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Conserved domains on  [gi|150247226|ref|NP_003699|]
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retinol dehydrogenase 16 isoform 1 [Homo sapiens]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 30-305 3.15e-140

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd09805:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 281  Bit Score: 397.42  E-value: 3.15e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTE--KGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVRDKGLW 107
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 108 GLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRVSLF-GGGYCISKYGVEAF 186
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 187 SDSLRRELSYFGVKVAMIEPGYFKTAVTSK-ERFLKSFLEIWDRSSPEVKEAYGEKFVADYKKSAEQMEQKCTQDLSLVT 265
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNsELWEKQAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 150247226 266 NCMEHALIACHPRTRYSAGWDAKLLYLPMSYMPTFLVDAI 305
Cdd:cd09805  241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFL 280
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 30-305 3.15e-140

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: 397.42  E-value: 3.15e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTE--KGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVRDKGLW 107
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 108 GLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRVSLF-GGGYCISKYGVEAF 186
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 187 SDSLRRELSYFGVKVAMIEPGYFKTAVTSK-ERFLKSFLEIWDRSSPEVKEAYGEKFVADYKKSAEQMEQKCTQDLSLVT 265
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNsELWEKQAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 150247226 266 NCMEHALIACHPRTRYSAGWDAKLLYLPMSYMPTFLVDAI 305
Cdd:cd09805  241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFL 280
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
27-306 2.07e-54

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 177.75  E-value: 2.07e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLR---GQTSDRLETVTLDVTKTESVAAAAQWVKEcvRD 103
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAaelRAAGARVEVVALDVTDPDAVAALAEAVLA--RF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 KGLWGLVNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSL-FGGGYCISKY 181
Cdd:COG0300   81 GPIDVLVNNAGVGGGGPFEEL-DLEDLRRVFEVNVFGPVRLTRALLPlMRARGRGRIVNVSSVAGLRGLpGMAAYAASKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 182 GVEAFSDSLRRELSYFGVKVAMIEPGYFKTavtskerflksflEIWDRSSPEvkeayGEKFVADYKKSAEQMeqkctqdl 261
Cdd:COG0300  160 ALEGFSESLRAELAPTGVRVTAVCPGPVDT-------------PFTARAGAP-----AGRPLLSPEEVARAI-------- 213

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 150247226 262 slvtncmeHALIAcHPRTRYSAGWDAKLLYLPMSYMPTfLVDAIM 306
Cdd:COG0300  214 --------LRALE-RGRAEVYVGWDARLLARLLRLLPR-LFDRLL 248
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 30-218 1.86e-48

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 160.47  E-value: 1.86e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226   30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLR---GQTSDRLETVTLDVTKTESVAAAAQWVKEcvRDKGL 106
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAkelGALGGKALFIQGDVTDRAQVKALVEQAVE--RLGRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  107 WGLVNNAGISlPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFGGG-YCISKYGVE 184
Cdd:pfam00106  79 DILVNNAGIT-GLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPYPGGSaYSASKAAVI 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 150247226  185 AFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKER 218
Cdd:pfam00106 158 GFTRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
PRK08017 PRK08017
SDR family oxidoreductase;
30-308 7.85e-40

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 140.22  E-value: 7.85e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRgqtSDRLETVTLDVTKTESVAAAAQWVKEcVRDKGLWGL 109
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDVARMN---SLGFTGILLDLDDPESVERAADEVIA-LTDNRLYGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 110 VNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVR-RARGRVVNVSSVMGRVSLFG-GGYCISKYGVEAFS 187
Cdd:PRK08017  79 FNNAGFGV-YGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLpHGEGRIVMTSSVMGLISTPGrGAYAASKYALEAWS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 188 DSLRRELSYFGVKVAMIEPGYFKTavtskeRFlksfleiwdrsSPEVKEAYGEKFVADykksaEQMEQKCTQDLSLVTNC 267
Cdd:PRK08017 158 DALRMELRHSGIKVSLIEPGPIRT------RF-----------TDNVNQTQSDKPVEN-----PGIAARFTLGPEAVVPK 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 150247226 268 MEHALIACHPRTRYSAGWDAKLLYLPMSYMPTFLVDAIMYW 308
Cdd:PRK08017 216 LRHALESPKPKLRYPVTLVTHAVMVLKRLLPGRMMDKILRG 256
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 32-216 4.03e-25

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: 100.75  E-value: 4.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226   32 VFITGCDSGFGKLLARQLDARGLRVLAACLT-EKGAEQLRGQTSD---RLETVTLDVTKTESVAAAaqwVKECVRDKG-L 106
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSsEEGAEEVVEELKAlgvKALGVVLDVSDREDVKAV---VEEIEEELGtI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  107 WGLVNNAGIslpTAPNELL--TKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGrvsLFGGG----YCIS 179
Cdd:TIGR01830  78 DILVNNAGI---TRDNLLMrmKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRsGRIINISSVVG---LMGNAgqanYAAS 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 150247226  180 KYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSK 216
Cdd:TIGR01830 152 KAGVIGFTKSLAKELASRNITVNAVAPGFIDTDMTDK 188
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 30-305 3.15e-140

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: 397.42  E-value: 3.15e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTE--KGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVRDKGLW 107
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 108 GLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRVSLF-GGGYCISKYGVEAF 186
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 187 SDSLRRELSYFGVKVAMIEPGYFKTAVTSK-ERFLKSFLEIWDRSSPEVKEAYGEKFVADYKKSAEQMEQKCTQDLSLVT 265
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNsELWEKQAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 150247226 266 NCMEHALIACHPRTRYSAGWDAKLLYLPMSYMPTFLVDAI 305
Cdd:cd09805  241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFL 280
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 30-288 4.04e-61

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: 195.14  E-value: 4.04e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKEcvRDKGLWGL 109
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIE--RFGRIDVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 110 VNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSL-FGGGYCISKYGVEAFS 187
Cdd:cd05374   79 VNNAGYGL-FGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGsGRIVNVSSVAGLVPTpFLGPYCASKAALEALS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 188 DSLRRELSYFGVKVAMIEPGYFKTAVTSKERflksfleIWDRSSPEvkeaygekfVADYKKSAEQMEQKCTQDLSL---- 263
Cdd:cd05374  158 ESLRLELAPFGIKVTIIEPGPVRTGFADNAA-------GSALEDPE---------ISPYAPERKEIKENAAGVGSNpgdp 221

                        250       260
                 ....*....|....*....|....*..
gi 150247226 264 --VTNCMEHALIACHPRTRYSAGWDAK 288
Cdd:cd05374  222 ekVADVIVKALTSESPPLRYFLGSDAL 248
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
27-306 2.07e-54

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 177.75  E-value: 2.07e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLR---GQTSDRLETVTLDVTKTESVAAAAQWVKEcvRD 103
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAaelRAAGARVEVVALDVTDPDAVAALAEAVLA--RF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 KGLWGLVNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSL-FGGGYCISKY 181
Cdd:COG0300   81 GPIDVLVNNAGVGGGGPFEEL-DLEDLRRVFEVNVFGPVRLTRALLPlMRARGRGRIVNVSSVAGLRGLpGMAAYAASKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 182 GVEAFSDSLRRELSYFGVKVAMIEPGYFKTavtskerflksflEIWDRSSPEvkeayGEKFVADYKKSAEQMeqkctqdl 261
Cdd:COG0300  160 ALEGFSESLRAELAPTGVRVTAVCPGPVDT-------------PFTARAGAP-----AGRPLLSPEEVARAI-------- 213

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 150247226 262 slvtncmeHALIAcHPRTRYSAGWDAKLLYLPMSYMPTfLVDAIM 306
Cdd:COG0300  214 --------LRALE-RGRAEVYVGWDARLLARLLRLLPR-LFDRLL 248
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 28-252 1.14e-50

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


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 167.67  E-value: 1.14e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  28 RDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKEcvRDKGLW 107
Cdd:COG4221    4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVA--EFGRLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 108 GLVNNAGISLPtAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSL-FGGGYCISKYGVEA 185
Cdd:COG4221   82 VLVNNAGVALL-GPLEELDPEDWDRMIDVNVKGVLYVTRAALPaMRARGSGHIVNISSIAGLRPYpGGAVYAATKAAVRG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150247226 186 FSDSLRRELSYFGVKVAMIEPGYFKTavtskerflksflEIWDRSSPEVKEAYGEKFVADYKKSAEQ 252
Cdd:COG4221  161 LSESLRAELRPTGIRVTVIEPGAVDT-------------EFLDSVFDGDAEAAAAVYEGLEPLTPED 214
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 30-218 1.86e-48

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 160.47  E-value: 1.86e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226   30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLR---GQTSDRLETVTLDVTKTESVAAAAQWVKEcvRDKGL 106
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAkelGALGGKALFIQGDVTDRAQVKALVEQAVE--RLGRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  107 WGLVNNAGISlPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFGGG-YCISKYGVE 184
Cdd:pfam00106  79 DILVNNAGIT-GLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPYPGGSaYSASKAAVI 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 150247226  185 AFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKER 218
Cdd:pfam00106 158 GFTRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
PRK08017 PRK08017
SDR family oxidoreductase;
30-308 7.85e-40

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 140.22  E-value: 7.85e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRgqtSDRLETVTLDVTKTESVAAAAQWVKEcVRDKGLWGL 109
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDVARMN---SLGFTGILLDLDDPESVERAADEVIA-LTDNRLYGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 110 VNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVR-RARGRVVNVSSVMGRVSLFG-GGYCISKYGVEAFS 187
Cdd:PRK08017  79 FNNAGFGV-YGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLpHGEGRIVMTSSVMGLISTPGrGAYAASKYALEAWS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 188 DSLRRELSYFGVKVAMIEPGYFKTavtskeRFlksfleiwdrsSPEVKEAYGEKFVADykksaEQMEQKCTQDLSLVTNC 267
Cdd:PRK08017 158 DALRMELRHSGIKVSLIEPGPIRT------RF-----------TDNVNQTQSDKPVEN-----PGIAARFTLGPEAVVPK 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 150247226 268 MEHALIACHPRTRYSAGWDAKLLYLPMSYMPTFLVDAIMYW 308
Cdd:PRK08017 216 LRHALESPKPKLRYPVTLVTHAVMVLKRLLPGRMMDKILRG 256
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 30-304 9.58e-40

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 140.42  E-value: 9.58e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGqtsdrLETVTLDVTKTESVAAAAQWVKEcvRDKGLWGL 109
Cdd:PRK06179   5 KVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIPG-----VELLELDVTDDASVQAAVDEVIA--RAGRIDVL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 110 VNNAGISLPTAPNELLTKQDfVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSL-FGGGYCISKYGVEAFS 187
Cdd:PRK06179  78 VNNAGVGLAGAAEESSIAQA-QALFDTNVFGILRMTRAVLPHMRAQGsGRIINISSVLGFLPApYMALYAASKHAVEGYS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 188 DSLRRELSYFGVKVAMIEPGYFKTavtskerflkSFleiwDRSSPEVKEAygekfVADYKKSAEQMEQkctqdlsLVTNC 267
Cdd:PRK06179 157 ESLDHEVRQFGIRVSLVEPAYTKT----------NF----DANAPEPDSP-----LAEYDRERAVVSK-------AVAKA 210

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 150247226 268 MEH-------------ALIACHPRTRYSAGWDAKLLYLPMSYMPTFLVDA 304
Cdd:PRK06179 211 VKKadapevvadtvvkAALGPWPKMRYTAGGQASLLSKLRRFMPAGAVDK 260
PRK05993 PRK05993
SDR family oxidoreductase;
30-308 1.40e-39

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 140.16  E-value: 1.40e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRgqtSDRLETVTLDVTKTESVAAAAQWVKECVRDKgLWGL 109
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALE---AEGLEAFQLDYAEPESIAALVAQVLELSGGR-LDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 110 VNNAGISLPTA----PNELLTKQdfvtiLDVNLLGVIDVTLSLLPLVR-RARGRVVNVSSVMGRVSL-FGGGYCISKYGV 183
Cdd:PRK05993  81 FNNGAYGQPGAvedlPTEALRAQ-----FEANFFGWHDLTRRVIPVMRkQGQGRIVQCSSILGLVPMkYRGAYNASKFAI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 184 EAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKErfLKSFLEIWD-RSSPEvKEAY--------GEKFVADYKKSAEQme 254
Cdd:PRK05993 156 EGLSLTLRMELQGSGIHVSLIEPGPIETRFRANA--LAAFKRWIDiENSVH-RAAYqqqmarleGGGSKSRFKLGPEA-- 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 150247226 255 qkctqdlslVTNCMEHALIACHPRTRYSAGWDAKLLYLPMSYMPTFLVDAIMYW 308
Cdd:PRK05993 231 ---------VYAVLLHALTAPRPRPHYRVTTPAKQGALLKRLLPARWLYRLLRK 275
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 32-226 4.09e-39

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


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 137.80  E-value: 4.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSD--RLETVTLDVTKTESVAAAAQWVKEcvRDKGLWGL 109
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEALggNAVAVQADVSDEEDVEALVEEALE--EFGRLDIL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 110 VNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFG-GGYCISKYGVEAFS 187
Cdd:cd05233   79 VNNAGIARPGPLEEL-TDEDWDRVLDVNLTGVFLLTRAALPhMKKQGGGRIVNISSVAGLRPLPGqAAYAASKAALEGLT 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 150247226 188 DSLRRELSYFGVKVAMIEPGYFKTAVTSKERFLKSFLEI 226
Cdd:cd05233  158 RSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKEL 196
PRK06182 PRK06182
short chain dehydrogenase; Validated
 30-306 5.18e-39

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 138.55  E-value: 5.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAAClteKGAEQLRGQTSDRLETVTLDVTKTESVAAA-AQWVKECVR-DKglw 107
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYGAA---RRVDKMEDLASLGVHPLSLDVTDEASIKAAvDTIIAEEGRiDV--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 108 gLVNNAGISLPTAPNELL---TKQDFvtilDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRV-SLFGGGYCISKYG 182
Cdd:PRK06182  78 -LVNNAGYGSYGAIEDVPideARRQF----EVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIyTPLGAWYHATKFA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 183 VEAFSDSLRRELSYFGVKVAMIEPGYFKT--AVTSKERFLKSfleiwDRSSPevkeaYGEKFVADYKKSAEQMEQKCTQD 260
Cdd:PRK06182 153 LEGFSDALRLEVAPFGIDVVVIEPGGIKTewGDIAADHLLKT-----SGNGA-----YAEQAQAVAASMRSTYGSGRLSD 222

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 150247226 261 LSLVTNCMEHALIACHPRTRYSAGWDAKLLYLPMSYMPTFLVDAIM 306
Cdd:PRK06182 223 PSVIADAISKAVTARRPKTRYAVGFGAKPLIFLRRILPDRAFDRLI 268
PRK06914 PRK06914
SDR family oxidoreductase;
30-298 2.64e-38

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 137.08  E-value: 2.64e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQT-----SDRLETVTLDVTKTESVAAAAQWVKECVRdk 104
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQAtqlnlQQNIKVQQLDVTDQNSIHNFQLVLKEIGR-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 gLWGLVNNAGISL----PTAPNELLTKQdfvtiLDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSLFG-GGYCI 178
Cdd:PRK06914  82 -IDLLVNNAGYANggfvEEIPVEEYRKQ-----FETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGlSPYVS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 179 SKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKErflKSFLEIW-DRSSPevKEAYGEKFVADYKKSAEQmeqkc 257
Cdd:PRK06914 156 SKYALEGFSESLRLELKPFGIDVALIEPGSYNTNIWEVG---KQLAENQsETTSP--YKEYMKKIQKHINSGSDT----- 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 150247226 258 TQDLSLVTNCMEHALIACHPRTRYSAGWDAKLLYLPMSYMP 298
Cdd:PRK06914 226 FGNPIDVANLIVEIAESKRPKLRYPIGKGVKLMILAKKILP 266
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 25-232 4.26e-38

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


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 135.30  E-value: 4.26e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  25 SHLRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLR---GQTSDRLETVTLDVTKTESVAAAAQWVKEcv 101
Cdd:COG1028    2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAaelRAAGGRALAVAADVTDEAAVEALVAAAVA-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 102 RDKGLWGLVNNAGIsLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFG-GGYCIS 179
Cdd:COG1028   80 AFGRLDILVNNAGI-TPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPhMRERGGGRIVNISSIAGLRGSPGqAAYAAS 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 150247226 180 KYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKERFLKSFLEIWDRSSP 232
Cdd:COG1028  159 KAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAARIP 211
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 27-211 1.09e-36

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 131.94  E-value: 1.09e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLaacLT-------EKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKE 99
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLV---LSarreerlEEVKSECLELGAPSPHVVPLDMSDLEDAEQVVEEALK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 100 CVRdkGLWGLVNNAGISLPtAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSL-FGGGYC 177
Cdd:cd05332   78 LFG--GLDILINNAGISMR-SLFHDTSIDVDRKIMEVNYFGPVALTKAALPhLIERSQGSIVVVSSIAGKIGVpFRTAYA 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 150247226 178 ISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:cd05332  155 ASKHALQGFFDSLRAELSEPNISVTVVCPGLIDT 188
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 33-211 2.56e-35

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 128.88  E-value: 2.56e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  33 FITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAaqwVKECVRDKG-LWGLVN 111
Cdd:PRK06180   8 LITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAV---VADAEATFGpIDVLVN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 112 NAGI----SLPTAPNELLTKQdfvtiLDVNLLGVIDVTLSLLPLVR-RARGRVVNVSSVMGRVSLFG-GGYCISKYGVEA 185
Cdd:PRK06180  85 NAGYghegAIEESPLAEMRRQ-----FEVNVFGAVAMTKAVLPGMRaRRRGHIVNITSMGGLITMPGiGYYCGSKFALEG 159

                        170       180
                 ....*....|....*....|....*.
gi 150247226 186 FSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK06180 160 ISESLAKEVAPFGIHVTAVEPGSFRT 185
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 30-216 1.05e-32

