.54e-09

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


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 57.54  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEEL--RRKTSERLETVILDVTKTENIVAATQWVKERVGNR 104
Cdd:cd08937    2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLaeILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 105 GLwgLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRvslggsGG----YCI 179
Cdd:cd08937   82 DV--LINNVGGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPhMLERQQGVIVNVSSIATR------GIyripYSA 153

                        170       180
                 ....*....|....*....|....*....
gi 226510520 180 SKYGIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:cd08937  154 AKGGVNALTASLAFEHARDGIRVNAVAPG 182
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 30-212 2.43e-09

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: 56.82  E-value: 2.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRV-LAACRKEEGAE--ELRRKTSERLETVILDVTKTENIVAATQWVKERVGnrgl 106
Cdd:cd09761    2 KVAIVTGGGHGIGKQICLDFLEAGDKVvFADIDEERGADfaEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRID---- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 wGLVNNAGISVPsGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEA 186
Cdd:cd09761   78 -VLVNNAARGSK-GILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAFQSEPDSEAYAASKGGLVA 155

                        170       180
                 ....*....|....*....|....*..
gi 226510520 187 FSDSLRREL-RYfgVKVAIIEPGFFLT 212
Cdd:cd09761  156 LTHALAMSLgPD--IRVNCISPGWINT 180
PRK08177 PRK08177
SDR family oxidoreductase;
30-214 2.50e-09

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 56.58  E-value: 2.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETviLDVTKTENIVAATQWVKERVGNRglwgL 109
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIEK--LDMNDPASLDQLLQRLQGQRFDL----L 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 110 VNNAGISVPSG-PNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCI---SKYGIE 185
Cdd:PRK08177  76 FVNAGISGPAHqSAADATAAEIGQLFLTNAIAPIRLARRLLGQVRPGQGVLAFMSSQLGSVELPDGGEMPLykaSKAALN 155

                        170       180
                 ....*....|....*....|....*....
gi 226510520 186 AFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:PRK08177 156 SMTRSFVAELGEPTLTVLSMHPGWVKTDM 184
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 28-211 2.52e-09

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


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 57.09  E-value: 2.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  28 QDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAE----ELRRKTSERLETVILDVTKTENIVAATQWVKERVGN 103
Cdd:cd05322    1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEkvadEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 RGLwgLVNNAGISVpSGPNEWMKKQDFASVLDVNLLG--LIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:cd05322   81 VDL--LVYSAGIAK-SAKITDFELGDFDRSLQVNLVGyfLCAREFSKLMIRDGIQGRIIQINSKSGKVGSKHNSGYSAAK 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPGFFL 211
Cdd:cd05322  158 FGGVGLTQSLALDLAEHGITVNSLMLGNLL 187
PRK07814 PRK07814
SDR family oxidoreductase;
13-212 2.54e-09

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 57.10  E-value: 2.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  13 MLLRFFRerqvvdhLQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELR---RKTSERLETVILDVTKTEN 89
Cdd:PRK07814   1 MILDRFR-------LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAeqiRAAGRRAHVVAADLAHPEA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  90 IVAATQWVKERVGNRGLwgLVNNAGISVPSgPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRK--ARGRVVNVSSILG 167
Cdd:PRK07814  74 TAGLAGQAVEAFGRLDI--VVNNVGGTMPN-PLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEhsGGGSVINISSTMG 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 226510520 168 RVSLGGSGGYCISKYGIEAFSDSLRREL--RyfgVKVAIIEPGFFLT 212
Cdd:PRK07814 151 RLAGRGFAAYGTAKAALAHYTRLAALDLcpR---IRVNAIAPGSILT 194
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 27-218 3.10e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 56.48  E-value: 3.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRK-TSERLETVIL--DVTKTENIVAATQWVKERVGn 103
Cdd:PRK07478   4 LNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEiRAEGGEAVALagDVRDEAYAKALVALAVERFG- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 rGLWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGR-VSLGGSGGYCISK 181
Cdd:PRK07478  83 -GLDIAFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPaMLARGGGSLIFTSTFVGHtAGFPGMAAYAASK 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA 218
Cdd:PRK07478 162 AGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAM 198
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 32-203 3.79e-09

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


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 56.24  E-value: 3.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVIL----DVTKTENIVAATQWVKERVGNRGLw 107
Cdd:cd05373    2 AAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKavptDARDEDEVIALFDLIEEEIGPLEV- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 108 gLVNNAGISVPSGPNEwMKKQDFASVLDVNLLGLI----EVTLSMLPlvrKARGRVV---NVSSILGRvslGGSGGYCIS 180
Cdd:cd05373   81 -LVYNAGANVWFPILE-TTPRVFEKVWEMAAFGGFlaarEAAKRMLA---RGRGTIIftgATASLRGR---AGFAAFAGA 152

                        170       180
                 ....*....|....*....|...
gi 226510520 181 KYGIEAFSDSLRRELRYFGVKVA 203
Cdd:cd05373  153 KFALRALAQSMARELGPKGIHVA 175
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 27-219 4.60e-09

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 56.12  E-value: 4.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGnrGL 106
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAFG--KL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAGI-----SVPSGPNEWMKKQdFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:PRK06200  82 DCFVGNAGIwdyntSLVDIPAETLDTA-FDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLSNSSFYPGGGGPLYTASK 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 226510520 182 YGIEAfsdsLRRELRYF---GVKVAIIEPGffltGMASSAR 219
Cdd:PRK06200 161 HAVVG----LVRQLAYElapKIRVNGVAPG----GTVTDLR 193
PRK07577 PRK07577
SDR family oxidoreductase;
27-208 4.89e-09

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 55.89  E-value: 4.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAacrkeegaeeLRRKTSE----RLETVIL-DVTKTENIVAATqwvkerV 101
Cdd:PRK07577   1 MSSRTVLVTGATKGIGLALSLRLANLGHQVIG----------IARSAIDdfpgELFACDLaDIEQTAATLAQI------N 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 102 GNRGLWGLVNNAGISVPsGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSS--ILG---RVSlggsg 175
Cdd:PRK07577  65 EIHPVDAIVNNVGIALP-QPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREqGRIVNICSraIFGaldRTS----- 138

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226510520 176 gYCISKYGIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:PRK07577 139 -YSAAKSALVGCTRTWALELAEYGITVNAVAPG 170
PRK08278 PRK08278
SDR family oxidoreductase;
27-219 5.38e-09