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


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 120.81  E-value: 1.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARG-LRV-LAACLTEKG---AEQLRGQTSDrLETVTLDVTKTESVAAAAQWVKEcvRDK 104
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGpGTViLTARDVERGqaaVEKLRAEGLS-VRFHQLDVTDDASIEAAADFVEE--KYG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 GLWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSLfggGYCISKYGV 183
Cdd:cd05324   78 GLDILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPaGRIVNVSSGLGSLTS---AYGVSKAAL 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 150247226 184 EAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSK 216
Cdd:cd05324  155 NALTRILAKELKETGIKVNACCPGWVKTDMGGG 187
PRK05693 PRK05693
SDR family oxidoreductase;
32-222 4.70e-32

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 120.28  E-value: 4.70e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRVLAaclTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKEcvRDKGLWGLVN 111
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWA---TARKAEDVEALAAAGFTAVQLDVNDGAALARLAEELEA--EHGGLDVLIN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 112 NAGIS----LPTAPNELLTKQdFVTildvNLLGVIDVTLSLLPLVRRARGRVVNVSSVMG-RVSLFGGGYCISKYGVEAF 186
Cdd:PRK05693  79 NAGYGamgpLLDGGVEAMRRQ-FET----NVFAVVGVTRALFPLLRRSRGLVVNIGSVSGvLVTPFAGAYCASKAAVHAL 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 150247226 187 SDSLRRELSYFGVKVAMIEPG-----YFKTAVTSKERFLKS 222
Cdd:PRK05693 154 SDALRLELAPFGVQVMEVQPGaiasqFASNASREAEQLLAE 194
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
30-211 1.00e-31

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 118.71  E-value: 1.00e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGA----EQLRGQTSDRLETVTLDVTKTESVAAAaqwVKECVRDKG 105
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCakdwFEEYGFTEDQVRLKELDVTDTEECAEA---LAEIEEEEG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LWG-LVNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLPLVR-RARGRVVNVSSVMGRVSLFGG-GYCISKYG 182
Cdd:PRK12824  80 PVDiLVNNAGITRDSVFKRM-SHQEWNDVINTNLNSVFNVTQPLFAAMCeQGYGRIINISSVNGLKGQFGQtNYSAAKAG 158

                        170       180
                 ....*....|....*....|....*....
gi 150247226 183 VEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK12824 159 MIGFTKALASEGARYGITVNCIAPGYIAT 187
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
27-214 1.79e-31

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 117.95  E-value: 1.79e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTS---DRLETVTLDVTKTESVAAAAQWVKEcvRD 103
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRaagGEARVLVFDVSDEAAVRALIEAAVE--AF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 KGLWGLVNNAGISlPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSLFGGG-YCISKY 181
Cdd:PRK05653  81 GALDILVNNAGIT-RDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARyGRIVNISSVSGVTGNPGQTnYSAAKA 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 150247226 182 GVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVT 214
Cdd:PRK05653 160 GVIGFTKALALELASRGITVNAVAPGFIDTDMT 192
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 30-211 2.13e-31

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: 117.77  E-value: 2.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLaacLT-------EKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVR 102
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLI---LTgrraerlQELADELGAKFPVKVLPLQLDVSDRESIEAALENLPEEFR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 DkgLWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFGGG-YCISK 180
Cdd:cd05346   78 D--IDILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPiMIARNQGHIINLGSIAGRYPYAGGNvYCATK 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 150247226 181 YGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:cd05346  156 AAVRQFSLNLRKDLIGTGIRVTNIEPGLVET 186
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 30-281 2.44e-31

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: 117.95  E-value: 2.44e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQL---DARGLRVLAACLTEKGAEQL----RGQTSDRLETVTLDVTKTESVAAAAqwvkECVR 102
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLasdPSKRFKVYATMRDLKKKGRLweaaGALAGGTLETLQLDVCDSKSVAAAV----ERVT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 DKGLWGLVNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSL-FGGGYCISK 180
Cdd:cd09806   77 ERHVDVLVCNAGVGL-LGPLEALSEDAMASVFDVNVFGTVRMLQAFLPdMKRRGSGRILVTSSVGGLQGLpFNDVYCASK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 181 YGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSkerflKSFLEIWDRSSPEVKEAYGEKFVADYKKSAEQMEQKCTQD 260
Cdd:cd09806  156 FALEGLCESLAVQLLPFNVHLSLIECGPVHTAFME-----KVLGSPEEVLDRTADDITTFHFFYQYLAHSKQVFREAAQN 230

                        250       260
                 ....*....|....*....|.
gi 150247226 261 LSLVTNCMEHALIACHPRTRY 281
Cdd:cd09806  231 PEEVAEVFLTAIRAPKPPLRY 251
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 32-211 4.01e-31

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: 116.63  E-value: 4.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARG-LRVLAACLTEKGAEQLRGQTS--DRLETVTLDVTKTESVAAAAqwVKECVRDKGLWG 108
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSAATELAALGAshSRLHILELDVTDEIAESAEA--VAERLGDAGLDV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 109 LVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRA-RGRVVNVSSVMGRVSLFGGG----YCISKYGV 183
Cdd:cd05325   79 LINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGaRAKIINISSRVGSIGDNTSGgwysYRASKAAL 158

                        170       180
                 ....*....|....*....|....*...
gi 150247226 184 EAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:cd05325  159 NMLTKSLAVELKRDGITVVSLHPGWVRT 186
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 27-238 8.71e-31

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 116.06  E-value: 8.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLT-EKGAEQL---RGQTSDRLETVTLDVTKTESVAAAAQWVKECVr 102
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASsEAGAEALvaeIGALGGKALAVQGDVSDAESVERAVDEAKAEF- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 dKGLWGLVNNAGIslpTAPNELL--TKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSLFGGG-YCI 178
Cdd:PRK05557  82 -GGVDILVNNAGI---TRDNLLMrmKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRsGRIINISSVVGLMGNPGQAnYAA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 179 SKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKerflksfleiwdrSSPEVKEAY 238
Cdd:PRK05557 158 SKAGVIGFTKSLARELASRGITVNAVAPGFIETDMTDA-------------LPEDVKEAI 204
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 30-216 4.18e-30

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


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 114.18  E-value: 4.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGA---EQLRGQTSDRLETVTLDVTKTESVAAAaqwVKECVRDKG- 105
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAaetVEEIKALGGNAAALEADVSDREAVEAL---VEKVEAEFGp 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LWGLVNNAGIslpTAPNELL--TKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSLFG-GGYCISKY 181
Cdd:cd05333   78 VDILVNNAGI---TRDNLLMrmSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRsGRIINISSVVGLIGNPGqANYAASKA 154

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 150247226 182 GVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSK 216
Cdd:cd05333  155 GVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDA 189
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 27-214 5.19e-30

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


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 114.17  E-value: 5.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQ---TSDRLETVTLDVTKTESVAAAAQWVKECVrd 103
Cdd:cd08934    1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADEleaEGGKALVLELDVTDEQQVDAAVERTVEAL-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 KGLWGLVNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVR-RARGRVVNVSSVMGRVSLFG-GGYCISKY 181
Cdd:cd08934   79 GRLDILVNNAGIML-LGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLlRNKGTIVNISSVAGRVAVRNsAVYNATKF 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 150247226 182 GVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVT 214
Cdd:cd08934  158 GVNAFSEGLRQEVTERGVRVVVIEPGTVDTELR 190
PRK09291 PRK09291
SDR family oxidoreductase;
30-211 6.16e-30

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 114.32  E-value: 6.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDR---LETVTLDVTKTESVAAAAQWvkecvrDKGL 106
Cdd:PRK09291   3 KTILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRglaLRVEKLDLTDAIDRAQAAEW------DVDV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 107 wgLVNNAGISLPTA----PNELLTKQdfvtiLDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSL-FGGGYCISK 180
Cdd:PRK09291  77 --LLNNAGIGEAGAvvdiPVELVREL-----FETNVFGPLELTQGFVRkMVARGKGKVVFTSSMAGLITGpFTGAYCASK 149

                        170       180       190
                 ....*....|....*....|....*....|.
gi 150247226 181 YGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK09291 150 HALEAIAEAMHAELKPFGIQVATVNPGPYLT 180
PRK12826 PRK12826
SDR family oxidoreductase;
27-211 1.22e-29

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 113.09  E-value: 1.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAE---QLRGQTSDRLETVTLDVTkteSVAAAAQWVKECVRD 103
Cdd:PRK12826   4 LEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAataELVEAAGGKARARQVDVR---DRAALKAAVAAGVED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 KG-LWGLVNNAGISlPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSLFGG--GYCIS 179
Cdd:PRK12826  81 FGrLDILVANAGIF-PLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGgGRIVLTSSVAGPRVGYPGlaHYAAS 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 150247226 180 KYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK12826 160 KAGLVGFTRALALELAARNITVNSVHPGGVDT 191
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 33-253 1.23e-29

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 113.98  E-value: 1.23e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  33 FITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAaqwVKECVRDKG-LWGLVN 111
Cdd:PRK08263   7 FITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAA---VETAVEHFGrLDIVVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 112 NAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSLFGGG-YCISKYGVEAFSDS 189
Cdd:PRK08263  84 NAGYGLFGMIEEV-TESEARAQIDTNFFGALWVTQAVLPYLREQRsGHIIQISSIGGISAFPMSGiYHASKWALEGMSEA 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150247226 190 LRRELSYFGVKVAMIEPGYFKT--AVTSKERFLKsfLEIWDRSSPEVKEAYGEK-FVADYKKSAEQM 253
Cdd:PRK08263 163 LAQEVAEFGIKVTLVEPGGYSTdwAGTSAKRATP--LDAYDTLREELAEQWSERsVDGDPEAAAEAL 227
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 27-215 2.68e-29

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 112.73  E-value: 2.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRV----LAACLTEKGAEQLrgqtsDRLETVTLDVTKTESVAAaaqWVKECVR 102
Cdd:PRK07825   3 LRGKVVAITGGARGIGLATARALAALGARVaigdLDEALAKETAAEL-----GLVVGGPLDVTDPASFAA---FLDAVEA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 DKGLWG-LVNNAGIsLPTAPneLLTKQDFVT--ILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFGGG-YC 177
Cdd:PRK07825  75 DLGPIDvLVNNAGV-MPVGP--FLDEPDAVTrrILDVNVYGVILGSKLAAPrMVPRGRGHVVNVASLAGKIPVPGMAtYC 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 150247226 178 ISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTS 215
Cdd:PRK07825 152 ASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELIA 189
PRK08264 PRK08264
SDR family oxidoreductase;
26-215 3.08e-29

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 111.90  E-value: 3.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  26 HLRDKYVFITGCDSGFGKLLARQLDARGLR-VLAACLTEKGAEQLrgqtSDRLETVTLDVTKTESVAAAAqwvkECVRDK 104
Cdd:PRK08264   3 DIKGKVVLVTGANRGIGRAFVEQLLARGAAkVYAAARDPESVTDL----GPRVVPLQLDVTDPASVAAAA----EAASDV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 GLwgLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSL-FGGGYCISKYG 182
Cdd:PRK08264  75 TI--LVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPvLAANGGGAIVNVLSVLSWVNFpNLGTYSASKAA 152

                        170       180       190
                 ....*....|....*....|....*....|...
gi 150247226 183 VEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTS 215
Cdd:PRK08264 153 AWSLTQALRAELAPQGTRVLGVHPGPIDTDMAA 185
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 29-211 8.97e-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: 110.81  E-value: 8.97e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  29 DKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQL-------RGQTSDRLETVTLDVTKTESVAAAaqwVKECV 101
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAveeieaeANASGQKVSYISADLSDYEEVEQA---FAQAV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 102 RDKGLWG-LVNNAGISLPtAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVR-RARGRVVNVSSVMGRVSLFG-GGYCI 178
Cdd:cd08939   78 EKGGPPDlVVNCAGISIP-GLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKeQRPGHIVFVSSQAALVGIYGySAYCP 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 150247226 179 SKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:cd08939  157 SKFALRGLAESLRQELKPYNIRVSVVYPPDTDT 189
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 27-222 2.34e-28

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 109.42  E-value: 2.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGL-RVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKEcvrdkg 105
Cdd:cd05354    1 IKDKTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAAQAKD------ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LWGLVNNAGISlptAPNELLTKQDFVT---ILDVNLLGVIDVTLSLLPLVRRA-RGRVVNVSSVMGRVSLFG-GGYCISK 180
Cdd:cd05354   75 VDVVINNAGVL---KPATLLEEGALEAlkqEMDVNVFGLLRLAQAFAPVLKANgGGAIVNLNSVASLKNFPAmGTYSASK 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 150247226 181 YGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKERFLKS 222
Cdd:cd05354  152 SAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGAGGPKE 193
PRK06482 PRK06482
SDR family oxidoreductase;
33-215 4.75e-28

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 109.82  E-value: 4.75e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  33 FITGCDSGFGKLLARQLDARGLRVlAACLTEKGA-EQLRGQTSDRLETVTLDVTKTESVAAAAQwvkecvRDKGLWG--- 108
Cdd:PRK06482   6 FITGASSGFGRGMTERLLARGDRV-AATVRRPDAlDDLKARYGDRLWVLQLDVTDSAAVRAVVD------RAFAALGrid 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 109 -LVNNAGISLPTAPNELLTKQDFVTIlDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSLFGGG-YCISKYGVEA 185
Cdd:PRK06482  79 vVVSNAGYGLFGAAEELSDAQIRRQI-DTNLIGSIQVIRAALPHLRRQGgGRIVQVSSEGGQIAYPGFSlYHATKWGIEG 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 150247226 186 FSDSLRRELSYFGVKVAMIEPGYFKTAVTS 215
Cdd:PRK06482 158 FVEAVAQEVAPFGIEFTIVEPGPARTNFGA 187
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 27-218 1.22e-27

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: 107.39  E-value: 1.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDrLETVTLDVTKTESVAAAAQWVKEcvRDKGL 106
Cdd:cd05370    3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN-IHTIVLDVGDAESVEALAEALLS--EYPNL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 107 WGLVNNAGISLP---TAPNELLtkQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFGGG-YCISKY 181
Cdd:cd05370   80 DILINNAGIQRPidlRDPASDL--DKADTEIDTNLIGPIRLIKAFLPhLKKQPEATIVNVSSGLAFVPMAANPvYCATKA 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 150247226 182 GVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKER 218
Cdd:cd05370  158 ALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERR 194
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 30-218 6.46e-27

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: 105.14  E-value: 6.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQtSDRLETVTLDVTKTEsvaaAAQWVKECVRDK--GLW 107
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS-GGDVEAVPYDARDPE----DARALVDALRDRfgRID 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 108 GLVNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMG-RVSLFGGGYCISKYGVEA 185
Cdd:cd08932   76 VLVHNAGIGRPTTLREG-SDAELEAHFSINVIAPAELTRALLPaLREAGSGRVVFLNSLSGkRVLAGNAGYSASKFALRA 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 150247226 186 FSDSLRRELSYFGVKVAMIEPGYFKTAVTSKER 218
Cdd:cd08932  155 LAHALRQEGWDHGVRVSAVCPGFVDTPMAQGLT 187
PRK05650 PRK05650
SDR family oxidoreductase;
32-218 8.92e-27

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 106.28  E-value: 8.92e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAE---QLRGQTSDRLETVTLDVTKTESVAAAAQWVKEcvrdkgLWG 108
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLALADVNEEGGEetlKLLREAGGDGFYQRCDVRDYSQLTALAQACEE------KWG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 109 ----LVNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSL-FGGGYCISKYG 182
Cdd:PRK05650  77 gidvIVNNAGVASGGFFEEL-SLEDWDWQIAINLMGVVKGCKAFLPLFKRQKsGRIVNIASMAGLMQGpAMSSYNVAKAG 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 150247226 183 VEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKER 218
Cdd:PRK05650 156 VVALSETLLVELADDEIGVHVVCPSFFQTNLLDSFR 191
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 32-225 1.46e-26

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: 105.02  E-value: 1.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAE---QLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVRDKGLwg 108
Cdd:cd05339    2 VLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEetaNNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTI-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 109 LVNNAGI----SLPTAPNELLTKqdfvtILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFGGG-YCISKYG 182
Cdd:cd05339   80 LINNAGVvsgkKLLELPDEEIEK-----TFEVNTLAHFWTTKAFLPdMLERNHGHIVTIASVAGLISPAGLAdYCASKAA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 150247226 183 VEAFSDSLRRELSYF---GVKVAMIEPGYFKTA----VTSKERFLKSFLE 225
Cdd:cd05339  155 AVGFHESLRLELKAYgkpGIKTTLVCPYFINTGmfqgVKTPRPLLAPILE 204
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 30-211 2.22e-26

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


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 104.13  E-value: 2.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVrdKGLWGL 109
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAF--GGLDAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 110 VNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTL-SLLPLVRRARGRVVNVSSVMGRVSLFGG-GYCISKYGVEAFS 187
Cdd:cd08929   79 VNNAGVGV-MKPVEELTPEEWRLVLDTNLTGAFYCIHkAAPALLRRGGGTIVNVGSLAGKNAFKGGaAYNASKFGLLGLS 157

                        170       180
                 ....*....|....*....|....
gi 150247226 188 DSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:cd08929  158 EAAMLDLREANIRVVNVMPGSVDT 181
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 29-211 7.93e-26

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: 103.46  E-value: 7.93e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  29 DKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQ-----TSDRLETVTLDVTKTESVAAAAQWVKECVRD 103
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEikketGNAKVEVIQLDLSSLASVRQFAEEFLARFPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 kgLWGLVNNAGISLPTApneLLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSLFGGG------- 175
Cdd:cd05327   81 --LDILINNAGIMAPPR---RLTKDGFELQFAVNYLGHFLLTNLLLPVLKASApSRIVNVSSIAHRAGPIDFNdldlenn 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 150247226 176 --------YCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:cd05327  156 keyspykaYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRT 199
PRK07024 PRK07024
SDR family oxidoreductase;
32-224 8.31e-26

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 103.09  E-value: 8.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRVLaacLTEKGAEQLRG-----QTSDRLETVTLDVTKTESVAAAAQwvkECVRDKGL 106
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLG---LVARRTDALQAfaarlPKAARVSVYAADVRDADALAAAAA---DFIAAHGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 107 WGLV-NNAGISLPTAPNELLTKQDFVTILDVNLLGVIdVTLS--LLPLVRRARGRVVNVSSVMGRVSLFGGG-YCISKYG 182
Cdd:PRK07024  79 PDVViANAGISVGTLTEEREDLAVFREVMDTNYFGMV-ATFQpfIAPMRAARRGTLVGIASVAGVRGLPGAGaYSASKAA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 150247226 183 VEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKERFLKSFL 224
Cdd:PRK07024 158 AIKYLESLRVELRPAGVRVVTIAPGYIRTPMTAHNPYPMPFL 199
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 27-201 8.56e-26

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 103.90  E-value: 8.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQ--TSDRLETVTLDVTKTESVAAAAQWVKEcvRDK 104
Cdd:PRK05872   7 LAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAElgGDDRVLTVVADVTDLAAMQAAAEEAVE--RFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 GLWGLVNNAGISlPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVmgrvSLFGGG-----YCIS 179
Cdd:PRK05872  85 GIDVVVANAGIA-SGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSL----AAFAAApgmaaYCAS 159

                        170       180
                 ....*....|....*....|..
gi 150247226 180 KYGVEAFSDSLRRELSYFGVKV 201
Cdd:PRK05872 160 KAGVEAFANALRLEVAHHGVTV 181
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 32-205 8.74e-26

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: 102.93  E-value: 8.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTsDRLETVTLDVTKTESVAAAAQWVKEcvRDKGLWGLVN 111
Cdd:COG3967    8 ILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAAN-PGLHTIVLDVADPASIAALAEQVTA--EFPDLNVLIN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 112 NAGISLP---TAPNELLtkQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFG-GGYCISKYGVEAF 186
Cdd:COG3967   85 NAGIMRAedlLDEAEDL--ADAEREITTNLLGPIRLTAAFLPhLKAQPEAAIVNVSSGLAFVPLAVtPTYSATKAALHSY 162

                        170
                 ....*....|....*....
gi 150247226 187 SDSLRRELSYFGVKVamIE 205
Cdd:COG3967  163 TQSLRHQLKDTSVKV--IE 179
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-217 3.04e-25

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 101.48  E-value: 3.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACL-TEKGAEQLRG---QTSDRLETVTLDVTKTESVAAAaqwVKECVR 102
Cdd:PRK12825   4 LMGRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEaveALGRRAQAVQADVTDKAALEAA---VAAAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 DKG-LWGLVNNAGIsLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSLFG-GGYCIS 179
Cdd:PRK12825  81 RFGrIDILVNNAGI-FEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRgGRIVNISSVAGLPGWPGrSNYAAA 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 150247226 180 KYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKE 217
Cdd:PRK12825 160 KAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEAT 197
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 32-216 4.03e-25

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: 100.75  E-value: 4.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226   32 VFITGCDSGFGKLLARQLDARGLRVLAACLT-EKGAEQLRGQTSD---RLETVTLDVTKTESVAAAaqwVKECVRDKG-L 106
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSsEEGAEEVVEELKAlgvKALGVVLDVSDREDVKAV---VEEIEEELGtI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  107 WGLVNNAGIslpTAPNELL--TKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGrvsLFGGG----YCIS 179
Cdd:TIGR01830  78 DILVNNAGI---TRDNLLMrmKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRsGRIINISSVVG---LMGNAgqanYAAS 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 150247226  180 KYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSK 216
Cdd:TIGR01830 152 KAGVIGFTKSLAKELASRNITVNAVAPGFIDTDMTDK 188
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 38-232 6.00e-25

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


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 100.20  E-value: 6.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226   38 DSGFGKLLARQLDARGLRVLAACLTEKGAEQLRgQTSDRL--ETVTLDVTKTESVAAAAQWVKEcvRDKGLWGLVNNAGI 115
Cdd:pfam13561   5 ESGIGWAIARALAEEGAEVVLTDLNEALAKRVE-ELAEELgaAVLPCDVTDEEQVEALVAAAVE--KFGRLDILVNNAGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  116 SLPTAPNEL-LTKQDFVTILDVNLLGVIDVTLSLLPLvRRARGRVVNVSSVMGRVSLFGGG-YCISKYGVEAFSDSLRRE 193
Cdd:pfam13561  82 APKLKGPFLdTSREDFDRALDVNLYSLFLLAKAALPL-MKEGGSIVNLSSIGAERVVPNYNaYGAAKAALEALTRYLAVE 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 150247226  194 LSYFGVKVAMIEPGYFKTAVTSKERFLKSFLEIWDRSSP 232
Cdd:pfam13561 161 LGPRGIRVNAISPGPIKTLAASGIPGFDELLAAAEARAP 199
PRK09072 PRK09072
SDR family oxidoreductase;
26-206 1.08e-24

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 100.40  E-value: 1.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  26 HLRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTS--DRLETVTLDVTKTESVAAAAQwvkECVRD 103
Cdd:PRK09072   2 DLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPypGRHRWVVADLTSEAGREAVLA---RAREM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 KGLWGLVNNAGIslptapNE--LLTKQDFVTI---LDVNLLGVIDVTLSLLPLVRRA-RGRVVNVSSVMGRVSLFG-GGY 176
Cdd:PRK09072  79 GGINVLINNAGV------NHfaLLEDQDPEAIerlLALNLTAPMQLTRALLPLLRAQpSAMVVNVGSTFGSIGYPGyASY 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 150247226 177 CISKYGVEAFSDSLRRELSYFGVKVAMIEP 206
Cdd:PRK09072 153 CASKFALRGFSEALRRELADTGVRVLYLAP 182
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 27-218 3.47e-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: 98.58  E-value: 3.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTE---KGAEQLRGQTSDRLETVTLDVTKTESVAAAaqwVKECVRD 103
Cdd:cd05347    3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEekaEEAQQLIEKEGVEATAFTCDVSDEEAIKAA---VEAIEED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 KG-LWGLVNNAGISLPtAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMgrvSLFGG----GYC 177
Cdd:cd05347   80 FGkIDILVNNAGIIRR-HPAEEFPEAEWRDVIDVNLNGVFFVSQAVARhMIKQGHGKIINICSLL---SELGGppvpAYA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 150247226 178 ISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKER 218
Cdd:cd05347  156 ASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTEAVV 196
PRK07832 PRK07832
SDR family oxidoreductase;
30-237 6.90e-24

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 98.19  E-value: 6.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLaacLTEKGAEQLRGQTSDR-------LETVTLDVTKTESVAAAAQWVKEcvR 102
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELF---LTDRDADGLAQTVADAralggtvPEHRALDISDYDAVAAFAADIHA--A 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 DKGLWGLVNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGR-VVNVSSVMGRVSL-FGGGYCIS 179
Cdd:PRK07832  76 HGSMDVVMNIAGISAWGTVDRL-THEQWRRMVDVNLMGPIHVIETFVPpMVAAGRGGhLVNVSSAAGLVALpWHAAYSAS 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 180 KYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKerflksfLEI--WDRSSPEVKEA 237
Cdd:PRK07832 155 KFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVNT-------VEIagVDREDPRVQKW 207
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 32-219 1.35e-23

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 97.13  E-value: 1.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVRDKGLwgLVN 111
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDV--LVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 112 NAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFGGG-YCISKYGVEAFSDS 189
Cdd:PRK10538  81 NAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPgMVERNHGHIINIGSTAGSWPYAGGNvYGATKAFVRQFSLN 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 150247226 190 LRRELSYFGVKVAMIEPGYFKTAVTSKERF 219
Cdd:PRK10538 161 LRTDLHGTAVRVTDIEPGLVGGTEFSNVRF 190
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 27-214 2.81e-23

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: 96.30  E-value: 2.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKEcvRDKGL 106
Cdd:cd05341    3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTARE--AFGRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 107 WGLVNNAGISLPtAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRA-RGRVVNVSSVMGRVSLFG-GGYCISKYGVE 184
Cdd:cd05341   81 DVLVNNAGILTG-GTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAgGGSIINMSSIEGLVGDPAlAAYNASKGAVR 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 150247226 185 AFSDSLRREL--SYFGVKVAMIEPGYFKTAVT 214
Cdd:cd05341  160 GLTKSAALECatQGYGIRVNSVHPGYIYTPMT 191
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 20-207 3.54e-23

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 96.28  E-value: 3.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  20 ERQVLSHLRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTL-DVTKTESVAAAAQWVK 98
Cdd:PRK12829   2 AIDLLKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPGAKVTATVaDVADPAQVERVFDTAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  99 EcvRDKGLWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVR-RARGRVV-NVSSVMGRVSL-FGGG 175
Cdd:PRK12829  82 E--RFGGLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKaSGHGGVIiALSSVAGRLGYpGRTP 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 150247226 176 YCISKYGVEAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:PRK12829 160 YAASKWAVVGLVKSLAIELGPLGIRVNAILPG 191
PRK07326 PRK07326
SDR family oxidoreductase;
27-207 3.92e-23

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 95.46  E-value: 3.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTL--DVTKTESVAAAaqwVKECVRDk 104
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGNVLGLaaDVRDEADVQRA---VDAIVAA- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 glWG----LVNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRvSLFGGG--YCI 178
Cdd:PRK07326  80 --FGgldvLIANAGVGH-FAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGT-NFFAGGaaYNA 155

                        170       180
                 ....*....|....*....|....*....
gi 150247226 179 SKYGVEAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:PRK07326 156 SKFGLVGFSEAAMLDLRQYGIKVSTIMPG 184
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 32-211 5.76e-23

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: 94.76  E-value: 5.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRVLAACLTEKG----AEQLRGQTSDRLeTVTLDVTKTESVAAAAQWVKECVRDKGLW 107
Cdd:cd05360    3 VVITGASSGIGRATALAFAERGAKVVLAARSAEAlhelAREVRELGGEAI-AVVADVADAAQVERAADTAVERFGRIDTW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 108 glVNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMG-RVSLFGGGYCISKYGVEA 185
Cdd:cd05360   82 --VNNAGVAVFGRFEDV-TPEEFRRVFDVNYLGHVYGTLAALPhLRRRGGGALINVGSLLGyRSAPLQAAYSASKHAVRG 158

                        170       180
                 ....*....|....*....|....*...
gi 150247226 186 FSDSLRRELSYFG--VKVAMIEPGYFKT 211
Cdd:cd05360  159 FTESLRAELAHDGapISVTLVQPTAMNT 186
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 27-206 1.15e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 96.14  E-value: 1.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKG----AEQLRGQTSDRLeTVTLDVTKTESVAAAAQwvkECVR 102
Cdd:PRK07109   6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGlealAAEIRAAGGEAL-AVVADVADAEAVQAAAD---RAEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 DKG---LWglVNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSL-FGGGYC 177
Cdd:PRK07109  82 ELGpidTW--VNNAMVTV-FGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRhMRPRDRGAIIQVGSALAYRSIpLQSAYC 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 150247226 178 ISKYGVEAFSDSLRRELSYFG--VKVAMIEP 206
Cdd:PRK07109 159 AAKHAIRGFTDSLRCELLHDGspVSVTMVQP 189
FabG-like PRK07231
SDR family oxidoreductase;
27-246 1.48e-22

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 94.13  E-value: 1.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKG----AEQLRGQtsDRLETVTLDVTKTESVAAAAQWVKECvr 102
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAaervAAEILAG--GRAIAVAADVSDEADVEAAVAAALER-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 dkglWG----LVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMG-RVSLFGGGY 176
Cdd:PRK07231  79 ----FGsvdiLVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGgGAIVNVASTAGlRPRPGLGWY 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 177 CISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTavtskeRFLKSFLEIWDrssPEVKeaygEKFVADY 246
Cdd:PRK07231 155 NASKGAVITLTKALAAELGPDKIRVNAVAPVVVET------GLLEAFMGEPT---PENR----AKFLATI 211
PRK06484 PRK06484
short chain dehydrogenase; Validated
 28-211 2.81e-22

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 96.84  E-value: 2.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  28 RDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKecvrdkGLW 107
Cdd:PRK06484 268 SPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQ------ARW 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 108 G----LVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRArGRVVNVSSVMGRVSLFG-GGYCISKYG 182
Cdd:PRK06484 342 GrldvLVNNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG-GVIVNLGSIASLLALPPrNAYCASKAA 420

                        170       180
                 ....*....|....*....|....*....
gi 150247226 183 VEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK06484 421 VTMLSRSLACEWAPAGIRVNTVAPGYIET 449
PRK06181 PRK06181
SDR family oxidoreductase;
29-211 2.83e-22

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 93.89  E-value: 2.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  29 DKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKG----AEQLRGQTSDRLeTVTLDVTKTESVAAAaqwVKECVRDK 104
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRlaslAQELADHGGEAL-VVPTDVSDAEACERL---IEAAVARF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 G-LWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRVSLFG-GGYCISKYG 182
Cdd:PRK06181  77 GgIDILVNNAGITMWSRFDELTDLSVFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTrSGYAASKHA 156

                        170       180
                 ....*....|....*....|....*....
gi 150247226 183 VEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK06181 157 LHGFFDSLRIELADDGVAVTVVCPGFVAT 185
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 30-260 1.32e-21

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: 91.59  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEK--GAEQLRGQ-TSDRLETVTLDVTKTESVAAAAQWVKEcvrdkgL 106
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENpgAAAELQAInPKVKATFVQCDVTSWEQLAAAFKKAIE------K 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 107 WG----LVNNAGISLPTAPNEL-LTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR----GRVVNVSSVMG-----RVSLf 172
Cdd:cd05323   75 FGrvdiLINNAGILDEKSYLFAgKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKggkgGVIVNIGSVAGlypapQFPV- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 173 gggYCISKYGVEAFSDSLRRELSY-FGVKVAMIEPGYFKTAVTSKER-FLKSFLEIWDRSSPE-VKEAYgEKFVADYKKS 249
Cdd:cd05323  154 ---YSASKHGVVGFTRSLADLLEYkTGVRVNAICPGFTNTPLLPDLVaKEAEMLPSAPTQSPEvVAKAI-VYLIEDDEKN 229

                        250
                 ....*....|.
gi 150247226 250 AEQMeqKCTQD 260
Cdd:cd05323  230 GAIW--IVDGG 238
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 32-216 4.41e-21

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: 90.08  E-value: 4.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRVLAAC-----LTEKGAEQLRGQTSDRLETvtLDVTKTESVAAaaqWVKECVRDKGL 106
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAArrtdrLDELKAELLNPNPSVEVEI--LDVTDEERNQL---VIAELEAELGG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 107 WGL-VNNAGISLPTaPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFGG-GYCISKYGV 183
Cdd:cd05350   76 LDLvIINAGVGKGT-SLGDLSFKAFRETIDTNLLGAAAILEAALPqFRAKGRGHLVLISSVAALRGLPGAaAYSASKAAL 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 150247226 184 EAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSK 216
Cdd:cd05350  155 SSLAESLRYDVKKRGIRVTVINPGFIDTPLTAN 187
PRK08219 PRK08219
SDR family oxidoreductase;
34-207 4.87e-21

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 89.61  E-value: 4.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  34 ITGCDSGFGKLLARQLdARGLRVLAACLTEKGAEQLRgQTSDRLETVTLDVTKTESVAAAaqwvkeCVRDKGLWGLVNNA 113
Cdd:PRK08219   8 ITGASRGIGAAIAREL-APTHTLLLGGRPAERLDELA-AELPGATPFPVDLTDPEAIAAA------VEQLGRLDVLVHNA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 114 GISLPtAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMG-RVSLFGGGYCISKYGVEAFSDSLRR 192
Cdd:PRK08219  80 GVADL-GPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGlRANPGWGSYAASKFALRALADALRE 158

                        170
                 ....*....|....*
gi 150247226 193 ELSYfGVKVAMIEPG 207
Cdd:PRK08219 159 EEPG-NVRVTSVHPG 172
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 30-207 6.62e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 89.77  E-value: 6.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDrlETVTLDVTKTESVAAAAQwvkecvRDKGLWGL 109
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGC--EPLRLDVGDDAAIRAALA------AAGAFDGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 110 VNNAGISLPTAPNElLTKQDFVTILDVNLLGVIDVTLSLLPLVRRA--RGRVVNVSSVMGRVSL-FGGGYCISKYGVEAF 186
Cdd:PRK07060  82 VNCAGIASLESALD-MTAEGFDRVMAVNARGAALVARHVARAMIAAgrGGSIVNVSSQAALVGLpDHLAYCASKAALDAI 160

                        170       180
                 ....*....|....*....|.
gi 150247226 187 SDSLRRELSYFGVKVAMIEPG 207
Cdd:PRK07060 161 TRVLCVELGPHGIRVNSVNPT 181
PRK08267 PRK08267
SDR family oxidoreductase;
30-310 1.58e-20

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 88.84  E-value: 1.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQ-TSDRLETVTLDVTKTESVAAAaqwVKECVR--DKGL 106
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAElGAGNAWTGALDVTDRAAWDAA---LADFAAatGGRL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 107 WGLVNNAGIsLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARG-RVVNVSSVMGrvsLFGGG----YCISKY 181
Cdd:PRK08267  79 DVLFNNAGI-LRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGaRVINTSSASA---IYGQPglavYSATKF 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 182 GVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVtskerfLKSFLEIWDRSSPevkEAYGekfvadYKKSAEQMEQKctqdl 261
Cdd:PRK08267 155 AVRGLTEALDLEWRRHGIRVADVMPLFVDTAM------LDGTSNEVDAGST---KRLG------VRLTPEDVAEA----- 214

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 150247226 262 slVTNCMEHAliachPRTRYSAGWDAKLLYLPMSYMPTFLVDAIMYWVS 310
Cdd:PRK08267 215 --VWAAVQHP-----TRLHWPVGKQAKLLAFLARLSPGFVRRLINKSLA 256
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 29-214 6.70e-20