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 56.07  E-value: 5.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACR------KEEG-----AEELRRKTSERLeTVILDVTKTENIVAATQ 95
Cdd:PRK08278   4 LSGKTLFITGASRGIGLAIALRAARDGANIVIAAKtaephpKLPGtihtaAEEIEAAGGQAL-PLVGDVRDEDQVAAAVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  96 WVKERVGnrGLWGLVNNAG-ISVPSGPNEWMKKQDFasVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSS--ILGRVSL 171
Cdd:PRK08278  83 KAVERFG--GIDICVNNASaINLTGTEDTPMKRFDL--MQQINVRGTFLVSQACLPHLKKSEnPHILTLSPplNLDPKWF 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 226510520 172 GGSGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEP---------GFFLTGMASSAR 219
Cdd:PRK08278 159 APHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWPrttiataavRNLLGGDEAMRR 215
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 26-212 5.51e-09

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 56.01  E-value: 5.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  26 HLQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVI---LDVTKTENIVAATQWVKERVG 102
Cdd:PRK06113   8 RLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFacrCDITSEQELSALADFALSKLG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 nrGLWGLVNNAGisvPSGPNEW-MKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVV-NVSSILGRVSLGGSGGYCIS 180
Cdd:PRK06113  88 --KVDILVNNAG---GGGPKPFdMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVIlTITSMAAENKNINMTSYASS 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 226510520 181 KYGIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:PRK06113 163 KAAASHLVRNMAFDLGEKNIRVNGIAPGAILT 194
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 27-208 6.31e-09

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


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 55.48  E-value: 6.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRK----------------EEGAEELRRKTSERLeTVILDVTKTENI 90
Cdd:cd05338    1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTasegdngsakslpgtiEETAEEIEAAGGQAL-PIVVDVRDEDQV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  91 VAATQWVKERVGnrGLWGLVNNAGISVPSGPNEWMKKQdFASVLDVNLLGLIEVTLSMLPLVRKA-RGRVVNVSSILGRV 169
Cdd:cd05338   80 RALVEATVDQFG--RLDILVNNAGAIWLSLVEDTPAKR-FDLMQRVNLRGTYLLSQAALPHMVKAgQGHILNISPPLSLR 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 226510520 170 SLGGSGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:cd05338  157 PARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPS 195
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-217 9.36e-09

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 55.11  E-value: 9.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVL--AACRKEEGAEELR--RKTSERLETVILDVTKTEnivAATQWVKERVG 102
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVvnAKKRAEEMNETLKmvKENGGEGIGVLADVSTRE---GCETLAKATID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 N-RGLWGLVNNAGISVPSgpnEWMKKQD--FASVLDVNLLGLIEVTLSMLPLVRKArGRVVNVSSILGRVSLGGSGGYCI 179
Cdd:PRK06077  81 RyGVADILVNNAGLGLFS---PFLNVDDklIDKHISTDFKSVIYCSQELAKEMREG-GAIVNIASVAGIRPAYGLSIYGA 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 226510520 180 SKYGIEAFSDSLRRELRYfGVKVAIIEPGFFLTGMASS 217
Cdd:PRK06077 157 MKAAVINLTKYLALELAP-KIRVNAIAPGFVKTKLGES 193
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-214 1.50e-08

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 55.61  E-value: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLaaCRKEEGAEELRRKTSERL--ETVILDVTKTENIVAATQWVKERVGnr 104
Cdd:PRK08261 208 LAGKVALVTGAARGIGAAIAEVLARDGAHVV--CLDVPAAGEALAAVANRVggTALALDITAPDAPARIAEHLAERHG-- 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 105 GLWGLVNNAGIS-----VPSGPNEWmkkqdfASVLDVNLLGLIEVTLSML-PLVRKARGRVVNVSSILGrvsLGGSGG-- 176
Cdd:PRK08261 284 GLDIVVHNAGITrdktlANMDEARW------DSVLAVNLLAPLRITEALLaAGALGDGGRIVGVSSISG---IAGNRGqt 354

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 226510520 177 -YCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:PRK08261 355 nYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQM 393
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-207 1.57e-08

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 54.79  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVL-----AACRKEEGAEELRRKTSeRLETVILDVTKTENivaATQWVKERV 101
Cdd:PRK07792  10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVvndvaSALDASDVLDEIRAAGA-KAVAVAGDISQRAT---ADELVATAV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 102 GNRGLWGLVNNAGIS----VPSgpnewMKKQDFASVLDVNLLGLIEVTLSMLPLVR-KAR-------GRVVNVSSILGRV 169
Cdd:PRK07792  86 GLGGLDIVVNNAGITrdrmLFN-----MSDEEWDAVIAVHLRGHFLLTRNAAAYWRaKAKaaggpvyGRIVNTSSEAGLV 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 226510520 170 SLGGSGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEP 207
Cdd:PRK07792 161 GPVGQANYGAAKAGITALTLSAARALGRYGVRANAICP 198
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 27-208 1.67e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 54.35  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLetVILDVTKTENIVAATQWVKERVGNRGL 106
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGGLF--VPTDVTDEDAVNALFDTAAETYGSVDI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 wgLVNNAGISVP-------SGPNEWMKkqdfasVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSIlgrVSLGGSG--- 175
Cdd:PRK06057  83 --AFNNAGISPPeddsilnTGLDAWQR------VQDVNLTSVYLCCKAALPhMVRQGKGSIINTASF---VAVMGSAtsq 151

                        170       180       190
                 ....*....|....*....|....*....|....
gi 226510520 176 -GYCISKYGIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:PRK06057 152 iSYTASKGGVLAMSRELGVQFARQGIRVNALCPG 185
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 25-185 5.48e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 53.09  E-value: 5.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  25 DHLQDKYVFITGCGSGFGNLLARQLDRRGMRVLAAC-RKEEGAEELRRKTSERLETVIL------DVTKTENIVAATQwv 97
Cdd:PRK06198   2 GRLDGKVALVTGGTQGLGAAIARAFAERGAAGLVICgRNAEKGEAQAAELEALGAKAVFvqadlsDVEDCRRVVAAAD-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  98 kERVGnrGLWGLVNNAGIS-----VPSGPnewmkkQDFASVLDVNLLG---LIEVTLSMLpLVRKARGRVVNVSSIlgrV 169
Cdd:PRK06198  80 -EAFG--RLDALVNAAGLTdrgtiLDTSP------ELFDRHFAVNVRApffLMQEAIKLM-RRRKAEGTIVNIGSM---S 146