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: 86.50  E-value: 6.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  29 DKYVFITGCDSGFGKLLARQLDARGLRVlaaCLTEKGAEQLRgQTSDRLE--------TVTLDVTKTESvaaAAQWVKEC 100
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNV---ILISRTQEKLD-AVAKEIEekygvetkTIAADFSAGDD---IYERIEKE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 101 VRDKGLWGLVNNAGISlPTAPNELLTKQDFV--TILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRV-SLFGGGY 176
Cdd:cd05356   74 LEGLDIGILVNNVGIS-HSIPEYFLETPEDElqDIINVNVMATLKMTRLILPgMVKRKKGAIVNISSFAGLIpTPLLATY 152

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 150247226 177 CISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVT 214
Cdd:cd05356  153 SASKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMS 190
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 27-216 6.70e-20

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 86.89  E-value: 6.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRV-LAACLTEKgAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVrdKG 105
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVgLHGTRVEK-LEALAAELGERVKIFPANLSDRDEVKALGQKAEADL--EG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LWGLVNNAGISlptaPNEL---LTKQDFVTILDVNLLGVIDVTLSLL-PLVRRARGRVVNVSSVMGRVSLFG-GGYCISK 180
Cdd:PRK12936  81 VDILVNNAGIT----KDGLfvrMSDEDWDSVLEVNLTATFRLTRELThPMMRRRYGRIINITSVVGVTGNPGqANYCASK 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 150247226 181 YGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSK 216
Cdd:PRK12936 157 AGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGK 192
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 27-216 1.40e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 86.25  E-value: 1.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKEcvRDKGL 106
Cdd:PRK06841  13 LSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVIS--AFGRI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 107 WGLVNNAGISlPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFGG-GYCISKYGVE 184
Cdd:PRK06841  91 DILVNSAGVA-LLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRhMIAAGGGKIVNLASQAGVVALERHvAYCASKAGVV 169

                        170       180       190
                 ....*....|....*....|....*....|..
gi 150247226 185 AFSDSLRRELSYFGVKVAMIEPGYFKTAVTSK 216
Cdd:PRK06841 170 GMTKVLALEWGPYGITVNAISPTVVLTELGKK 201
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 25-214 5.34e-19

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 84.64  E-value: 5.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  25 SHLRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRG---QTSDRLETVTLDVTKTESVAAAAQWVKEcv 101
Cdd:PRK12939   3 SNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAaleAAGGRAHAIAADLADPASVQRFFDAAAA-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 102 RDKGLWGLVNNAGIsLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRR-ARGRVVNVSSvmgRVSLFG----GGY 176
Cdd:PRK12939  81 ALGGLDGLVNNAGI-TNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDsGRGRIVNLAS---DTALWGapklGAY 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 150247226 177 CISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVT 214
Cdd:PRK12939 157 VASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEAT 194
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 30-213 5.38e-19

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: 84.04  E-value: 5.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQT-SDRLETVTLDVTKTESVAAA-AQ-WVKECVRDKGL 106
Cdd:cd08931    1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELgAENVVAGALDVTDRAAWAAAlADfAAATGGRLDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 107 WglvNNAGIsLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARG-RVVNVSSVMGrvsLFG----GGYCISKY 181
Cdd:cd08931   81 F---NNAGV-GRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGaRVINTASSSA---IYGqpdlAVYSATKF 153

                        170       180       190
                 ....*....|....*....|....*....|..
gi 150247226 182 GVEAFSDSLRRELSYFGVKVAMIEPGYFKTAV 213
Cdd:cd08931  154 AVRGLTEALDVEWARHGIRVADVWPWFVDTPI 185
PRK05855 PRK05855
SDR family oxidoreductase;
27-219 9.25e-19

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 86.57  E-value: 9.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQ---LRGQTSDRLETVTLDVTKTESVAAAAQWVKEC--V 101
Cdd:PRK05855 313 FSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERtaeLIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEhgV 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 102 RDKglwgLVNNAGISLptAPNELLTK-QDFVTILDVNLLGVIDVTLSLLP-LVRRAR-GRVVNVSSVMGrvslFG----- 173
Cdd:PRK05855 393 PDI----VVNNAGIGM--AGGFLDTSaEDWDRVLDVNLWGVIHGCRLFGRqMVERGTgGHIVNVASAAA----YApsrsl 462

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 150247226 174 GGYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKERF 219
Cdd:PRK05855 463 PAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVATTRF 508
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 27-244 1.02e-18

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


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 83.72  E-value: 1.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSD-----RLETVTLDVTKTESVAAaaqWVKECV 101
Cdd:cd05330    1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEiapdaEVLLIKADVSDEAQVEA---YVDATV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 102 RDKG-LWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMG-RVSLFGGGYCI 178
Cdd:cd05330   78 EQFGrIDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGsGMIVNTASVGGiRGVGNQSGYAA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150247226 179 SKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSkerflKSFLEIwdrsSPEVKEAYGEKFVA 244
Cdd:cd05330  158 AKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVE-----GSLKQL----GPENPEEAGEEFVS 214
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 27-214 1.68e-18

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: 82.92  E-value: 1.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAaqwVKECVRD-KG 105
Cdd:cd08944    1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAAL---FERAVEEfGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVR-RARGRVVNVSSVMGRV-SLFGGGYCISKYGV 183
Cdd:cd08944   78 LDLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIaRGGGSIVNLSSIAGQSgDPGYGAYGASKAAI 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 150247226 184 EAFSDSLRRELSYFGVKVAMIEPGYFKTAVT 214
Cdd:cd08944  158 RNLTRTLAAELRHAGIRCNALAPGLIDTPLL 188
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 24-211 1.77e-18

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 83.13  E-value: 1.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  24 LSHLRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEK-GAEQLRGQTSDR---LETVTLDVTKTESvaaAAQWVKE 99
Cdd:PRK12935   1 MVQLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKeAAENLVNELGKEghdVYAVQADVSKVED---ANRLVEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 100 CVRDKG-LWGLVNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSLFG-GGY 176
Cdd:PRK12935  78 AVNHFGkVDILVNNAGITRDRTFKKL-NREDWERVIDVNLSSVFNTTSAVLPYITEAEeGRIISISSIIGQAGGFGqTNY 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 150247226 177 CISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK12935 157 SAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDT 191
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 27-207 2.30e-18

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 83.14  E-value: 2.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQlrgqtsDRLETVTLDVTKTESVAAAAQWVKEcvRDKGL 106
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQH------ENYQFVPTDVSSAEEVNHTVAEIIE--KFGRI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 107 WGLVNNAGISLP--------TAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMG-RVSLFGGGY 176
Cdd:PRK06171  79 DGLVNNAGINIPrllvdekdPAGKYELNEAAFDKMFNINQKGVFLMSQAVARqMVKQHDGVIVNMSSEAGlEGSEGQSCY 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 150247226 177 CISKYGVEAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:PRK06171 159 AATKAALNSFTRSWAKELGKHNIRVVGVAPG 189
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-240 2.35e-18

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 82.58  E-value: 2.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAAC-LTEKGAEQLRGQTSDRLETVTL---DVTKTESVAAAaqwVKECVR 102
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYdINEEAAQELLEEIKEEGGDAIAvkaDVSSEEDVENL---VEQIVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 DKG-LWGLVNNAGIS----LPTAPNELLTKqdfvtILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSL-FGGG 175
Cdd:PRK05565  80 KFGkIDILVNNAGISnfglVTDMTDEEWDR-----VIDVNLTGVMLLTRYALPyMIKRKSGVIVNISSIWGLIGAsCEVL 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150247226 176 YCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTavtskerflksflEIWDRSSPEVKEAYGE 240
Cdd:PRK05565 155 YSASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDT-------------EMWSSFSEEDKEGLAE 206
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 33-241 2.40e-18

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: 82.97  E-value: 2.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  33 FITGCDSGFGKLLARQLDARGLRVLaacLTEKGAEQLRgQTSDRLET-------VTLDVTKTESVAAAaqwVKECVRDKG 105
Cdd:cd08945    7 LVTGATSGIGLAIARRLGKEGLRVF---VCARGEEGLA-TTVKELREagveadgRTCDVRSVPEIEAL---VAAAVARYG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LWG-LVNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLP---LVRRARGRVVNVSSVMGRVS-LFGGGYCISK 180
Cdd:cd08945   80 PIDvLVNNAGRSGGGATAEL-ADELWLDVVETNLTGVFRVTKEVLKaggMLERGTGRIINIASTGGKQGvVHAAPYSASK 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150247226 181 YGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKERflKSFLEIWDRSSPEVKEAYGEK 241
Cdd:cd08945  159 HGVVGFTKALGLELARTGITVNAVCPGFVETPMAASVR--EHYADIWEVSTEEAFDRITAR 217
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 27-215 4.90e-18

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: 81.69  E-value: 4.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLArQLDARglrvLAACLTEKG--AEQL---------RGQTSDRLETVTLDVTKTESVAAAaq 95
Cdd:cd05364    1 LSGKVAIITGSSSGIGAGTA-ILFAR----LGARLALTGrdAERLeetrqsclqAGVSEKKILLVVADLTEEEGQDRI-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  96 wVKECVRDKG-LWGLVNNAGISLPTApNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRVSLFGG 174
Cdd:cd05364   74 -ISTTLAKFGrLDILVNNAGILAKGG-GEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGRSFPGV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 150247226 175 -GYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTS 215
Cdd:cd05364  152 lYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHR 193
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 27-211 5.20e-18

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: 81.86  E-value: 5.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAAC----LTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAaqwVKECVR 102
Cdd:cd05369    1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGrkpeVLEAAAEEISSATGGRAHPIQCDVRDPEAVEAA---VDETLK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 DKG-LWGLVNNAGISLPtAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR--GRVVNVSSVMGRvslFGGGYCI- 178
Cdd:cd05369   78 EFGkIDILINNAAGNFL-APAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKhgGSILNISATYAY---TGSPFQVh 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 150247226 179 ---SKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:cd05369  154 saaAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPT 189
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
27-211 6.28e-18

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 81.60  E-value: 6.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAAC-----LTEKGAEQLRGQTSDRLETVTlDVTKTESVAAAAQWVKECV 101
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAGCgpnspRRVKWLEDQKALGFDFIASEG-NVGDWDSTKAAFDKVKAEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 102 RDKGLwgLVNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFG-GGYCIS 179
Cdd:PRK12938  80 GEIDV--LVNNAGITRDVVFRKM-TREDWTAVIDTNLTSLFNVTKQVIDgMVERGWGRIINISSVNGQKGQFGqTNYSTA 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 150247226 180 KYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK12938 157 KAGIHGFTMSLAQEVATKGVTVNTVSPGYIGT 188
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 25-214 1.53e-17

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 80.60  E-value: 1.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  25 SHLRDKYVFITGCDSGFGKLLARQLDARGLRVlaACL---TEKGAEQLRGQTSdrlETVTLDVTKTESVAAAAQWVKECV 101
Cdd:PRK06463   3 MRFKGKVALITGGTRGIGRAIAEAFLREGAKV--AVLynsAENEAKELREKGV---FTIKCDVGNRDQVKKSKEVVEKEF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 102 RDKGLwgLVNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMG-----RVSLFggg 175
Cdd:PRK06463  78 GRVDV--LVNNAGIMY-LMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKnGAIVNIASNAGigtaaEGTTF--- 151

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 150247226 176 YCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVT 214
Cdd:PRK06463 152 YAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMT 190
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 27-238 1.64e-17

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: 80.13  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKEcvRDKGL 106
Cdd:cd05345    3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALS--KFGRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 107 WGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMG---RVSLfgGGYCISKYG 182
Cdd:cd05345   81 DILVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPhMEEQGGGVIINIASTAGlrpRPGL--TWYNASKGW 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 150247226 183 VEAFSDSLRRELSYFGVKVAMIEPgyfktaVTSKERFLKSFLeiwDRSSPEVKEAY 238
Cdd:cd05345  159 VVTATKAMAVELAPRNIRVNCLCP------VAGETPLLSMFM---GEDTPENRAKF 205
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 27-207 1.76e-17

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 80.31  E-value: 1.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKgaeqlrGQTSDRLETVTLDVTKTESVAAA-AQWVKEcvrDKG 105
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFL------TQEDYPFATFVLDVSDAAAVAQVcQRLLAE---TGP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LWGLVNNAGIsLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFG-GGYCISKYGV 183
Cdd:PRK08220  77 LDVLVNAAGI-LRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPqFRRQRSGAIVTVGSNAAHVPRIGmAAYGASKAAL 155

                        170       180
                 ....*....|....*....|....
gi 150247226 184 EAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:PRK08220 156 TSLAKCVGLELAPYGVRCNVVSPG 179
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-206 2.18e-17

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 79.73  E-value: 2.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLR---GQTSDRLETVTLDVTKTESVAAAAQWVKECVRD 103
Cdd:PRK07666   5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAeevEAYGVKVVIATADVSDYEEVTAAIEQLKNELGS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 KGLwgLVNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMG-RVSLFGGGYCISKY 181
Cdd:PRK07666  85 IDI--LINNAGISKFGKFLEL-DPAEWEKIIQVNLMGVYYATRAVLPsMIERQSGDIINISSTAGqKGAAVTSAYSASKF 161

                        170       180
                 ....*....|....*....|....*
gi 150247226 182 GVEAFSDSLRRELSYFGVKVAMIEP 206
Cdd:PRK07666 162 GVLGLTESLMQEVRKHNIRVTALTP 186
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 31-207 2.50e-17

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


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 79.64  E-value: 2.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  31 YVFITGCDSGFGKLLARQLDARGLRVLAACLTE------KGAEQLRGqtSDRLETVTLDVTKTESVAAaaqwVKECVRDK 104
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARseeplqELKEELRP--GLRVTTVKADLSDAAGVEQ----LLEAIRKL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 G--LWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLV--RRARGRVVNVSSVMGRVSLFG-GGYCIS 179
Cdd:cd05367   75 DgeRDLLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFkkRGLKKTVVNVSSGAAVNPFKGwGLYCSS 154

                        170       180
                 ....*....|....*....|....*...
gi 150247226 180 KYGVEAFSDSLRRELSyfGVKVAMIEPG 207
Cdd:cd05367  155 KAARDMFFRVLAAEEP--DVRVLSYAPG 180
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 29-237 2.83e-17

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: 79.62  E-value: 2.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  29 DKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLR---GQTSDRLETVTLDVTKTESVAAAaqwVKECVRDKG 105
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAAselRAGGAGVLAVVADLTDPEDIDRL---VEKAGDAFG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 -LWGLVNNAGiSLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSLFGGGYC-ISKYG 182
Cdd:cd05344   78 rVDILVNNAG-GPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLTVKEPEPNLVLSnVARAG 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 150247226 183 VEAFSDSLRRELSYFGVKVAMIEPGYFKTavtskERFLKSFLEIWDRSSPEVKEA 237
Cdd:cd05344  157 LIGLVKTLSRELAPDGVTVNSVLPGYIDT-----ERVRRLLEARAEKEGISVEEA 206
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 27-208 3.26e-17

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 79.62  E-value: 3.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSD---RLETVTLDVTKTESVAAAAQWVKEcvRD 103
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDlgrRALAVPTDITDEDQCANLVALALE--RF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 KGLWGLVNNAGISLPTAPnelLTKQDFVTI---LDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRVSLFG-GGYCIS 179
Cdd:PRK07890  81 GRVDALVNNAFRVPSMKP---LADADFAHWravIELNVLGTLRLTQAFTPALAESGGSIVMINSMVLRHSQPKyGAYKMA 157

                        170       180
                 ....*....|....*....|....*....
gi 150247226 180 KYGVEAFSDSLRRELSYFGVKVAMIEPGY 208
Cdd:PRK07890 158 KGALLAASQSLATELGPQGIRVNSVAPGY 186
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 30-241 4.83e-17

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: 79.34  E-value: 4.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACL----TEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKEcvRDKG 105
Cdd:cd05366    3 KVAIITGAAQGIGRAIAERLAADGFNIVLADLnleeAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVE--KFGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LWGLVNNAGISlPTAPNELLTKQDFVTILDVNLLGVIdvtLSLLPLVRR-----ARGRVVNVSSVMGRVSLFG-GGYCIS 179
Cdd:cd05366   81 FDVMVNNAGIA-PITPLLTITEEDLKKVYAVNVFGVL---FGIQAAARQfkklgHGGKIINASSIAGVQGFPNlGAYSAS 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150247226 180 KYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTavtskerflksflEIWDRSSPEVKEAYGEK 241
Cdd:cd05366  157 KFAVRGLTQTAAQELAPKGITVNAYAPGIVKT-------------EMWDYIDEEVGEIAGKP 205
PRK07454 PRK07454
SDR family oxidoreductase;
32-235 5.96e-17

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 78.46  E-value: 5.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGK--------------LLARQLDArgLRVLAACLTEKGAEqlrgqtsdrLETVTLDVTKTESVAAAaqwV 97
Cdd:PRK07454   9 ALITGASSGIGKatalafakagwdlaLVARSQDA--LEALAAELRSTGVK---------AAAYSIDLSNPEAIAPG---I 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  98 KECVRDKGLWG-LVNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVR-RARGRVVNVSSVMGRVSLFG-G 174
Cdd:PRK07454  75 AELLEQFGCPDvLINNAGMAY-TGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRaRGGGLIINVSSIAARNAFPQwG 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150247226 175 GYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGyfktAVTSkerflksflEIWDrsSPEVK 235
Cdd:PRK07454 154 AYCVSKAALAAFTKCLAEEERSHGIRVCTITLG----AVNT---------PLWD--TETVQ 199
PRK07774 PRK07774
SDR family oxidoreductase;
27-214 6.00e-17

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 78.63  E-value: 6.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLET---VTLDVTKTESVAA-AAQWVKECvr 102
Cdd:PRK07774   4 FDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTaiaVQVDVSDPDSAKAmADATVSAF-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 dKGLWGLVNNAGISLPTAPNELLTK--QDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGrvSLFGGGYCIS 179
Cdd:PRK07774  82 -GGIDYLVNNAAIYGGMKLDLLITVpwDYYKKFMSVNLDGALVCTRAVYKhMAKRGGGAIVNQSSTAA--WLYSNFYGLA 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 150247226 180 KYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVT 214
Cdd:PRK07774 159 KVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEAT 193
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 27-246 6.40e-17