                        170
                 ....*....|....*....
gi 226510520 170 SLGGS---GGYCISKYGIE 185
Cdd:PRK06198 147 AHGGQpflAAYCASKGALA 165
PRK07856 PRK07856
SDR family oxidoreductase;
27-215 7.43e-08

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 52.63  E-value: 7.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRktserLETVILDVTKTENIVAATQWVKERVGnrGL 106
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETVDGRP-----AEFHAADVRDPDQVAALVDAIVERHG--RL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAGISvPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRK--ARGRVVNVSSILGRVSLGGSGGYCISKYGI 184
Cdd:PRK07856  77 DVLVNNAGGS-PYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQqpGGGSIVNIGSVSGRRPSPGTAAYGAAKAGL 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226510520 185 EAFSDSLRRElryFG--VKVAIIEPGFFLTGMA 215
Cdd:PRK07856 156 LNLTRSLAVE---WApkVRVNAVVVGLVRTEQS 185
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 33-216 9.83e-08

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 52.27  E-value: 9.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  33 FITGCGSGFGNLLARQLDRRGMRV-LAACRKEEGAEELRRKTSE---RLETVILDVTKTENIVAATQWVKERVGnrGLWG 108
Cdd:PRK12745   6 LVTGGRRGIGLGIARALAAAGFDLaINDRPDDEELAATQQELRAlgvEVIFFPADVADLSAHEAMLDAAQAAWG--RIDC 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 109 LVNNAGISVPS-GPNEWMKKQDFASVLDVNLLGLIEVT-------LSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCIS 180
Cdd:PRK12745  84 LVNNAGVGVKVrGDLLDLTPESFDRVLAINLRGPFFLTqavakrmLAQPEPEELPHRSIVFVSSVNAIMVSPNRGEYCIS 163

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226510520 181 KYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMAS 216
Cdd:PRK12745 164 KAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTA 199
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 25-228 1.29e-07

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


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 51.77  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  25 DHLQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEelrrKTSERLETVILDVTKT----------ENIVAAT 94
Cdd:cd08936    6 DPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVD----RAVATLQGEGLSVTGTvchvgkaedrERLVATA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  95 QwvkERVGnrGLWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRK-ARGRVVNVSSILGRVSLGG 173
Cdd:cd08936   82 V---NLHG--GVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKrGGGSVVIVSSVAAFHPFPG 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 226510520 174 SGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASsarlcsniqMLW 228
Cdd:cd08936  157 LGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSS---------ALW 202
DUF1776 pfam08643
Fungal family of unknown function (DUF1776); This is a fungal family of unknown function. One ...
 44-304 1.57e-07

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: 52.04  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520   44 LLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKTENIVAA---------TQWVKERVGNRG---LWGLVN 111
Cdd:pfam08643  19 AIALDLERRGFIVFVTVTSAKDYKTVESEQRPDIRPLSLDDTAPSSIEASleeflqlleTPHVPFPGAKPHvlrLRGVIL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  112 NAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVR----KARGRVVNvSSILGRVSLGGSGGYCISKYGIEAF 187
Cdd:pfam08643  99 VPSLSYPTGPIENIPPSSWASEFNSRLLNYYLTLQGLLPLLRsrsqKAQIIVFN-PSISSSLNLPYHAPEALVSSALSTL 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  188 SDSLRRELRYFGVKVAIIEPGFF--LTGMASSARLCSNIQMLWDQTSSEIREIYGEKYLASYLKNLNELDQRCN---KDL 262
Cdd:pfam08643 178 FTTLKRELRPHGIDVTQIKLGNLdlSNGSASNYKYLNIAGSEVLSWSEIMRALYGPNYVSIQSKAIGIRSTRGSslrELH 257

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 226510520  263 SVVTDCMEHALTachPRTRYsAGWDAKLFFTPLSYLPTFLVD 304
Cdd:pfam08643 258 NALFDLLYGSSP---KPVVY-CGKGARLYSWVGKWLPEWLLS 295
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 27-212 2.54e-07

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 50.92  E-value: 2.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACR---KEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGN 103
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRdpaKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 RGLwgLVNNAGISVPSgPNEWMKKQDFASVLDVNLLGLIEVTLSML-PLVRKARGRVVNVSSILGRVSLGGSGGYCISKY 182
Cdd:PRK07523  88 IDI--LVNNAGMQFRT-PLEDFPADAFERLLRTNISSVFYVGQAVArHMIARGAGKIINIASVQSALARPGIAPYTATKG 164

                        170       180       190
                 ....*....|....*....|....*....|
gi 226510520 183 GIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:PRK07523 165 AVGNLTKGMATDWAKHGLQCNAIAPGYFDT 194
PRK07102 PRK07102
SDR family oxidoreductase;
30-214 2.83e-07

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 50.69  E-value: 2.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEG----AEELRRKTSERLETVILDVTKTENIVAATQwvkervgnrG 105
Cdd:PRK07102   2 KKILIIGATSDIARACARRYAAAGARLYLAARDVERlerlADDLRARGAVAVSTHELDILDTASHAAFLD---------S 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 106 LWGLVNNAGISVPSGPNEWMKKQDFA---SVLDVNLLGlievTLSMLPLVRK---ARGR--VVNVSSIL---GRVS--LG 172
Cdd:PRK07102  73 LPALPDIVLIAVGTLGDQAACEADPAlalREFRTNFEG----PIALLTLLANrfeARGSgtIVGISSVAgdrGRASnyVY 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 226510520 173 GSGgycisKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGM 214
Cdd:PRK07102 149 GSA-----KAALTAFLSGLRNRLFKSGVHVLTVKPGFVRTPM 185
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 27-208 3.18e-07

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 50.72  E-value: 3.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFgNL-LARQLDRRGMRVLAACRKEE----GAEELRRKTSERLeTVILDVTKTENIVAATQWVKERV 101
Cdd:PRK07576   7 FAGKNVVVVGGTSGI-NLgIAQAFARAGANVAVASRSQEkvdaAVAQLQQAGPEGL-GVSADVRDYAAVEAAFAQIADEF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 102 GNRGLwgLVNNAGISVPSgPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:PRK07576  85 GPIDV--LVSGAAGNFPA-PAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPGASIIQISAPQAFVPMPMQAHVCAAK 161