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: 78.53  E-value: 6.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRV----LAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAaqwVKECVR 102
Cdd:cd05352    6 LKGKVAIVTGGSRGIGLAIARALAEAGADVaiiyNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKT---FKQIQK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 DKG-LWGLVNNAGISLPTaPNELLTKQDFVTILDVNLLGVIDVTLSL-LPLVRRARGRVVNVSSVMGRV---SLFGGGYC 177
Cdd:cd05352   83 DFGkIDILIANAGITVHK-PALDYTYEQWNKVIDVNLNGVFNCAQAAaKIFKKQGKGSLIITASMSGTIvnrPQPQAAYN 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150247226 178 ISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKERflKSFLEIWDRSSPEVKEAYGEKFVADY 246
Cdd:cd05352  162 ASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVD--KELRKKWESYIPLKRIALPEELVGAY 228
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 26-211 6.86e-17

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 78.30  E-value: 6.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  26 HLRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQ-LRGQTSDRLETVTLDVTkteSVAAAAQWVKECVRDK 104
Cdd:PRK12828   4 SLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQtLPGVPADALRIGGIDLV---DPQAARRAVDEVNRQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 G-LWGLVNNAGIsLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFG-GGYCISKY 181
Cdd:PRK12828  81 GrLDALVNIAGA-FVWGTIADGDADTWDRMYGVNVKTTLNASKAALPaLTASGGGRIVNIGAGAALKAGPGmGAYAAAKA 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 150247226 182 GVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK12828 160 GVARLTEALAAELLDRGITVNAVLPSIIDT 189
PRK09242 PRK09242
SDR family oxidoreductase;
27-215 7.58e-17

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 78.64  E-value: 7.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSD-----RLETVTLDVTKTESVAAAAQWVKECV 101
Cdd:PRK09242   7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEefperEVHGLAADVSDDEDRRAILDWVEDHW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 102 rdKGLWGLVNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLPLV-RRARGRVVNVSSVMGRVSLFGGG-YCIS 179
Cdd:PRK09242  87 --DGLHILVNNAGGNIRKAAIDY-TEDEWRGIFETNLFSAFELSRYAHPLLkQHASSAIVNIGSVSGLTHVRSGApYGMT 163

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 150247226 180 KYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTS 215
Cdd:PRK09242 164 KAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTS 199
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
30-219 1.36e-16

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 77.80  E-value: 1.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTE-KGAEQLRGQTSDRLETVTLDVTkteSVAAAAQWVKECVR------ 102
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTEnKELTKLAEQYNSNLTFHSLDLQ---DVHELETNFNEILSsiqedn 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 DKGLWgLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARG--RVVNVSSVMGRVSLFG-GGYCIS 179
Cdd:PRK06924  79 VSSIH-LINNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKVdkRVINISSGAAKNPYFGwSAYCSS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 150247226 180 KYGVEAFSDS--LRRELSYFGVKVAMIEPGYFKTAV------TSKERF 219
Cdd:PRK06924 158 KAGLDMFTQTvaTEQEEEEYPVKIVAFSPGVMDTNMqaqirsSSKEDF 205
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 27-211 1.91e-16

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 77.62  E-value: 1.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTE----KGAEQLRGQTSDRLeTVTLDVTKTESVAAAAQWVKECvr 102
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDeaaaAAAEALQKAGGKAI-GVAMDVTDEEAINAGIDYAVET-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 dkglWG----LVNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRV-SLFGGGY 176
Cdd:PRK12429  79 ----FGgvdiLVNNAGIQH-VAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGgGRIINMASVHGLVgSAGKAAY 153

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 150247226 177 CISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK12429 154 VSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDT 188
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 27-213 2.26e-16

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: 77.04  E-value: 2.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEK-GAEQLRGQ-TSDRLET--VTLDVTKTESVAAAAQwvkECVR 102
Cdd:cd05358    1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEdAAEEVVEEiKAVGGKAiaVQADVSKEEDVVALFQ---SAIK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 DKG-LWGLVNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLPLVR--RARGRVVNVSSVMGRVSLFG-GGYCI 178
Cdd:cd05358   78 EFGtLDILVNNAGLQGDASSHEM-TLEDWNKVIDVNLTGQFLCAREAIKRFRksKIKGKIINMSSVHEKIPWPGhVNYAA 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 150247226 179 SKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAV 213
Cdd:cd05358  157 SKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPI 191
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 26-222 3.53e-16

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 76.54  E-value: 3.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  26 HLRDKYVFITGCDSGFGKLLARQLDARGLRVlaACL---------TEKGAEQLRGQTsdrlETVTLDVTKTESVAAAAQW 96
Cdd:PRK08217   2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAKL--ALIdlnqekleeAVAECGALGTEV----RGYAANVTDEEDVEATFAQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  97 VKEcvrDKG-LWGLVNNAGIS-----LPTAPNELLTK---QDFVTILDVNLLGVI----DVTLSLLPLVRRarGRVVNVS 163
Cdd:PRK08217  76 IAE---DFGqLNGLINNAGILrdgllVKAKDGKVTSKmslEQFQSVIDVNLTGVFlcgrEAAAKMIESGSK--GVIINIS 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 164 SV-----MGRVSlfgggYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVT------SKERFLKS 222
Cdd:PRK08217 151 SIaragnMGQTN-----YSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTaamkpeALERLEKM 215
PRK07063 PRK07063
SDR family oxidoreductase;
27-214 4.93e-16

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 76.24  E-value: 4.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRV----LAACLTEKGAEQLRGQTSD-RLETVTLDVTKTESVAAAaqwVKECV 101
Cdd:PRK07063   5 LAGKVALVTGAAQGIGAAIARAFAREGAAValadLDAALAERAAAAIARDVAGaRVLAVPADVTDAASVAAA---VAAAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 102 RDKG-LWGLVNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFGG-GYCI 178
Cdd:PRK07063  82 EAFGpLDVLVNNAGINVFADPLAM-TDEDWRRCFAVDLDGAWNGCRAVLPgMVERGRGSIVNIASTHAFKIIPGCfPYPV 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 150247226 179 SKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVT 214
Cdd:PRK07063 161 AKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLT 196
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 32-212 5.78e-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: 5.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRVLAACLtekgAEQLRGQTSDRLETVTLDVTKTESVAA-AAQWVKEcvrDKGLWGLV 110
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIALDL----PFVLLLEYGDPLRLTPLDVADAAAVREvCSRLLAE---HGPIDALV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 111 NNAGIsLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMG---RVSLfgGGYCISKYGVEAF 186
Cdd:cd05331   74 NCAGV-LRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPhMKDRRTGAIVTVASNAAhvpRISM--AAYGASKAALASL 150

                        170       180
                 ....*....|....*....|....*.
gi 150247226 187 SDSLRRELSYFGVKVAMIEPGYFKTA 212
Cdd:cd05331  151 SKCLGLELAPYGVRCNVVSPGSTDTA 176
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 30-255 6.21e-16

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: 76.35  E-value: 6.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACL----TEKGAEQLRGQTSDRLETVT-LDVTKTESVAAAAQWVKEcvRDK 104
Cdd:cd09807    2 KTVIITGANTGIGKETARELARRGARVIMACRdmakCEEAAAEIRRDTLNHEVIVRhLDLASLKSIRAFAAEFLA--EED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 GLWGLVNNAGISLptAPnELLTKQDFVTILDVNLLGVIDVTLSLLPLVRR-ARGRVVNVSSVM---GRVSL--------- 171
Cdd:cd09807   80 RLDVLINNAGVMR--CP-YSKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKsAPSRIVNVSSLAhkaGKINFddlnseksy 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 172 -FGGGYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKERFLKSFLE--IWDRSSPEVKEAYGEKFVADYKK 248
Cdd:cd09807  157 nTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELGRHTGIHHLFLStlLNPLFWPFVKTPREGAQTSIYLA 236


                 ....*..
gi 150247226 249 SAEQMEQ 255
Cdd:cd09807  237 LAEELEG 243
PRK06114 PRK06114
SDR family oxidoreductase;
22-216 1.36e-15

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 75.20  E-value: 1.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  22 QVLSHLRDKYVFITGCDSGFGKLLARQLDARGLRVlaACLTEKGAEQLrGQTSDRLET-------VTLDVTKTESVAAAA 94
Cdd:PRK06114   1 PQLFDLDGQVAFVTGAGSGIGQRIAIGLAQAGADV--ALFDLRTDDGL-AETAEHIEAagrraiqIAADVTSKADLRAAV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  95 QWVKEcvRDKGLWGLVNNAGISlPTAPNELLTKQDFVTILDVNLLGVIdvtLSLLP----LVRRARGRVVNVSSVMGRVS 170
Cdd:PRK06114  78 ARTEA--ELGALTLAVNAAGIA-NANPAEEMEEEQWQTVMDINLTGVF---LSCQAearaMLENGGGSIVNIASMSGIIV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 150247226 171 ---LFGGGYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSK 216
Cdd:PRK06114 152 nrgLLQAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTR 200
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 26-221 2.88e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 74.17  E-value: 2.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  26 HLRDKYVFITGCDSGFGKLLARQLDARGLRVLAAcltekgAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKEcvRDKG 105
Cdd:PRK06523   6 ELAGKRALVTGGTKGIGAATVARLLEAGARVVTT------ARSRPDDLPEGVEFVAADLTTAEGCAAVARAVLE--RLGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LWGLVNNAGISlpTAPN---ELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFGG--GYCIS 179
Cdd:PRK06523  78 VDILVHVLGGS--SAPAggfAALTDEEWQDELNLNLLAAVRLDRALLPgMIARGSGVIIHVTSIQRRLPLPESttAYAAA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 150247226 180 KYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTavTSKERFLK 221
Cdd:PRK06523 156 KAALSTYSKSLSKEVAPKGVRVNTVSPGWIET--EAAVALAE 195
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
27-207 2.97e-15

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 74.29  E-value: 2.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAaqwVKECV-RDKG 105
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRI---VAAAVeRFGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LWGLVNNAGIsLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARG-RVVNVSSVMGR-----VSLfgggYCI 178
Cdd:PRK07067  81 IDILFNNAAL-FDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARhMVEQGRGgKIINMASQAGRrgealVSH----YCA 155

                        170       180
                 ....*....|....*....|....*....
gi 150247226 179 SKYGVEAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:PRK07067 156 TKAAVISYTQSAALALIRHGINVNAIAPG 184
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 27-214 4.38e-15

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 73.63  E-value: 4.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSD---RLETVTLDVTKTESVAAAAQWVKECVrd 103
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQegiKAHAAPFNVTHKQEVEAAIEHIEKDI-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 KGLWGLVNNAGISLPTAPNElLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSV---MGRVSLfgGGYCIS 179
Cdd:PRK08085  85 GPIDVLINNAGIQRRHPFTE-FPEQEWNDVIAVNQTAVFLVSQAVARyMVKRQAGKIINICSMqseLGRDTI--TPYAAS 161

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 150247226 180 KYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVT 214
Cdd:PRK08085 162 KGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMT 196
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 27-206 4.92e-15

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: 73.27  E-value: 4.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDrLETVTLDVTKTESVAAAAQWVKEcvrdkgL 106
Cdd:cd05351    5 FAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPG-IEPVCVDLSDWDATEEALGSVGP------V 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 107 WGLVNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP--LVRRARGRVVNVSSVMGRVSLFG-GGYCISKYGV 183
Cdd:cd05351   78 DLLVNNAAVAI-LQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARgmIARGVPGSIVNVSSQASQRALTNhTVYCSTKAAL 156

                        170       180
                 ....*....|....*....|...
gi 150247226 184 EAFSDSLRRELSYFGVKVAMIEP 206
Cdd:cd05351  157 DMLTKVMALELGPHKIRVNSVNP 179
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-218 6.35e-15

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 73.23  E-value: 6.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAE--QLRGQTSDRLETVTLDVTKTESVAAAaqwVKECVRDK 104
Cdd:PRK06935  13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWDEtrRLIEKEGRKVTFVQVDLTKPESAEKV---VKEALEEF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 G-LWGLVNNAGIsLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGrvslFGGG-----YC 177
Cdd:PRK06935  90 GkIDILVNNAGT-IRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKvMAKQGSGKIINIASMLS----FQGGkfvpaYT 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 150247226 178 ISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKER 218
Cdd:PRK06935 165 ASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAPIR 205
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 27-207 6.56e-15

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: 72.87  E-value: 6.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTE-KGAEQLRGQTSDRLETVTLDVTKTESVAAAaqwVKECVRDKG 105
Cdd:cd05326    2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDdAGQAVAAELGDPDISFVHCDVTVEADVRAA---VDTAVARFG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 -LWGLVNNAGISLPTAPNEL-LTKQDFVTILDVNLLGVIDVTL-SLLPLVRRARGRVVNVSSVMGRVSLFGG-GYCISKY 181
Cdd:cd05326   79 rLDIMFNNAGVLGAPCYSILeTSLEEFERVLDVNVYGAFLGTKhAARVMIPAKKGSIVSVASVAGVVGGLGPhAYTASKH 158

                        170       180
                 ....*....|....*....|....*.
gi 150247226 182 GVEAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:cd05326  159 AVLGLTRSAATELGEHGIRVNCVSPY 184
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 23-217 8.58e-15

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 73.01  E-value: 8.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  23 VLSHLRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAE---QLRGQTSDRLETVTLDVTKTESVAAAAQWVKE 99
Cdd:PRK13394   1 MMSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANavaDEINKAGGKAIGVAMDVTNEDAVNAGIDKVAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 100 cvRDKGLWGLVNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR--GRVVNVSSVMGRV-SLFGGGY 176
Cdd:PRK13394  81 --RFGSVDILVSNAGIQI-VNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHSHEaSPLKSAY 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 150247226 177 CISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKE 217
Cdd:PRK13394 158 VTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQ 198
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 34-211 8.89e-15

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 72.71  E-value: 8.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  34 ITGCDSGFGKLLARQLDARGLRVLAACLT-EKGAEQLRGQtsDRLETVTLDVTKTESVAAAaqwVKECVRDKG-LWGLVN 111
Cdd:cd05371    7 VTGGASGLGLATVERLLAQGAKVVILDLPnSPGETVAKLG--DNCRFVPVDVTSEKDVKAA---LALAKAKFGrLDIVVN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 112 NAGISLP--------TAPNELltkQDFVTILDVNLLGVIDVT-LSLLPLVRRA------RGRVVNVSSVMGRVSLFG-GG 175
Cdd:cd05371   82 CAGIAVAaktynkkgQQPHSL---ELFQRVINVNLIGTFNVIrLAAGAMGKNEpdqggeRGVIINTASVAAFEGQIGqAA 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 150247226 176 YCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:cd05371  159 YSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDT 194
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 27-216 9.71e-15

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


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 72.22  E-value: 9.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLaacLTEKGAEQLRgQTSDRLET--------VTLDV---TKTESVAAAAQ 95
Cdd:cd05340    2 LNDRIILVTGASDGIGREAALTYARYGATVI---LLGRNEEKLR-QVADHINEeggrqpqwFILDLltcTSENCQQLAQR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  96 WVKECVRdkgLWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRV-SLFG 173
Cdd:cd05340   78 IAVNYPR---LDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQgRANW 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 150247226 174 GGYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSK 216
Cdd:cd05340  155 GAYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRAS 197
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 27-216 1.51e-14

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: 72.16  E-value: 1.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAAC----LTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKEcvr 102
Cdd:cd05343    4 WRGRVALVTGASVGIGAAVARALVQHGMKVVGCArrvdKIEALAAECQSAGYPTLFPYQCDLSNEEQILSMFSAIRT--- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 dkgLWG----LVNNAGISlptAPNELLT--KQDFVTILDVNLLGVIDVT-LSLLPLVRR--ARGRVVNVSSVMGR----V 169
Cdd:cd05343   81 ---QHQgvdvCINNAGLA---RPEPLLSgkTEGWKEMFDVNVLALSICTrEAYQSMKERnvDDGHIININSMSGHrvppV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 150247226 170 SLFgGGYCISKYGVEAFSDSLRRELSYF--GVKVAMIEPGYFKTAVTSK 216
Cdd:cd05343  155 SVF-HFYAATKHAVTALTEGLRQELREAktHIRATSISPGLVETEFAFK 202
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 29-207 1.72e-14

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


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 72.18  E-value: 1.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  29 DKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQ--TSDRLETVTL--DVTKTESVAaaaQWVKECVRDK 104
Cdd:cd08933    9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESElnRAGPGSCKFVpcDVTKEEDIK---TLISVTVERF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 G-LWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRV-SLFGGGYCISKYG 182
Cdd:cd08933   86 GrIDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIgQKQAAPYVATKGA 165

                        170       180
                 ....*....|....*....|....*
gi 150247226 183 VEAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:cd08933  166 ITAMTKALAVDESRYGVRVNCISPG 190
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
30-248 2.41e-14

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 73.34  E-value: 2.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQ--TSDRLETVTLDVTKTESVAAAAQWVkeCVRDKGLW 107
Cdd:PRK08324 423 KVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAElgGPDRALGVACDVTDEAAVQAAFEEA--ALAFGGVD 500

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 108 GLVNNAGISLPtAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRA--RGRVVNVSSVMGRVSLFG-GGYCISKygve 184
Cdd:PRK08324 501 IVVSNAGIAIS-GPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQglGGSIVFIASKNAVNPGPNfGAYGAAK---- 575

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150247226 185 AFSDSLRR----ELSYFGVKVAMIEPgyfkTAVTSKERflksfleIWDrssPEVKE----AYG---EKFVADYKK 248
Cdd:PRK08324 576 AAELHLVRqlalELGPDGIRVNGVNP----DAVVRGSG-------IWT---GEWIEaraaAYGlseEELEEFYRA 636
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
30-211 2.89e-14

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 71.30  E-value: 2.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLE---TVTLDVTKTESVAAAAQWVKECVRDkgL 106
Cdd:PRK08643   3 KVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGkaiAVKADVSDRDQVFAAVRQVVDTFGD--L 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 107 WGLVNNAGISlPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR--GRVVNVSSVMGRV-----SLFGGgyciS 179
Cdd:PRK08643  81 NVVVNNAGVA-PTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGhgGKIINATSQAGVVgnpelAVYSS----T 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 150247226 180 KYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK08643 156 KFAVRGLTQTAARDLASEGITVNAYAPGIVKT 187
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-216 4.79e-14

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 70.38  E-value: 4.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKgaeqlrGQTSDRLETVTLDVtkTESVAAAAQWVKECvrDKgl 106
Cdd:PRK06550   3 FMTKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDK------PDLSGNFHFLQLDL--SDDLEPLFDWVPSV--DI-- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 107 wgLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSlfGGG---YCISKYG 182
Cdd:PRK06550  71 --LCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPqMLERKSGIIINMCSIASFVA--GGGgaaYTASKHA 146

                        170       180       190
                 ....*....|....*....|....*....|....
gi 150247226 183 VEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSK 216
Cdd:PRK06550 147 LAGFTKQLALDYAKDGIQVFGIAPGAVKTPMTAA 180
PRK07201 PRK07201
SDR family oxidoreductase;
18-206 5.12e-14

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 72.29  E-value: 5.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  18 YRERQVLSHLRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETV---TLDVTKTESVAAAa 94
Cdd:PRK07201 360 ARRRDLRGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAhayTCDLTDSAAVDHT- 438

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  95 qwVKECVRDKGlwG---LVNNAGISLPTAPnELLTKQ--DFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSS--VM 166
Cdd:PRK07201 439 --VKDILAEHG--HvdyLVNNAGRSIRRSV-ENSTDRfhDYERTMAVNYFGAVRLILGLLPhMRERRFGHVVNVSSigVQ 513

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 150247226 167 GRVSLFgGGYCISKYGVEAFSDSLRRELSYFG----------VKVAMIEP 206
Cdd:PRK07201 514 TNAPRF-SAYVASKAALDAFSDVAASETLSDGitfttihmplVRTPMIAP 562
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 32-211 5.13e-14

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 70.52  E-value: 5.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRV----LAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVRDKG-L 106
Cdd:PRK12827   9 VLITGGSGGLGRAIAVRLAADGADVivldIHPMRGRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAGVEEFGrL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 107 WGLVNNAGISlPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR--GRVVNVSSVMG-RVSLFGGGYCISKYGV 183
Cdd:PRK12827  89 DILVNNAGIA-TDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARrgGRIVNIASVAGvRGNRGQVNYAASKAGL 167

                        170       180
                 ....*....|....*....|....*...
gi 150247226 184 EAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK12827 168 IGLTKTLANELAPRGITVNAVAPGAINT 195
PRK06194 PRK06194
hypothetical protein; Provisional
 34-256 5.52e-14

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 70.81  E-value: 5.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  34 ITGCDSGFGKLLARQLDARGLR-VLAACLT---EKGAEQLRGQTSDRLETVTlDVTKTESVAAAAQWVKECVRDKGLwgL 109
Cdd:PRK06194  11 ITGAASGFGLAFARIGAALGMKlVLADVQQdalDRAVAELRAQGAEVLGVRT-DVSDAAQVEALADAALERFGAVHL--L 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 110 VNNAGislpTAPNELL---TKQDFVTILDVNLLGVIDVTLSLLPLVRRA-------RGRVVNVSSVMGRVSLFGGG-YCI 178
Cdd:PRK06194  88 FNNAG----VGAGGLVwenSLADWEWVLGVNLWGVIHGVRAFTPLMLAAaekdpayEGHIVNTASMAGLLAPPAMGiYNV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 179 SKYGVEAFSDSLRRELSYFG--VKVAMIEPGYFKTAVTSKERFLKSFL--EIWDRSSPEVKEAYGEKFVADYKKSAEQME 254
Cdd:PRK06194 164 SKHAVVSLTETLYQDLSLVTdqVGASVLCPYFVPTGIWQSERNRPADLanTAPPTRSQLIAQAMSQKAVGSGKVTAEEVA 243


                 ..
gi 150247226 255 QK 256
Cdd:PRK06194 244 QL 245
PRK06484 PRK06484
short chain dehydrogenase; Validated
 28-211 6.57e-14

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 72.19  E-value: 6.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  28 RDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAaqwVKECVRDKG-L 106
Cdd:PRK06484   4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREG---FEQLHREFGrI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 107 WGLVNNAGISLPTAPNEL-LTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR--GRVVNVSSVMGRVSLFG-GGYCISKYG 182
Cdd:PRK06484  81 DVLVNNAGVTDPTMTATLdTTLEEFARLQAINLTGAYLVAREALRLMIEQGhgAAIVNVASGAGLVALPKrTAYSASKAA 160

                        170       180
                 ....*....|....*....|....*....
gi 150247226 183 VEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK06484 161 VISLTRSLACEWAAKGIRVNAVLPGYVRT 189
PRK06949 PRK06949
SDR family oxidoreductase;
27-211 9.71e-14

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 69.79  E-value: 9.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRV-LAACLTEKGAE---QLRGQTSDRlETVTLDVTKTESV-AAAAQWVKECv 101
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVvLASRRVERLKElraEIEAEGGAA-HVVSLDVTDYQSIkAAVAHAETEA- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 102 rdkglwG----LVNNAGISlptAPNELL--TKQDFVTILDVNLLGVIDVTLSLLP-LVRRARG--------RVVNVSSVM 166
Cdd:PRK06949  85 ------GtidiLVNNSGVS---TTQKLVdvTPADFDFVFDTNTRGAFFVAQEVAKrMIARAKGagntkpggRIINIASVA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 150247226 167 G-RVSLFGGGYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK06949 156 GlRVLPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDT 201
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 27-211 9.78e-14

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


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 69.61  E-value: 9.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEK-GAEQLRGQTSD---RLETVTLDVTKTESVAAAAQWVKEcvR 102
Cdd:cd05362    1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNYASSKaAAEEVVAEIEAaggKAIAVQADVSDPSQVARLFDAAEK--A 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 DKGLWGLVNNAGISLPtAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRArGRVVNVSSVMGRVSL-FGGGYCISKY 181
Cdd:cd05362   79 FGGVDILVNNAGVMLK-KPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDG-GRIINISSSLTAAYTpNYGAYAGSKA 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 150247226 182 GVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:cd05362  157 AVEAFTRVLAKELGGRGITVNAVAPGPVDT 186
PRK05866 PRK05866
SDR family oxidoreductase;
27-206 1.23e-13

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 70.16  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDR---LETVTLDVTKTESVAAAAQWVKEcvRD 103
Cdd:PRK05866  38 LTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAggdAMAVPCDLSDLDAVDALVADVEK--RI 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 KGLWGLVNNAGISLPTAPNELLTK-QDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSS--VMGRVSLFGGGYCIS 179
Cdd:PRK05866 116 GGVDILINNAGRSIRRPLAESLDRwHDVERTMVLNYYAPLRLIRGLAPgMLERGDGHIINVATwgVLSEASPLFSVYNAS 195

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 150247226 180 KYGVEAFSDSLRRELSYFGVKVA----------MIEP 206
Cdd:PRK05866 196 KAALSAVSRVIETEWGDRGVHSTtlyyplvatpMIAP 232
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 28-217 1.28e-13

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: 69.40  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  28 RDKYVFITGCDSGFGKLLARQLDARGLRVL------AACLtEKGAEQLRGQTSDRLETVTLDVTKtesVAAAAQWVKECV 101
Cdd:cd08940    1 KGKVALVTGSTSGIGLGIARALAAAGANIVlngfgdAAEI-EAVRAGLAAKHGVKVLYHGADLSK---PAAIEDMVAYAQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 102 RDKG-LWGLVNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVR-RARGRVVNVSSVMGRV-SLFGGGYCI 178
Cdd:cd08940   77 RQFGgVDILVNNAGIQH-VAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKkQGWGRIINIASVHGLVaSANKSAYVA 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 150247226 179 SKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKE 217
Cdd:cd08940  156 AKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPLVEKQ 194
PRK07775 PRK07775
SDR family oxidoreductase;
32-229 1.88e-13

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 69.40  E-value: 1.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRV-LAACLTEKGAEQLRGQTSDRLETVT--LDVTKTESVAAAAQWVKECVRDKGLwg 108
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVaLGARRVEKCEELVDKIRADGGEAVAfpLDVTDPDSVKSFVAQAEEALGEIEV-- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 109 LVNNAGISLPTAPNELLTKQdFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSS-VMGRVSLFGGGYCISKYGVEAF 186
Cdd:PRK07775  91 LVSGAGDTYFGKLHEISTEQ-FESQVQIHLVGANRLATAVLPgMIERRRGDLIFVGSdVALRQRPHMGAYGAAKAGLEAM 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 150247226 187 SDSLRRELSYFGVKVAMIEPGYFKTAV--TSKERFLKSFLEIWDR 229
Cdd:PRK07775 170 VTNLQMELEGTGVRASIVHPGPTLTGMgwSLPAEVIGPMLEDWAK 214
PRK08589 PRK08589
SDR family oxidoreductase;
27-225 3.07e-13

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 68.65  E-value: 3.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRG--QTSDRLETVTLDVTKTESVAAAAQWVKECVRDK 104
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDKikSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 GLwgLVNNAGIS-----LPTAPNELLTKqdfvtILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRVS-LFGGGYCI 178
Cdd:PRK08589  84 DV--LFNNAGVDnaagrIHEYPVDVFDK-----IMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAAdLYRSGYNA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 150247226 179 SKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT------AVTSKERFLKSFLE 225
Cdd:PRK08589 157 AKGAVINFTKSIAIEYGRDGIRANAIAPGTIETplvdklTGTSEDEAGKTFRE 209
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 30-207 3.73e-13

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 67.84  E-value: 3.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVL-----AACLTEKGAEQLRgQTSDRLETVTLDVTKTESVAAAAQWVKECVrdK 104
Cdd:PRK12937   6 KVAIVTGASRGIGAAIARRLAADGFAVAvnyagSAAAADELVAEIE-AAGGRAIAVQADVADAAAVTRLFDAAETAF--G 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 GLWGLVNNAGIsLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRArGRVVNVSSVMGRVSLFGGG-YCISKYGV 183
Cdd:PRK12937  83 RIDVLVNNAGV-MPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQG-GRIINLSTSVIALPLPGYGpYAASKAAV 160

                        170       180
                 ....*....|....*....|....
gi 150247226 184 EAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:PRK12937 161 EGLVHVLANELRGRGITVNAVAPG 184
PRK06124 PRK06124
SDR family oxidoreductase;
27-211 4.37e-13

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 67.82  E-value: 4.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVL-----AACLtEKGAEQLRgQTSDRLETVTLDVTKTESVAAAaqwVKECV 101
Cdd:PRK06124   9 LAGQVALVTGSARGLGFEIARALAGAGAHVLvngrnAATL-EAAVAALR-AAGGAAEALAFDIADEEAVAAA---FARID 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 102 RDKG-LWGLVNNAGiSLPTAPNELLTKQDFVTILDVNLLGVIDVT-LSLLPLVRRARGRVVNVSSVMGRVSLFGGG-YCI 178
Cdd:PRK06124  84 AEHGrLDILVNNVG-ARDRRPLAELDDAAIRALLETDLVAPILLSrLAAQRMKRQGYGRIIAITSIAGQVARAGDAvYPA 162

                        170       180       190
                 ....*....|....*....|....*....|...
gi 150247226 179 SKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK06124 163 AKQGLTGLMRALAAEFGPHGITSNAIAPGYFAT 195
PRK07074 PRK07074
SDR family oxidoreductase;
29-211 5.35e-13

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 67.49  E-value: 5.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  29 DKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSD-RLETVTLDVTKTESVAAAaqwVKECVRDKGLW 107
Cdd:PRK07074   2 KRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDaRFVPVACDLTDAASLAAA---LANAAAERGPV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 108 G-LVNNAGISLPTAPNELlTKQDFVTILDVNLLGV-IDVTLSLLPLVRRARGRVVNVSSVMGrVSLFGG-GYCISKYGVE 184
Cdd:PRK07074  79 DvLVANAGAARAASLHDT-TPASWRADNALNLEAAyLCVEAVLEGMLKRSRGAVVNIGSVNG-MAALGHpAYSAAKAGLI 156

                        170       180
                 ....*....|....*....|....*..
gi 150247226 185 AFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK07074 157 HYTKLLAVEYGRFGIRANAVAPGTVKT 183
PRK06101 PRK06101
SDR family oxidoreductase;
32-219 8.10e-13

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 66.82  E-value: 8.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRVLAaCLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKeCVRDkgLWglVN 111
Cdd:PRK06101   4 VLITGATSGIGKQLALDYAKQGWQVIA-CGRNQSVLDELHTQSANIFTLAFDVTDHPGTKAALSQLP-FIPE--LW--IF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 112 NAGiSLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARgRVVNVSSVMGRVSL-FGGGYCISKYGVEAFSDSL 190
Cdd:PRK06101  78 NAG-DCEYMDDGKVDATLMARVFNVNVLGVANCIEGIQPHLSCGH-RVVIVGSIASELALpRAEAYGASKAAVAYFARTL 155

                        170       180
                 ....*....|....*....|....*....
gi 150247226 191 RRELSYFGVKVAMIEPGYFKTAVTSKERF 219
Cdd:PRK06101 156 QLDLRPKGIEVVTVFPGFVATPLTDKNTF 184
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 27-196 1.22e-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: 66.61  E-value: 1.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAaqwVKECVRDKG- 105
Cdd:cd05348    2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERA---VARCVERFGk 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LWGLVNNAGI-----SLPTAPNELLTKQdFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRVSlfGGG---YC 177
Cdd:cd05348   79 LDCFIGNAGIwdystSLVDIPEEKLDEA-FDELFHINVKGYILGAKAALPALYATEGSVIFTVSNAGFYP--GGGgplYT 155

                        170
                 ....*....|....*....
gi 150247226 178 ISKYGVEAfsdsLRRELSY 196
Cdd:cd05348  156 ASKHAVVG----LVKQLAY 170
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 34-218 1.49e-12

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 66.52  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  34 ITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQ----LRGQTSDrLETVTLDVTKTESVAAAAQwvkECVRDKGLWGL 109
Cdd:PRK05876  11 ITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQavnhLRAEGFD-VHGVMCDVRHREEVTHLAD---EAFRLLGHVDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 110 V-NNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP--LVRRARGRVVNVSSVMGRVSLFG-GGYCISKYGVEA 185
Cdd:PRK05876  87 VfSNAGIVV-GGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPrlLEQGTGGHVVFTASFAGLVPNAGlGAYGVAKYGVVG 165

                        170       180       190
                 ....*....|....*....|....*....|....
gi 150247226 186 FSDSLRRELSYFGVKVAMIEPGYFKTA-VTSKER 218
Cdd:PRK05876 166 LAETLAREVTADGIGVSVLCPMVVETNlVANSER 199
PRK06953 PRK06953
SDR family oxidoreductase;
30-211 1.87e-12

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 65.48  E-value: 1.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSdrlETVTLDVTKTESVAAAAqwvkecvrdkglWGL 109
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQALGA---EALALDVADPASVAGLA------------WKL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 110 --------VNNAGISLP-TAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRV----SLFGGGY 176
Cdd:PRK06953  67 dgealdaaVYVAGVYGPrTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSRMGSIgdatGTTGWLY 146

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 150247226 177 CISKygvEAFSDSLR-RELSYFGVKVAMIEPGYFKT 211
Cdd:PRK06953 147 RASK---AALNDALRaASLQARHATCIALHPGWVRT 179
PRK07023 PRK07023
SDR family oxidoreductase;
34-219 1.97e-12

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 65.80  E-value: 1.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  34 ITGCDSGFGKLLARQLDARGLRVLaaCLTEKGAEQLRGQTSDRLETVTLDVTKTesvAAAAQWV-----KECVRDKGLWG 108
Cdd:PRK07023   6 VTGHSRGLGAALAEQLLQPGIAVL--GVARSRHPSLAAAAGERLAEVELDLSDA---AAAAAWLagdllAAFVDGASRVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 109 LVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRR-ARGRVVNVSSVMGRVSLFG-GGYCISKYGVEAF 186
Cdd:PRK07023  81 LINNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDaAERRILHISSGAARNAYAGwSVYCATKAALDHH 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 150247226 187 SDSLRRELSYfGVKVAMIEPGYFKTAV------TSKERF 219
Cdd:PRK07023 161 ARAVALDANR-ALRIVSLAPGVVDTGMqatiraTDEERF 198
PRK06947 PRK06947
SDR family oxidoreductase;
30-213 3.26e-12

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 65.21  E-value: 3.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRV--------LAACLTEKGAEQLRGqtsdRLETVTLDVTKTESVAAAAQWVKEcv 101
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVginyardaAAAEETADAVRAAGG----RACVVAGDVANEADVIAMFDAVQS-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 102 RDKGLWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR----GRVVNVSSVMGRVslfgGG-- 175
Cdd:PRK06947  77 AFGRLDALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRggrgGAIVNVSSIASRL----GSpn 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 150247226 176 ----YCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAV 213
Cdd:PRK06947 153 eyvdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEI 194
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 27-212 3.95e-12

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 65.17  E-value: 3.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLT-EKGAEQLR-----GQTSDRLETvtlDVTKTESVAAAAQwvkEC 100
Cdd:cd08935    3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNqEKGDKVAKeitalGGRAIALAA---DVLDRASLERARE---EI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 101 VRDkglWG----LVNNAGISLP--TAPNEL-----------LTKQDFVTILDVNLLGvidvtlSLLP-------LVRRAR 156
Cdd:cd08935   77 VAQ---FGtvdiLINGAGGNHPdaTTDPEHyepeteqnffdLDEEGWEFVFDLNLNG------SFLPsqvfgkdMLEQKG 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150247226 157 GRVVNVSSV-----MGRVSlfggGYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTA 212
Cdd:cd08935  148 GSIINISSMnafspLTKVP----AYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTP 204
PRK08628 PRK08628
SDR family oxidoreductase;
26-206 5.25e-12