                        170       180
                 ....*....|....*....|....*..
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:PRK07576 162 AGVDMLTRTLALEWGPEGIRVNSIVPG 188
PRK07062 PRK07062
SDR family oxidoreductase;
27-168 3.66e-07

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 50.43  E-value: 3.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVlAACRKEEG------AEELRRKTSERLETVILDVTKTENIVAATQWVKER 100
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASV-AICGRDEErlasaeARLREKFPGARLLAARCDVLDEADVAAFAAAVEAR 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226510520 101 VGnrGLWGLVNNAGISVPS----GPNE-WMKKqdfasvLDVNLLGLIEVTLSMLPLVRKA-RGRVVNVSSILGR 168
Cdd:PRK07062  85 FG--GVDMLVNNAGQGRVStfadTTDDaWRDE------LELKYFSVINPTRAFLPLLRASaAASIVCVNSLLAL 150
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 34-164 3.88e-07

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: 50.29  E-value: 3.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  34 ITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKT-----SERLETVILDVTKTENIVAATQWVKERvgNRGLWG 108
Cdd:cd09808    6 ITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIetesgNQNIFLHIVDMSDPKQVWEFVEEFKEE--GKKLHV 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 226510520 109 LVNNAGISVPSGP-NEWMKKQDFASvldvNLLGLIEVTLSMLPLVRKARG-RVVNVSS 164
Cdd:cd09808   84 LINNAGCMVNKRElTEDGLEKNFAT----NTLGTYILTTHLIPVLEKEEDpRVITVSS 137
PRK09135 PRK09135
pteridine reductase; Provisional
 28-195 3.97e-07

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 50.31  E-value: 3.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  28 QDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEG-----AEELRRKTSERLETVILDVTKTENIVAATQWVKERVG 102
Cdd:PRK09135   5 SAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRSAAeadalAAELNALRPGSAAALQADLLDPDALPELVAACVAAFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 nrGLWGLVNNAGISVPSGPNEwMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISKY 182
Cdd:PRK09135  85 --RLDALVNNASSFYPTPLGS-ITEAQWDDLFASNLKAPFFLSQAAAPQLRKQRGAIVNITDIHAERPLKGYPVYCAAKA 161

                        170
                 ....*....|...
gi 226510520 183 GIEAFSDSLRREL 195
Cdd:PRK09135 162 ALEMLTRSLALEL 174
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 25-208 4.41e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 50.42  E-value: 4.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  25 DHLQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEG-AEELRRKTSERLETVIL---DVTKT---ENIVAATqwV 97
Cdd:PRK06701  42 GKLKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEdANETKQRVEKEGVKCLLipgDVSDEafcKDAVEET--V 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  98 KErVGnrGLWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVrKARGRVVNVSSILGrvsLGGSG-- 175
Cdd:PRK06701 120 RE-LG--RLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL-KQGSAIINTGSITG---YEGNEtl 192

                        170       180       190
                 ....*....|....*....|....*....|....
gi 226510520 176 -GYCISKYGIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:PRK06701 193 iDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPG 226
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 31-219 5.89e-07

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 50.25  E-value: 5.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  31 YVFITGCGSGFGNLLARQLDRRGMRVLAACRK----EEGAEELRRKTSE-RLETVILDVTKteNIVAATQWVKERVGNRG 105
Cdd:PLN02780  55 WALVTGPTDGIGKGFAFQLARKGLNLVLVARNpdklKDVSDSIQSKYSKtQIKTVVVDFSG--DIDEGVKRIKETIEGLD 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 106 LWGLVNNAGISVPSGpnEWMKKQD---FASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRV--SLGGSGGYCI 179
Cdd:PLN02780 133 VGVLINNVGVSYPYA--RFFHEVDeelLKNLIKVNVEGTTKVTQAVLPgMLKRKKGAIINIGSGAAIVipSDPLYAVYAA 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 226510520 180 SKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSAR 219
Cdd:PLN02780 211 TKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMASIRR 250
PRK09730 PRK09730
SDR family oxidoreductase;
34-238 8.58e-07

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 49.46  E-value: 8.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  34 ITGCGSGFGNLLARQLDRRGMRV-LAACRKEEGAEELRRKTSE---RLETVILDVTKTENIVAATQWVKERVGNrgLWGL 109
Cdd:PRK09730   6 VTGGSRGIGRATALLLAQEGYTVaVNYQQNLHAAQEVVNLITQaggKAFVLQADISDENQVVAMFTAIDQHDEP--LAAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 110 VNNAGISVPSGPNEWMKKQDFASVLDVNLLGLI----EVTLSMLPLVRKARGRVVNVSSILGRvsLGGSG---GYCISKY 182
Cdd:PRK09730  84 VNNAGILFTQCTVENLTAERINRVLSTNVTGYFlccrEAVKRMALKHGGSGGAIVNVSSAASR--LGAPGeyvDYAASKG 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226510520 183 GIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSA-------RLCSNIQMLWDQTSSEIREI 238
Cdd:PRK09730 162 AIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASGgepgrvdRVKSNIPMQRGGQPEEVAQA 224
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 32-174 1.22e-06

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: 49.44  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGCGSGFGNLLARQLDRRGM-RVLAACRKEEGAEELRRKT---SERLETVILDVTKTENIvaaTQWVKE-RVGNRGL 106
Cdd:cd09810    4 VVITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQEVgmpKDSYSVLHCDLASLDSV---RQFVDNfRRTGRPL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226510520 107 WGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLG-LIEVTLSMLPLVRK--ARGRVVNVSSILGRVS-LGGS 174
Cdd:cd09810   81 DALVCNAAVYLPTAKEPRFTADGFELTVGVNHLGhFLLTNLLLEDLQRSenASPRIVIVGSITHNPNtLAGN 152
PRK05854 PRK05854
SDR family oxidoreductase;
27-168 1.63e-06

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 48.91  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACR---KEEGA-EELRRKTSE-RLETVILDVTKTENIVAATQWVKERv 101
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRnraKGEAAvAAIRTAVPDaKLSLRALDLSSLASVAALGEQLRAE- 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226510520 102 gNRGLWGLVNNAGISVPsgPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGR 168
Cdd:PRK05854  91 -GRPIHLLINNAGVMTP--PERQTTADGFELQFGTNHLGHFALTAHLLPLLRAGRARVTSQSSIAAR 154
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 32-218 2.03e-06