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 64.98  E-value: 5.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  26 HLRDKYVFITGCDSGFGKLLARQLDARG-LRVLAACLTEKG--AEQLRgQTSDRLETVTLDVTKTESVAAAaqwVKECVR 102
Cdd:PRK08628   4 NLKDKVVIVTGGASGIGAAISLRLAEEGaIPVIFGRSAPDDefAEELR-ALQPRAEFVQVDLTDDAQCRDA---VEQTVA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 DKG-LWGLVNNAG----ISLPTapnellTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSvmgRVSLFG---- 173
Cdd:PRK08628  80 KFGrIDGLVNNAGvndgVGLEA------GREAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISS---KTALTGqggt 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 150247226 174 GGYCISKYGVEAFSDSLRRELSYFGVKVAMIEP 206
Cdd:PRK08628 151 SGYAAAKGAQLALTREWAVALAKDGVRVNAVIP 183
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 27-225 6.51e-12

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: 64.39  E-value: 6.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDR---LETVTLDVTKTESVAAAAQWVkECVRD 103
Cdd:cd05329    4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKgfkVEGSVCDVSSRSERQELMDTV-ASHFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 KGLWGLVNNAGISLPTaPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRR-ARGRVVNVSSVMGRVSL-FGGGYCISKY 181
Cdd:cd05329   83 GKLNILVNNAGTNIRK-EAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKAsGNGNIVFISSVAGVIAVpSGAPYGATKG 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 150247226 182 GVEAFSDSLRRELSYFGVKVAMIEPGYFKT----AVTSKERFLKSFLE 225
Cdd:cd05329  162 ALNQLTRSLACEWAKDNIRVNAVAPWVIATplvePVIQQKENLDKVIE 209
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 29-207 7.65e-12

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 64.29  E-value: 7.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  29 DKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTS-----DRLETVTLDVTKTESVAAAAQWVKECVRD 103
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINaeygeGMAYGFGADATSEQSVLALSRGVDEIFGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 KGLwgLVNNAGIsLPTAPNELLTKQDFVTILDVNLLG--VIDVTLSLLPLVRRARGRVVNVSSVMGRV-SLFGGGYCISK 180
Cdd:PRK12384  82 VDL--LVYNAGI-AKAAFITDFQLGDFDRSLQVNLVGyfLCAREFSRLMIRDGIQGRIIQINSKSGKVgSKHNSGYSAAK 158

                        170       180
                 ....*....|....*....|....*..
gi 150247226 181 YGVEAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:PRK12384 159 FGGVGLTQSLALDLAEYGITVHSLMLG 185
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 27-214 7.91e-12

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: 64.04  E-value: 7.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTL--DVTKTESVAAAAQWVKEcvRDK 104
Cdd:cd08942    4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYGECIAIpaDLSSEEGIEALVARVAE--RSD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 GLWGLVNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-----GRVVNVSSVMGRV--SLFGGGYC 177
Cdd:cd08942   82 RLDVLVNNAGATW-GAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAAtaenpARVINIGSIAGIVvsGLENYSYG 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 150247226 178 ISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVT 214
Cdd:cd08942  161 ASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMT 197
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 27-216 1.44e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 63.43  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLaacLTEKGAEQLRgQTSDRLE-------TVTLDVTKTESVAAAAQWVKE 99
Cdd:PRK08213  10 LSGKTALVTGGSRGLGLQIAEALGEAGARVV---LSARKAEELE-EAAAHLEalgidalWIAADVADEADIERLAEETLE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 100 cvRDKGLWGLVNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVT-----LSLLPlvrRARGRVVNVSSVMGrvsLFGG 174
Cdd:PRK08213  86 --RFGHVDILVNNAGATW-GAPAEDHPVEAWDKVMNLNVRGLFLLSqavakRSMIP---RGYGRIINVASVAG---LGGN 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 150247226 175 --------GYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSK 216
Cdd:PRK08213 157 ppevmdtiAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRG 206
PRK06139 PRK06139
SDR family oxidoreductase;
27-211 1.59e-11

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 63.97  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLR-VLAACLTE---KGAEQLRGQTSDRLeTVTLDVTKTESVAAAAQWVKECVR 102
Cdd:PRK06139   5 LHGAVVVITGASSGIGQATAEAFARRGARlVLAARDEEalqAVAEECRALGAEVL-VVPTDVTDADQVKALATQAASFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 DKGLWglVNNAGI-------SLPTAPNElltkqdfvTILDVNLLGVIDVTLSLLPL-VRRARGRVVNVSSVMGRVSL-FG 173
Cdd:PRK06139  84 RIDVW--VNNVGVgavgrfeETPIEAHE--------QVIQTNLIGYMRDAHAALPIfKKQGHGIFINMISLGGFAAQpYA 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 150247226 174 GGYCISKYGVEAFSDSLRRELSYF-GVKVAMIEPGYFKT 211
Cdd:PRK06139 154 AAYSASKFGLRGFSEALRGELADHpDIHVCDVYPAFMDT 192
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-219 1.84e-11

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 63.18  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACL-TEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVrDKG 105
Cdd:PRK08642   3 ISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHqSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEHF-GKP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LWGLVNNA-------GISLPTAPNelLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSvmgrvSLFGG--- 174
Cdd:PRK08642  82 ITTVVNNAladfsfdGDARKKADD--ITWEDFQQQLEGSVKGALNTIQAALPGMREQGfGRIINIGT-----NLFQNpvv 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 150247226 175 ---GYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT----AVTSKERF 219
Cdd:PRK08642 155 pyhDYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTtdasAATPDEVF 206
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 27-196 2.53e-11

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 63.05  E-value: 2.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAaqwVKECVRDKG- 105
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRA---VDQTVDAFGk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LWGLVNNAGI-----SLPTAPNELLTKQdFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRVSlfGGG---YC 177
Cdd:PRK06200  81 LDCFVGNAGIwdyntSLVDIPAETLDTA-FDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLSNSSFYP--GGGgplYT 157

                        170
                 ....*....|....*....
gi 150247226 178 ISKYGVEAfsdsLRRELSY 196
Cdd:PRK06200 158 ASKHAVVG----LVRQLAY 172
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 27-212 2.77e-11

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 62.58  E-value: 2.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLaacltekgaeqLRGQTSDRLETV---------------TLD---VTKTE 88
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVI-----------LLGRTEEKLEAVydeieaaggpqpaiiPLDlltATPQN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  89 SVAAAAQWVKECVRdkgLWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMG 167
Cdd:PRK08945  79 YQQLADTIEEQFGR---LDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPaASLVFTSSSVG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 150247226 168 RVS-LFGGGYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTA 212
Cdd:PRK08945 156 RQGrANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTA 201
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 30-225 2.87e-11

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


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 62.49  E-value: 2.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGqtSDRLETVTLDVTKTESVAAAAQwvkecvRDKGLWGL 109
Cdd:cd05368    3 KVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELER--GPGITTRVLDVTDKEQVAALAK------EEGRIDVL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 110 VNNAGIsLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFGG--GYCISKYGVEAF 186
Cdd:cd05368   75 FNCAGF-VHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPkMLARKDGSIINMSSVASSIKGVPNrfVYSTTKAAVIGL 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 150247226 187 SDSLRRELSYFGVKVAMIEPGYFKT--------AVTSKERFLKSFLE 225
Cdd:cd05368  154 TKSVAADFAQQGIRCNAICPGTVDTpsleeriqAQPDPEEALKAFAA 200
PRK06138 PRK06138
SDR family oxidoreductase;
26-211 3.99e-11

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 62.09  E-value: 3.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  26 HLRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSD--RLETVTLDVTKTESVAAAAQWVkecvrd 103
Cdd:PRK06138   2 RLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAggRAFARQGDVGSAEAVEALVDFV------ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 KGLWG----LVNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSLFG-GGYC 177
Cdd:PRK06138  76 AARWGrldvLVNNAGFGC-GGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGgGSIVNTASQLALAGGRGrAAYV 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 150247226 178 ISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK06138 155 ASKGAIASLTRAMALDHATDGIRVNAVAPGTIDT 188
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 30-219 5.85e-11

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: 61.70  E-value: 5.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACL-TEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVRDKGLwg 108
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYrSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDT-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 109 LVNNAGISLPTAPN-----ELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSvmgrvSLFGGG------Y 176
Cdd:cd05349   79 IVNNALIDFPFDPDqrktfDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGsGRVINIGT-----NLFQNPvvpyhdY 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 150247226 177 CISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT----AVTSKERF 219
Cdd:cd05349  154 TTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKVtdasAATPKEVF 200
PRK12743 PRK12743
SDR family oxidoreductase;
34-217 6.11e-11

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 61.59  E-value: 6.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  34 ITGCDSGFGKLLARQLDARGLRVlaaCLT----EKGA----EQLRGQtSDRLETVTLDVTKTESVAAAAQWVKEcvRDKG 105
Cdd:PRK12743   7 VTASDSGIGKACALLLAQQGFDI---GITwhsdEEGAketaEEVRSH-GVRAEIRQLDLSDLPEGAQALDKLIQ--RLGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LWGLVNNAGislpTAPNELLTKQDFVT---ILDVNLLGVidvtlsLLPLVRRAR--------GRVVNVSSVMGRVSLFGG 174
Cdd:PRK12743  81 IDVLVNNAG----AMTKAPFLDMDFDEwrkIFTVDVDGA------FLCSQIAARhmvkqgqgGRIINITSVHEHTPLPGA 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 150247226 175 G-YCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKE 217
Cdd:PRK12743 151 SaYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIATPMNGMD 194
PRK08251 PRK08251
SDR family oxidoreductase;
28-216 6.55e-11

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 61.49  E-value: 6.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  28 RDKYVFITGCDSGFGKLLARQLDARGlRVLAAC------LTEKGAEQLRGQTSDRLETVTLDVTKTESVAAaaqwVKECV 101
Cdd:PRK08251   1 TRQKILITGASSGLGAGMAREFAAKG-RDLALCarrtdrLEELKAELLARYPGIKVAVAALDVNDHDQVFE----VFAEF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 102 RDK--GLWGLVNNAGI----SLPTAPNELlTKQDFVTILdVNLLGVIDVTLSLLPlvRRARGRVVNVSSVMGRVSLFG-- 173
Cdd:PRK08251  76 RDElgGLDRVIVNAGIgkgaRLGTGKFWA-NKATAETNF-VAALAQCEAAMEIFR--EQGSGHLVLISSVSAVRGLPGvk 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 150247226 174 GGYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSK 216
Cdd:PRK08251 152 AAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNAK 194
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 32-167 8.22e-11

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: 61.36  E-value: 8.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRVLAACLTEkgAEqlrgqtsdrletVTLDVTKTESVAAA-AQWVKECvrDKGLWGLV 110
Cdd:cd05328    2 IVITGAASGIGAATAELLEDAGHTVIGIDLRE--AD------------VIADLSTPEGRAAAiADVLARC--SGVLDGLV 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 150247226 111 NNAGISlPTAPNELltkqdfvtILDVNLLGVIDVTLSLLPLVRRARG-RVVNVSSVMG 167
Cdd:cd05328   66 NCAGVG-GTTVAGL--------VLKVNYFGLRALMEALLPRLRKGHGpAAVVVSSIAG 114
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 30-206 8.49e-11

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: 61.25  E-value: 8.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTS--DRLETVTLDVTKTESVAAAAQwvKECVRDKGLW 107
Cdd:cd08943    2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQggPRALGVQCDVTSEAQVQSAFE--QAVLEFGGLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 108 GLVNNAGISLPtAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR--GRVVNVSSvmgRVSLFGG----GYCISKy 181
Cdd:cd08943   80 IVVSNAGIATS-SPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGigGNIVFNAS---KNAVAPGpnaaAYSAAK- 154

                        170       180
                 ....*....|....*....|....*....
gi 150247226 182 gveAFSDSLRR----ELSYFGVKVAMIEP 206
Cdd:cd08943  155 ---AAEAHLARclalEGGEDGIRVNTVNP 180
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 27-207 1.06e-10

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: 61.00  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQL--RGQTSDRLETVTLDVtktESVAAAAQWVKECVRDK 104
Cdd:cd08937    2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLaeILAAGDAAHVHTADL---ETYAGAQGVVRAAVERF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 G-LWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRvSLFGGGYCISKYG 182
Cdd:cd08937   79 GrVDVLINNVGGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPhMLERQQGVIVNVSSIATR-GIYRIPYSAAKGG 157

                        170       180
                 ....*....|....*....|....*
gi 150247226 183 VEAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:cd08937  158 VNALTASLAFEHARDGIRVNAVAPG 182
PRK07577 PRK07577
SDR family oxidoreductase;
27-211 1.55e-10

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 60.13  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAacLTEKGAEQLRGQtsdrLETVTL-DVTKTESVAAaaqwvkECVRDKG 105
Cdd:PRK07577   1 MSSRTVLVTGATKGIGLALSLRLANLGHQVIG--IARSAIDDFPGE----LFACDLaDIEQTAATLA------QINEIHP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LWGLVNNAGISLPtAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSvmgrVSLFGG----GYCISK 180
Cdd:PRK07577  69 VDAIVNNVGIALP-QPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREqGRIVNICS----RAIFGAldrtSYSAAK 143

                        170       180       190
                 ....*....|....*....|....*....|.
gi 150247226 181 YGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK07577 144 SALVGCTRTWALELAEYGITVNAVAPGPIET 174
PRK05854 PRK05854
SDR family oxidoreductase;
27-168 2.05e-10

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 60.85  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQ----LRGQTSD-RLETVTLDVTKTESVAAAAQWVKECV 101
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAavaaIRTAVPDaKLSLRALDLSSLASVAALGEQLRAEG 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150247226 102 RDKGLwgLVNNAGISLPtaPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGR 168
Cdd:PRK05854  92 RPIHL--LINNAGVMTP--PERQTTADGFELQFGTNHLGHFALTAHLLPLLRAGRARVTSQSSIAAR 154
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 27-218 2.58e-10

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 60.08  E-value: 2.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRV----LAACLTEKGAEQLRGQTSDRLETVtLDVTKTESVAAAaqwVKECVR 102
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIvfndINQELVDKGLAAYRELGIEAHGYV-CDVTDEDGVQAM---VSQIEK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 DKGLWG-LVNNAGIsLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVM---GRVSLfgGGYC 177
Cdd:PRK07097  84 EVGVIDiLVNNAGI-IKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPsMIKKGHGKIINICSMMselGRETV--SAYA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 150247226 178 ISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKER 218
Cdd:PRK07097 161 AAKGGLKMLTKNIASEYGEANIQCNGIGPGYIATPQTAPLR 201
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 27-219 3.25e-10

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 59.74  E-value: 3.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLT-EKGAEQLRG---QTSDRLETVTLDVTKTESVAAAaqwVKECVR 102
Cdd:PRK08936   5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSdEEEANDVAEeikKAGGEAIAVKGDVTVESDVVNL---IQTAVK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 DKG-LWGLVNNAGISLPTAPNElLTKQDFVTILDVNLLGVIDVTLSLLP--LVRRARGRVVNVSSVMGRV--SLFgGGYC 177
Cdd:PRK08936  82 EFGtLDVMINNAGIENAVPSHE-MSLEDWNKVINTNLTGAFLGSREAIKyfVEHDIKGNIINMSSVHEQIpwPLF-VHYA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 150247226 178 ISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSkERF 219
Cdd:PRK08936 160 ASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINA-EKF 200
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 32-216 3.26e-10

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


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 59.29  E-value: 3.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRV-------------LAACLTEKGAeqlrgqtsdRLETVTLDVTKTESVAAAAQWVK 98
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVvinyrkskdaaaeVAAEIEELGG---------KAVVVRADVSQPQDVEEMFAAVK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  99 EcvRDKGLWGLVNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSV-MGRVSLFGGGY 176
Cdd:cd05359   72 E--RFGRLDVLVSNAAAGAFRPLSEL-TPAHWDAKMNTNLKALVHCAQQAAKLMRERGgGRIVAISSLgSIRALPNYLAV 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 150247226 177 CISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSK 216
Cdd:cd05359  149 GTAKAALEALVRYLAVELGPRGIRVNAVSPGVIDTDALAH 188
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
32-209 3.92e-10

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 59.61  E-value: 3.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCdSGF-GKLLARQLDARGLRVLAACLTEKGAEQLRGQtsDRLETVTLDVTKTESVAAAAQWVkECVrdkglwglV 110
Cdd:COG0451    2 ILVTGG-AGFiGSHLARRLLARGHEVVGLDRSPPGAANLAAL--PGVEFVRGDLRDPEALAAALAGV-DAV--------V 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 111 NNAGISLPTApnelltkQDFVTILDVNLLGvidvTLSLLPLVRRAR-GRVVNVSS--VMGRVSLF---------GGGYCI 178
Cdd:COG0451   70 HLAAPAGVGE-------EDPDETLEVNVEG----TLNLLEAARAAGvKRFVYASSssVYGDGEGPidedtplrpVSPYGA 138

                        170       180       190
                 ....*....|....*....|....*....|.
gi 150247226 179 SKYGVEAFSDSLRRElsyFGVKVAMIEPGYF 209
Cdd:COG0451  139 SKLAAELLARAYARR---YGLPVTILRPGNV 166
PRK06398 PRK06398
aldose dehydrogenase; Validated
 27-183 4.17e-10

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 59.08  E-value: 4.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQlrgqtSDRLEtvtLDVTKTESVAAAAQWV-KECVRdkg 105
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYND-----VDYFK---VDVSNKEQVIKGIDYViSKYGR--- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LWGLVNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGR-VSLFGGGYCISKYGV 183
Cdd:PRK06398  73 IDILVNNAGIES-YGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDkGVIINIASVQSFaVTRNAAAYVTSKHAV 151
PRK07069 PRK07069
short chain dehydrogenase; Validated
 33-213 5.58e-10