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: 47.92  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGcGSGF-GNLLARQLDRRGMRVLAACRKEEGAEELRRKtseRLETVILDVTKTENIVAATQwvkervgnrGLWGLV 110
Cdd:COG0702    2 ILVTG-ATGFiGRRVVRALLARGHPVRALVRDPEKAAALAAA---GVEVVQGDLDDPESLAAALA---------GVDAVF 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 111 NNAGISVpsgpnewmkKQDFASVLDvnllglievtlSMLPLVRKAR----GRVVNVSSIlgRVSLGGSGGYCISKYGIE- 185
Cdd:COG0702   69 LLVPSGP---------GGDFAVDVE-----------GARNLADAAKaagvKRIVYLSAL--GADRDSPSPYLRAKAAVEe 126

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226510520 186 AFSDSlrrelryfGVKVAIIEPGFFLTGMASSA 218
Cdd:COG0702  127 ALRAS--------GLPYTILRPGWFMGNLLGFF 151
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 32-220 2.85e-06

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


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 47.23  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGcGSGF-GNLLARQLDRRGMRVLAACRKEEGAEELRRKTserLETVILDVTKTENIVAATQwvkervgnrGLWGLV 110
Cdd:cd05243    2 VLVVG-ATGKvGRHVVRELLDRGYQVRALVRDPSQAEKLEAAG---AEVVVGDLTDAESLAAALE---------GIDAVI 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 111 NNAGisvpSGPnewmkkQDFASVLDVNLLGLIEvtlsmlpLVRKARG----RVVNVSSI---LGRVSLGGSGGYCISKYG 183
Cdd:cd05243   69 SAAG----SGG------KGGPRTEAVDYDGNIN-------LIDAAKKagvkRFVLVSSIgadKPSHPLEALGPYLDAKRK 131

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226510520 184 IEafsdslrRELRYFGVKVAIIEPGFFLTGMASSARL 220
Cdd:cd05243  132 AE-------DYLRASGLDYTIVRPGGLTDDPAGTGRV 161
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 30-211 3.65e-06

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


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 47.27  E-value: 3.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRK-EEGAEELRRKTSERLETVIL------DVTKTENIVAATQWVKERVG 102
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRsEAEAQRLKDELNALRNSAVLvqadlsDFAACADLVAAAFRAFGRCD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 NrglwgLVNNAGISVPSGPNEWMKkQDFASVLDVNLLGLIEVTLSMLPLVRK-ARGRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:cd05357   81 V-----LVNNASAFYPTPLGQGSE-DAWAELFGINLKAPYLLIQAFARRLAGsRNGSIINIIDAMTDRPLTGYFAYCMSK 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 226510520 182 YGIEAFSDSLRRELRYFgVKVAIIEPGFFL 211
Cdd:cd05357  155 AALEGLTRSAALELAPN-IRVNGIAPGLIL 183
PRK05867 PRK05867
SDR family oxidoreductase;
27-212 4.08e-06

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 47.34  E-value: 4.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEG----AEELRRKTSERLeTVILDVTKTENIVAATQWVKERVG 102
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDAleklADEIGTSGGKVV-PVCCDVSQHQQVTSMLDQVTAELG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 nrGLWGLVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGL-IEVTLSMLPLVRKARGrvvnvSSILGRVSLGGS------- 174
Cdd:PRK05867  86 --GIDIAVCNAGI-ITVTPMLDMPLEEFQRLQNTNVTGVfLTAQAAAKAMVKQGQG-----GVIINTASMSGHiinvpqq 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 226510520 175 -GGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:PRK05867 158 vSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILT 196
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 27-227 5.10e-06

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 47.05  E-value: 5.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEE-----------GAEELRRKTSERLeTVILDVTKTENIVAATQ 95
Cdd:cd09762    1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEphpklpgtiytAAEEIEAAGGKAL-PCIVDIRDEDQVRAAVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  96 WVKERVGnrGLWGLVNNA-GISVPSGPNEWMKKQDFasVLDVNLLGLIEVTLSMLPLVRKARG-RVVNVSSILG--RVSL 171
Cdd:cd09762   80 KAVEKFG--GIDILVNNAsAISLTGTLDTPMKRYDL--MMGVNTRGTYLCSKACLPYLKKSKNpHILNLSPPLNlnPKWF 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226510520 172 GGSGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPgffLTGMASSArlcsnIQML 227
Cdd:cd09762  156 KNHTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWP---RTAIATAA-----MNML 203
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 25-231 8.72e-06

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


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 46.52  E-value: 8.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  25 DHLQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEgaEELRRKTSERLET-----VIL--DVTKTENIVAATQWV 97
Cdd:cd05355   22 GKLKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEE--EDDAEETKKLIEEegrkcLLIpgDLGDESFCRDLVKEV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  98 KERVGnrGLWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKArGRVVNVSSILGRVslgGSG-- 175
Cdd:cd05355  100 VKEFG--KLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKKG-SSIINTTSVTAYK---GSPhl 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 226510520 176 -GYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSARLCSNIQMLWDQT 231
Cdd:cd05355  174 lDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIPSSFPEEKVSEFGSQV 230
PRK05717 PRK05717
SDR family oxidoreductase;
30-209 8.74e-06

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 46.42  E-value: 8.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSERLETVILDVTKtENIVAATqwVKERVGNRG-LWG 108
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFIAMDVAD-EAQVAAG--VAEVLGQFGrLDA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 109 LVNNAGISVP-SGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARGRVVNVSSILGRVSLGGSGGYCISKYGIEAF 187
Cdd:PRK05717  88 LVCNAAIADPhNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHNGAIVNLASTRARQSEPDTEAYAASKGGLLAL 167

                        170       180
                 ....*....|....*....|....
gi 226510520 188 SDSLRRELryfG--VKVAIIEPGF 209
Cdd:PRK05717 168 THALAISL---GpeIRVNAVSPGW 188
PRK07985 PRK07985
SDR family oxidoreductase;
27-208 9.56e-06

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 46.53  E-value: 9.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAAC--RKEEGAEELRRKTSERLETVIL---DVTKTENIVAATQWVKERV 101
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISYlpVEEEDAQDVKKIIEECGRKAVLlpgDLSDEKFARSLVHEAHKAL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 102 GNRGLWGLVNNAGISVPSGPNewMKKQDFASVLDVNLLGLIEVTLSMLPLVRKArGRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:PRK07985 127 GGLDIMALVAGKQVAIPDIAD--LTSEQFQKTFAINVFALFWLTQEAIPLLPKG-ASIITTSSIQAYQPSPHLLDYAATK 203

                        170       180
                 ....*....|....*....|....*..
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:PRK07985 204 AAILNYSRGLAKQVAEKGIRVNIVAPG 230
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
28-173 2.32e-05

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


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 45.37  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  28 QDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSER---LETVILDVTKTENIvaaTQWVKE-RVGN 103
Cdd:COG5748    5 QKSTVIITGASSGVGLYAAKALADRGWHVIMACRDLEKAEAAAQELGIPpdsYTIIHIDLASLESV---RRFVADfRALG 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226510520 104 RGLWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARG---RVVnvssILGRV-----SLGG 173
Cdd:COG5748   82 RPLDALVCNAAVYYPLLKEPLRSPDGYELSVATNHLGHFLLCNLLLEDLKKSPAsdpRLV----ILGTVtanpkELGG 155
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-219 2.73e-05

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 44.90  E-value: 2.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAAcrKEEGAEELRRK---TSERLETVILDVTKTENIVAATQWVKERVGN 103
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVGV--GVAEAPETQAQveaLGRKFHFITADLIQQKDIDSIVSQAVEVMGH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 104 RGLwgLVNNAGISVPSGPNEWmKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR--GRVVNVSSILG-----RVSlggsgG 176
Cdd:PRK12481  84 IDI--LINNAGIIRRQDLLEF-GNKDWDDVININQKTVFFLSQAVAKQFVKQGngGKIINIASMLSfqggiRVP-----S 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 226510520 177 YCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSAR 219
Cdd:PRK12481 156 YTASKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAALR 198
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 30-208 3.52e-05

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 44.28  E-value: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  30 KYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSE---RLETVILDVTKTENIVAATQWVKERVGNrgL 106
Cdd:PRK07677   2 KVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQfpgQVLTVQMDVRNPEDVQKMVEQIDEKFGR--I 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 107 WGLVNNAG--ISVPS---GPNEWmkkqdfASVLDVNLLGLIEVT--LSMLPLVRKARGRVVNvssILGRVSLGGSGGYCI 179
Cdd:PRK07677  80 DALINNAAgnFICPAedlSVNGW------NSVIDIVLNGTFYCSqaVGKYWIEKGIKGNIIN---MVATYAWDAGPGVIH 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226510520 180 S---KYGIEAFSDSLRRELRY-FGVKVAIIEPG 208
Cdd:PRK07677 151 SaaaKAGVLAMTRTLAVEWGRkYGIRVNAIAPG 183
PRK06196 PRK06196
oxidoreductase; Provisional
 27-170 4.38e-05

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 44.67  E-value: 4.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTsERLETVILDVTKTENIVA-ATQWVKERvgnRG 105
Cdd:PRK06196  24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGI-DGVEVVMLDLADLESVRAfAERFLDSG---RR 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 106 LWGLVNNAGI----SVPSGPNEWMKkqdFAsvldVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVS 170
Cdd:PRK06196 100 IDILINNAGVmacpETRVGDGWEAQ---FA----TNHLGHFALVNLLWPaLAAGAGARVVALSSAGHRRS 162
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
27-212 4.41e-05

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 44.32  E-value: 4.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVL---AACRK--EEGAEELRRKTSERLeTVILDVTKTENIVAATQWVKERV 101
Cdd:PRK08063   2 FSGKVALVTGSSRGIGKAIALRLAEEGYDIAvnyARSRKaaEETAEEIEALGRKAL-AVKANVGDVEKIKEMFAQIDEEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 102 GnrGLWGLVNNAGisvpSG---PNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSIlgrvslgGSGGY 177
Cdd:PRK08063  81 G--RLDVFVNNAA----SGvlrPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGgGKIISLSSL-------GSIRY 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 226510520 178 C-------ISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:PRK08063 148 LenyttvgVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDT 189
PRK09186 PRK09186
flagellin modification protein A; Provisional
 27-167 7.77e-05

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 43.44  E-value: 7.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRK-----TSERLETVILDVTKTENIVAATQWVKERV 101
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESlgkefKSKKLSLVELDITDQESLEEFLSKSAEKY 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226510520 102 GNrgLWGLVNNAgisVPSGPNeWMKK------QDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILG 167
Cdd:PRK09186  82 GK--IDGAVNCA---YPRNKD-YGKKffdvslDDFNENLSLHLGSSFLFSQQFAKyFKKQGGGNLVNISSIYG 148
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
45-167 1.09e-04

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 42.68  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  45 LARQLDRRGMRVLAACRKEEGAEelrrktserLETVI-LDVTKTENIVAATQWVKERVGnrglwGLVNNAGISvPSGPNE 123
Cdd:PRK12428   1 TARLLRFLGARVIGVDRREPGMT---------LDGFIqADLGDPASIDAAVAALPGRID-----ALFNIAGVP-GTAPVE 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 226510520 124 wmkkqdfaSVLDVNLLGLIEVTLSMLPLVRkARGRVVNVSSILG 167
Cdd:PRK12428  66 --------LVARVNFLGLRHLTEALLPRMA-PGGAIVNVASLAG 100
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 27-212 1.35e-04

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


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 42.82  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACR----KEEGAEELRRKTSERLETVILDVTKTENIVAATQWVKERVG 102
Cdd:cd09763    1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRtilpQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 NRgLWGLVNNA------GISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKA-RGRVVNVSSiLGRVSLGGSG 175
Cdd:cd09763   81 GR-LDILVNNAyaavqlILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAgKGLIVIISS-TGGLEYLFNV 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226510520 176 GYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:cd09763  159 AYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRT 195
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 27-220 1.41e-04

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: 43.14  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLA-ACRKEEGAEELRRKTSE-----RLETVILDVTKTEnivAATQWVKER 100
Cdd:cd05274  148 GLDGTYLITGGLGGLGLLVARWLAARGARHLVlLSRRGPAPRAAARAALLraggaRVSVVRCDVTDPA---ALAALLAEL 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 101 VGNRGLWGLVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGLievtLSMLPLVRKARG-RVVNVSSILGrvSLGGSG--GY 177
Cdd:cd05274  225 AAGGPLAGVIHAAGV-LRDALLAELTPAAFAAVLAAKVAGA----LNLHELTPDLPLdFFVLFSSVAA--LLGGAGqaAY 297

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 226510520 178 CISkygiEAFSDSLRRELRYFGVKVAIIEPGFF-LTGMASSARL 220
Cdd:cd05274  298 AAA----NAFLDALAAQRRRRGLPATSVQWGAWaGGGMAAAAAL 337
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 29-164 2.52e-04

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 42.20  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  29 DKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEE-----LRRKTSERLETVILDVTKTENIVAATQWVKERvgN 103
Cdd:cd09809    1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAavsriLEEWHKARVEAMTLDLASLRSVQRFAEAFKAK--N 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226510520 104 RGLWGLVNNAGI-SVPsgpneWMKKQD-FASVLDVNLLGLIEVTLSMLPLVRK-ARGRVVNVSS 164
Cdd:cd09809   79 SPLHVLVCNAAVfALP-----WTLTEDgLETTFQVNHLGHFYLVQLLEDVLRRsAPARVIVVSS 137
PRK06128 PRK06128
SDR family oxidoreductase;
27-217 3.01e-04

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 41.77  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEE--GAEELRR--KTSERLETVILDVTKTENIvaATQWVKERV- 101
Cdd:PRK06128  53 LQGRKALITGADSGIGRATAIAFAREGADIALNYLPEEeqDAAEVVQliQAEGRKAVALPGDLKDEAF--CRQLVERAVk 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 102 GNRGLWGLVNNAGISVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVrKARGRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:PRK06128 131 ELGGLDILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHL-PPGASIINTGSIQSYQPSPTLLDYASTK 209

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASS 217
Cdd:PRK06128 210 AAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPS 245
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 66-217 3.07e-04

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 41.70  E-value: 3.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  66 AEELRrKTSERLETVILDVTKTENIVAATQWVKERVGNRGLwgLVNNAGISVpsgpnewmkKQDF----ASVLD----VN 137
Cdd:PRK12859  60 QEELL-KNGVKVSSMELDLTQNDAPKELLNKVTEQLGYPHI--LVNNAAYST---------NNDFsnltAEELDkhymVN 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 138 LLGLIEVTLSMLPLVRKARG-RVVNVSSILGRVSLGGSGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMAS 216
Cdd:PRK12859 128 VRATTLLSSQFARGFDKKSGgRIINMTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGWMT 207


                 .
gi 226510520 217 S 217
Cdd:PRK12859 208 E 208
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 26-208 3.76e-04

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 41.21  E-value: 3.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  26 HLQDKYVFITGC--GSGFGNLLARQLDRRGMRVL------------AACRKEEG---AEELRRKtSERLETVILDVTKTE 88
Cdd:PRK12748   2 PLMKKIALVTGAsrLNGIGAAVCRRLAAKGIDIFftywspydktmpWGMHDKEPvllKEEIESY-GVRCEHMEIDLSQPY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  89 NIVAATQWVKERVGNRGLwgLVNNAGISVPSGPNEwmkkqdfasvLDVNLLGL---IEVTLSMLpLVR--------KARG 157
Cdd:PRK12748  81 APNRVFYAVSERLGDPSI--LINNAAYSTHTRLEE----------LTAEQLDKhyaVNVRATML-LSSafakqydgKAGG 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 226510520 158 RVVNVSS--ILGrvSLGGSGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPG 208
Cdd:PRK12748 148 RIINLTSgqSLG--PMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPG 198
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 27-212 5.10e-04

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 40.99  E-value: 5.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRRKTSER----LETVILDVTKTENIVAATQWVKErVG 102
Cdd:PRK08339   6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSEsnvdVSYIVADLTKREDLERTVKELKN-IG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 103 NRGLWGLvnNAGISVPSGPNEwMKKQDFASVLDVNLLGLIEVTLSMLP-LVRKARGRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:PRK08339  85 EPDIFFF--STGGPKPGYFME-MSMEDWEGAVKLLLYPAVYLTRALVPaMERKGFGRIIYSTSVAIKEPIPNIALSNVVR 161

                        170       180       190
                 ....*....|....*....|....*....|.
gi 226510520 182 YGIEAFSDSLRRELRYFGVKVAIIEPGFFLT 212
Cdd:PRK08339 162 ISMAGLVRTLAKELGPKGITVNGIMPGIIRT 192
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-219 6.82e-04

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 40.63  E-value: 6.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRVLAAcRKEEGAEELRRKTSE--RLETVILDVTKTENIVAATQWVKERVGNR 104
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGI-NIVEPTETIEQVTALgrRFLSLTADLRKIDGIPALLERAVAEFGHI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 105 GLwgLVNNAGISVPSGPNEWmKKQDFASVLDVNllglIEVTLSMLPLVRKA------RGRVVNVSSILG-----RVSlgg 173
Cdd:PRK08993  87 DI--LVNNAGLIRREDAIEF-SEKDWDDVMNLN----IKSVFFMSQAAAKHfiaqgnGGKIINIASMLSfqggiRVP--- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 226510520 174 sgGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSAR 219
Cdd:PRK08993 157 --SYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLR 200
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 31-219 9.15e-04

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


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 40.28  E-value: 9.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520   31 YVFITGCGSGFGNLLARQLDRR-----GMRVLAAcRKEEGAEELR-----RKTSERLETVILDVTKTENIVAATQWVKER 100
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKClkspgSVLVLSA-RNDEALRQLKaeigaERSGLRVVRVSLDLGAEAGLEQLLKALREL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  101 VGNRGLWG--LVNNAGI--SVPSGPNEWMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARG---RVVNVSSILGRVSLGG 173
Cdd:TIGR01500  81 PRPKGLQRllLINNAGTlgDVSKGFVDLSDSTQVQNYWALNLTSMLCLTSSVLKAFKDSPGlnrTVVNISSLCAIQPFKG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 226510520  174 SGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEPGFFLTGMASSAR 219
Cdd:TIGR01500 161 WALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQQVR 206
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 34-165 9.15e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 40.39  E-value: 9.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  34 ITGCGSGFGNLLARQLDRRGMRVLAACRK-EEGAEELRRKTSERLETVI----LDVTKTENIVAATQWVKERVGNRGLwg 108
Cdd:PRK06197  21 VTGANTGLGYETAAALAAKGAHVVLAVRNlDKGKAAAARITAATPGADVtlqeLDLTSLASVRAAADALRAAYPRIDL-- 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 226510520 109 LVNNAGISVPsgPNEwMKKQDFASVLDVNLLGLIEVTLSMLPLVRKARG-RVVNVSSI 165
Cdd:PRK06197  99 LINNAGVMYT--PKQ-TTADGFELQFGTNHLGHFALTGLLLDRLLPVPGsRVVTVSSG 153
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 12-108 1.06e-03

2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176645 [Multi-domain]  Cd Length: 323  Bit Score: 40.34  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  12 WMLLRFFRERQvvdhlQDKYVFITGCGSGFGNLLARQLDRRGMRVLAACRKEEGAEELRrktsERLETVILDvTKTENIV 91
Cdd:cd05282  127 WLMLTEYLKLP-----PGDWVIQNAANSAVGRMLIQLAKLLGFKTINVVRRDEQVEELK----ALGADEVID-SSPEDLA 196

                         90
                 ....*....|....*..
gi 226510520  92 AAtqwVKERVGNRGLWG 108
Cdd:cd05282  197 QR---VKEATGGAGARL 210
SDR_a2 cd05245
atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified ...
 32-95 1.26e-03

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


Pssm-ID: 187556 [Multi-domain]  Cd Length: 293  Bit Score: 40.02  E-value: 1.26e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226510520  32 VFITGcGSGF-GNLLARQLDRRGMRVLAACRKEEGAeeLRRKTSERLETVILDVTKTENIVAATQ 95
Cdd:cd05245    1 VLVTG-ATGYvGGRLVPRLLQEGHQVRALVRSPEKL--ADRPWSERVTVVRGDLEDPESLRAALE 62
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
 32-165 1.33e-03

uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 39.96  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  32 VFITGcGSGF-GNLLARQLDRRGMRVLAACRKEEGAEELRRktsERLETVILDVTKTENIVAATQWVkERVgnrglwglV 110
Cdd:cd05228    1 ILVTG-ATGFlGSNLVRALLAQGYRVRALVRSGSDAVLLDG---LPVEVVEGDLTDAASLAAAMKGC-DRV--------F 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226510520 111 NNAGIsvpsgPNEWMKkqDFASVLDVNLLGlievTLSMLPLVRKAR-GRVVNVSSI 165
Cdd:cd05228   68 HLAAF-----TSLWAK--DRKELYRTNVEG----TRNVLDAALEAGvRRVVHTSSI 112
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 27-207 2.77e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 38.89  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGSGFGNLLARQLDRRGMRV----LAACRKEEGAEElrrktsERLETVILD--------VTKTENI---V 91
Cdd:PRK07791   4 LDGRVVIVTGAGGGIGRAHALAFAAEGARVvvndIGVGLDGSASGG------SAAQAVVDEivaaggeaVANGDDIadwD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  92 AATQWVKERVGNRG-LWGLVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGLIeVTLSMLPLVRKAR--------GRVVNV 162
Cdd:PRK07791  78 GAANLVDAAVETFGgLDVLVNNAGI-LRDRMIANMSEEEWDAVIAVHLKGHF-ATLRHAAAYWRAEskagravdARIINT 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 226510520 163 SSILGRVSLGGSGGYCISKYGIEAFSDSLRRELRYFGVKVAIIEP 207
Cdd:PRK07791 156 SSGAGLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP 200
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 46-210 2.78e-03

haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. Haloalcohol dehalogenase show low sequence similarity to short-chain dehydrogenases/reductases (SDRs). Like the SDRs, haloalcohol dehalogenases have a conserved catalytic triad (Ser-Tyr-Lys/Arg), and form a Rossmann fold. However, the normal classical SDR NAD(P)-binding motif (TGXXGXG) and NAD-binding function is replaced with a halide binding site, allowing the enzyme to catalyze a dehalogenation reaction. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in 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: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 38.71  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  46 ARQLDRRGMRVlaACRKEE--GAEELRRKTSERLETVILDVTKTENIVAATQWVKERVGNrglwgLVNNAGISVPSGPNE 123
Cdd:cd05361   18 AEALTEDGYTV--VCHDASfaDAAERQAFESENPGTKALSEQKPEELVDAVLQAGGAIDV-----LVSNDYIPRPMNPID 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 124 WMKKQDFASVLDVNLLGLIEVTLSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISKYGIEAFSDSLRRELRYFGVKV 202
Cdd:cd05361   91 GTSEADIRQAFEALSIFPFALLQAAIAQMKKAGgGSIIFITSAVPKKPLAYNSLYGPARAAAVALAESLAKELSRDNILV 170


                 ....*...
gi 226510520 203 AIIEPGFF 210
Cdd:cd05361  171 YAIGPNFF 178
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
27-103 3.26e-03

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 38.56  E-value: 3.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  27 LQDKYVFITGCGS----GFGnlLARQLDRRGMRVLAACRKEEGAEELRR--KTSERLETVIL--DVTKTENIVAATQWVK 98
Cdd:PRK08594   5 LEGKTYVVMGVANkrsiAWG--IARSLHNAGAKLVFTYAGERLEKEVRElaDTLEGQESLLLpcDVTSDEEITACFETIK 82


                 ....*
gi 226510520  99 ERVGN 103
Cdd:PRK08594  83 EEVGV 87
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 34-204 8.34e-03

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


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 37.73  E-value: 8.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520  34 ITGCGSGFGNLLARQLDRRGMR--VLAACRKEEGAEELRRKTSERLET-------VILDVTKTenivAATQWVKERVGNR 104
Cdd:cd08953  210 VTGGAGGIGRALARALARRYGArlVLLGRSPLPPEEEWKAQTLAALEAlgarvlyISADVTDA----AAVRRLLEKVRER 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226510520 105 G--LWGLVNNAGIsVPSGPNEWMKKQDFASVLDVNLLGLIevtlSMLPLVRKAR-GRVVNVSSILGRVSLGGSGGYCISK 181
Cdd:cd08953  286 YgaIDGVIHAAGV-LRDALLAQKTAEDFEAVLAPKVDGLL----NLAQALADEPlDFFVLFSSVSAFFGGAGQADYAAAN 360

                        170       180
                 ....*....|....*....|...
gi 226510520 182 YGIEAFSDSLRReLRYFGVKVAI 204
Cdd:cd08953  361 AFLDAFAAYLRQ-RGPQGRVLSI 382
 
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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