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 58.95  E-value: 5.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  33 FITGCDSGFGKLLARQLDARGLRVLaacLTEKGAEQLRGQTSDRLET---------VTLDVTKTESVAAAAQWVKECVRd 103
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVF---LTDINDAAGLDAFAAEINAahgegvafaAVQDVTDEAQWQALLAQAADAMG- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 kGLWGLVNNAGISLPTAPnELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMG-RVSLFGGGYCISKY 181
Cdd:PRK07069  79 -GLSVLVNNAGVGSFGAI-EQIELDEWRRVMAINVESIFLGCKHALPYLRASQpASIVNISSVAAfKAEPDYTAYNASKA 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 150247226 182 GVEAFSDSL-----RRELsyfGVKVAMIEPGYFKTAV 213
Cdd:PRK07069 157 AVASLTKSIaldcaRRGL---DVRCNSIHPTFIRTGI 190
PRK07102 PRK07102
SDR family oxidoreductase;
30-214 5.74e-10

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 58.78  E-value: 5.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRV-LAACLTEK---GAEQLRGQTSDRLETVTLDVTKTESVAAAAQwvkecvrdkG 105
Cdd:PRK07102   2 KKILIIGATSDIARACARRYAAAGARLyLAARDVERlerLADDLRARGAVAVSTHELDILDTASHAAFLD---------S 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LWGLVNNAGISLPTAPNELLTKQDF---VTILDVNLLGVIdvtlSLLPLV-----RRARGRVVNVSSVM---GRVS--LF 172
Cdd:PRK07102  73 LPALPDIVLIAVGTLGDQAACEADPalaLREFRTNFEGPI----ALLTLLanrfeARGSGTIVGISSVAgdrGRASnyVY 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 150247226 173 GGGycisKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVT 214
Cdd:PRK07102 149 GSA----KAALTAFLSGLRNRLFKSGVHVLTVKPGFVRTPMT 186
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 27-221 6.58e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 58.59  E-value: 6.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKG----AEQLRGqtsdrlETVTLDVTKTESVAAAAQWVKEcvr 102
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAgkaaADEVGG------LFVPTDVTDEDAVNALFDTAAE--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 dkgLWGLV----NNAGISLPTAPNELLTKQD-FVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSS---VMG----RV 169
Cdd:PRK06057  76 ---TYGSVdiafNNAGISPPEDDSILNTGLDaWQRVQDVNLTSVYLCCKAALPhMVRQGKGSIINTASfvaVMGsatsQI 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 150247226 170 SlfgggYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTsKERFLK 221
Cdd:PRK06057 153 S-----YTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLL-QELFAK 198
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 30-224 6.90e-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: 58.94  E-value: 6.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFG-----KLLARQLDARGLRVLAACLTEKGAEQLRGQTSD-------RLETVTLDVTKTESVAAAAQWV 97
Cdd:cd08941    2 KVVLVTGANSGLGlaiceRLLAEDDENPELTLILACRNLQRAEAACRALLAshpdarvVFDYVLVDLSNMVSVFAAAKEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  98 KEcvRDKGLWGLVNNAGI--------------------------SLPTAPNELLTKQDFVT------ILDVNLLGVIDVT 145
Cdd:cd08941   82 KK--RYPRLDYLYLNAGImpnpgidwigaikevltnplfavtnpTYKIQAEGLLSQGDKATedglgeVFQTNVFGHYYLI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 146 LSLLPLVRRAR--GRVVNVSSVMGRVSLFG----------GGYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAV 213
Cdd:cd08941  160 RELEPLLCRSDggSQIIWTSSLNASPKYFSlediqhlkgpAPYSSSKYLVDLLSLALNRKFNKLGVYSYVVHPGICTTNL 239

                        250
                 ....*....|.
gi 150247226 214 TSKerFLKSFL 224
Cdd:cd08941  240 TYG--ILPPFT 248
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 24-211 8.90e-10

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 58.24  E-value: 8.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  24 LSHLRDKYVFITGCDSGFGKLLARQLDARGLRVL-----AACLtEKGAEQLRGQTSDrLETVTLDVTKTESVAAAAQWVK 98
Cdd:PRK07523   5 LFDLTGRRALVTGSSQGIGYALAEGLAQAGAEVIlngrdPAKL-AAAAESLKGQGLS-AHALAFDVTDHDAVRAAIDAFE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  99 EcvrDKG-LWGLVNNAGISLPTaPNELLTKQDFVTILDVNLLGVIDVTLSLL-PLVRRARGRVVNVSSV---MGRVSLfg 173
Cdd:PRK07523  83 A---EIGpIDILVNNAGMQFRT-PLEDFPADAFERLLRTNISSVFYVGQAVArHMIARGAGKIINIASVqsaLARPGI-- 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 150247226 174 GGYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK07523 157 APYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDT 194
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 32-217 1.22e-09

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 56.76  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGL-RVLAacltekgaeqlrgqtsdrleTVTLDVtktesvaaaaqwvkecvrdkglwgLV 110
Cdd:cd02266    1 VLVTGGSGGIGGAIARWLASRGSpKVLV--------------------VSRRDV------------------------VV 36

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 111 NNAGISLPTaPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSL-FGGGYCISKYGVEAFSD 188
Cdd:cd02266   37 HNAAILDDG-RLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRlGRFILISSVAGLFGApGLGGYAASKAALDGLAQ 115

                        170       180
                 ....*....|....*....|....*....
gi 150247226 189 SLRRELSYFGVKVAMIEPGYFKTAVTSKE 217
Cdd:cd02266  116 QWASEGWGNGLPATAVACGTWAGSGMAKG 144
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 27-211 1.28e-09

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 57.99  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLT-EKG---AEQLRGQTSDRLeTVTLDVTKTESVAAAAQWVKEcvr 102
Cdd:PRK08277   8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNqEKAeavVAEIKAAGGEAL-AVKADVLDKESLEQARQQILE--- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 dkgLWG----LVNNAGISLP--TAPNEL------------LTKQDFVTILDVNLLGvidvtlSLLP-------LVRRARG 157
Cdd:PRK08277  84 ---DFGpcdiLINGAGGNHPkaTTDNEFhelieptktffdLDEEGFEFVFDLNLLG------TLLPtqvfakdMVGRKGG 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 150247226 158 RVVNVSSV-----MGRVSlfggGYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK08277 155 NIINISSMnaftpLTKVP----AYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLT 209
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 34-216 2.01e-09

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: 57.09  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  34 ITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLET----VTLDVTKTESVAAAAQWVKEcvRDKGLWGL 109
Cdd:cd05337    6 VTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAGRraiyFQADIGELSDHEALLDQAWE--DFGRLDCL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 110 VNNAGISLPTAPNEL-LTKQDFVTILDVNLLGVIDVT-------LSLLPLVRRARGRVVNVSSV-MGRVSLFGGGYCISK 180
Cdd:cd05337   84 VNNAGIAVRPRGDLLdLTEDSFDRLIAINLRGPFFLTqavarrmVEQPDRFDGPHRSIIFVTSInAYLVSPNRGEYCISK 163

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 150247226 181 YGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSK 216
Cdd:cd05337  164 AGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAP 199
PRK12746 PRK12746
SDR family oxidoreductase;
24-216 2.06e-09

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 57.35  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  24 LSHLRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGA--EQLRGQTSD--RLETVTLDVTKTESVAAAAQWVKE 99
Cdd:PRK12746   1 MKNLDGKVALVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAadETIREIESNggKAFLIEADLNSIDGVKKLVEQLKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 100 CVRDK----GLWGLVNNAGISlPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRrARGRVVNVSSVMGRVSLFGG- 174
Cdd:PRK12746  81 ELQIRvgtsEIDILVNNAGIG-TQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLR-AEGRVINISSAEVRLGFTGSi 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 150247226 175 GYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSK 216
Cdd:PRK12746 159 AYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAK 200
PRK09135 PRK09135
pteridine reductase; Provisional
 29-207 3.87e-09

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 56.09  E-value: 3.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  29 DKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTsdrletvtLDVTKTESVA----------AAAQWVK 98
Cdd:PRK09135   6 AKVALITGGARRIGAAIARTLHAAGYRVAIHYHRSAAEADALAAE--------LNALRPGSAAalqadlldpdALPELVA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  99 ECVRDKG-LWGLVNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSV-----MGRVSLf 172
Cdd:PRK09135  78 ACVAAFGrLDALVNNASSFYPTPLGSI-TEAQWDDLFASNLKAPFFLSQAAAPQLRKQRGAIVNITDIhaerpLKGYPV- 155

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 150247226 173 gggYCISKYGVEAFSDSLRRELSYfGVKVAMIEPG 207
Cdd:PRK09135 156 ---YCAAKAALEMLTRSLALELAP-EVRVNAVAPG 186
PRK08177 PRK08177
SDR family oxidoreductase;
30-211 4.02e-09

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 55.81  E-value: 4.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLEtvTLDVTKTESVAAAAQWVKECVRDKglwgL 109
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIE--KLDMNDPASLDQLLQRLQGQRFDL----L 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 110 VNNAGISLPtAPNELLT------KQDFVTildvNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRVSLFGGG----YCIS 179
Cdd:PRK08177  76 FVNAGISGP-AHQSAADataaeiGQLFLT----NAIAPIRLARRLLGQVRPGQGVLAFMSSQLGSVELPDGGemplYKAS 150

                        170       180       190
                 ....*....|....*....|....*....|..
gi 150247226 180 KYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK08177 151 KAALNSMTRSFVAELGEPTLTVLSMHPGWVKT 182
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 26-207 4.12e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 56.21  E-value: 4.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  26 HLRDKYVFITGCDSGFGKLLARQLDARGLRV-LAACLTEK---GAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECv 101
Cdd:PRK06125   4 HLAGKRVLITGASKGIGAAAAEAFAAEGCHLhLVARDADAleaLAADLRAAHGVDVAVHALDLSSPEAREQLAAEAGDI- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 102 rDKglwgLVNNAGiSLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVR-RARGRVVNVSSVMGRVslFGGGYCISK 180
Cdd:PRK06125  83 -DI----LVNNAG-AIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKaRGSGVIVNVIGAAGEN--PDADYICGS 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 150247226 181 YG---VEAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:PRK06125 155 AGnaaLMAFTRALGGKSLDDGVRVVGVNPG 184
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 32-174 4.80e-09

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: 56.37  E-value: 4.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGL-RVLAACLTEKGAEQLR---GQTSDRLETVTLDVTKTESVaaaaqwvKECVRD---- 103
Cdd:cd09810    4 VVITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAqevGMPKDSYSVLHCDLASLDSV-------RQFVDNfrrt 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150247226 104 -KGLWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARG---RVVNVSSVMGRVSLFGG 174
Cdd:cd09810   77 gRPLDALVCNAAVYLPTAKEPRFTADGFELTVGVNHLGHFLLTNLLLEDLQRSENaspRIVIVGSITHNPNTLAG 151
PRK07814 PRK07814
SDR family oxidoreductase;
27-180 7.87e-09

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 55.56  E-value: 7.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSD---RLETVTLDVTKTESVAA-AAQWVKECVR 102
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAagrRAHVVAADLAHPEATAGlAGQAVEAFGR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 dkgLWGLVNNAGislPTAPNELL--TKQDFVTILDVNLLGVIDVTLSLLPLVRR--ARGRVVNVSSVMGRVSLFG-GGYC 177
Cdd:PRK07814  88 ---LDIVVNNVG---GTMPNPLLstSTKDLADAFTFNVATAHALTVAAVPLMLEhsGGGSVINISSTMGRLAGRGfAAYG 161


                 ...
gi 150247226 178 ISK 180
Cdd:PRK07814 162 TAK 164
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 29-207 8.96e-09

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


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 55.03  E-value: 8.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  29 DKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQ----LRGQTSDRLETVTLDVTKTESVAAAAQWVKEcvRDK 104
Cdd:cd08930    2 DKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQlkeeLTNLYKNRVIALELDITSKESIKELIESYLE--KFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 GLWGLVNNAGIS--LPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLV-RRARGRVVNVSSVMGRVS----LFGGG-- 175
Cdd:cd08930   80 RIDILINNAYPSpkVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFkKQGKGSIINIASIYGVIApdfrIYENTqm 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 150247226 176 -----YCISKYGVEAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:cd08930  160 yspveYSVIKAGIIHLTKYLAKYYADTGIRVNAISPG 196
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 27-207 9.32e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 55.42  E-value: 9.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGK----LLARQldarGLRVLAACLTEKGAEQlrgQTSDRLE-------TVTLDVtKTESVAAAAq 95
Cdd:PRK06701  44 LKGKVALITGGDSGIGRavavLFAKE----GADIAIVYLDEHEDAN---ETKQRVEkegvkclLIPGDV-SDEAFCKDA- 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  96 wVKECVRDKG-LWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRArGRVVNVSSVMGrvsLFGG 174
Cdd:PRK06701 115 -VEETVRELGrLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLKQG-SAIINTGSITG---YEGN 189

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 150247226 175 G----YCISKYGVEAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:PRK06701 190 EtlidYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPG 226
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 27-208 1.04e-08

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 55.01  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKEcvRDKGL 106
Cdd:PRK08265   4 LAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVA--RFGRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 107 WGLVNNAGISLPtaPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRVSLFGGG-YCISKYGVEA 185
Cdd:PRK08265  82 DILVNLACTYLD--DGLASSRADWLAALDVNLVSAAMLAQAAHPHLARGGGAIVNFTSISAKFAQTGRWlYPASKAAIRQ 159

                        170       180
                 ....*....|....*....|...
gi 150247226 186 FSDSLRRELSYFGVKVAMIEPGY 208
Cdd:PRK08265 160 LTRSMAMDLAPDGIRVNSVSPGW 182
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 33-216 1.50e-08

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 54.58  E-value: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  33 FITGCDSGFGKLLARQLDARGLRVLAACLTEkgAEQLRGqTSDRLET-------VTLDVTKTES----VAAAAQWvkecv 101
Cdd:PRK12745   6 LVTGGRRGIGLGIARALAAAGFDLAINDRPD--DEELAA-TQQELRAlgvevifFPADVADLSAheamLDAAQAA----- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 102 rdkglWG----LVNNAGISlPTAPNELL--TKQDFVTILDVNLLGVIDVT------LSLLPLVRRARGR-VVNVSSV-MG 167
Cdd:PRK12745  78 -----WGridcLVNNAGVG-VKVRGDLLdlTPESFDRVLAINLRGPFFLTqavakrMLAQPEPEELPHRsIVFVSSVnAI 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 150247226 168 RVSLFGGGYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSK 216
Cdd:PRK12745 152 MVSPNRGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAP 200
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 30-209 1.52e-08

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


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 54.78  E-value: 1.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACL----TEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVRDKG 105
Cdd:cd05322    3 QVAVVIGGGQTLGEFLCHGLAEAGYDVAVADInsenAEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKRVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LwgLVNNAGISlPTAPNELLTKQDFVTILDVNLLG--VIDVTLSLLPLVRRARGRVVNVSSVMGRV-SLFGGGYCISKYG 182
Cdd:cd05322   83 L--LVYSAGIA-KSAKITDFELGDFDRSLQVNLVGyfLCAREFSKLMIRDGIQGRIIQINSKSGKVgSKHNSGYSAAKFG 159

                        170       180
                 ....*....|....*....|....*..
gi 150247226 183 VEAFSDSLRRELSYFGVKVAMIEPGYF 209
Cdd:cd05322  160 GVGLTQSLALDLAEHGITVNSLMLGNL 186
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 27-207 1.62e-08

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 54.55  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKEcvRDKGL 106
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVD--RWGSI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 107 WGLVNNAGIsLPTAPNELLTKQDFVTILDVNLLGvidvTLSLLPLVRRAR------GRVVNVSSVMGRV-SLFGGGYCIS 179
Cdd:cd05363   79 DILVNNAAL-FDLAPIVDITRESYDRLFAINVSG----TLFMMQAVARAMiaqgrgGKIINMASQAGRRgEALVGVYCAT 153

                        170       180
                 ....*....|....*....|....*...
gi 150247226 180 KYGVEAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:cd05363  154 KAAVISLTQSAGLNLIRHGINVNAIAPG 181
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-216 1.71e-08

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 55.23  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLaaCLTEKGAEQLRGQTSDRL--ETVTLDVTKTESVAAAAQWVKEcvRDK 104
Cdd:PRK08261 208 LAGKVALVTGAARGIGAAIAEVLARDGAHVV--CLDVPAAGEALAAVANRVggTALALDITAPDAPARIAEHLAE--RHG 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 GLWGLVNNAGISlptaPNELLTKQD---FVTILDVNLLGVIDVTLSLL-PLVRRARGRVVNVSSVMGRVSLFG-GGYCIS 179
Cdd:PRK08261 284 GLDIVVHNAGIT----RDKTLANMDearWDSVLAVNLLAPLRITEALLaAGALGDGGRIVGVSSISGIAGNRGqTNYAAS 359

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 150247226 180 KYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSK 216
Cdd:PRK08261 360 KAGVIGLVQALAPLLAERGITINAVAPGFIETQMTAA 396
PRK07062 PRK07062
SDR family oxidoreductase;
27-168 1.91e-08

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 54.28  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVlAACLTE----KGAE-QLRGQTSD-RLETVTLDVTKTESVAAAAQWVKEc 100
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASV-AICGRDeerlASAEaRLREKFPGaRLLAARCDVLDEADVAAFAAAVEA- 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150247226 101 vRDKGLWGLVNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRA-RGRVVNVSSVMGR 168
Cdd:PRK07062  84 -RFGGVDMLVNNAGQGR-VSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASaAASIVCVNSLLAL 150
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 32-211 2.64e-08

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


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 53.29  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRVLaacLTEKGAEQLRGQTSDRLE-TVTLDVTKTESVAAAAQwvkecvRDKGLWGLV 110
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLL---LSGRDAGALAGLAAEVGAlARPADVAAELEVWALAQ------ELGPLDLLV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 111 NNAGISLPtAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVrRARGRVVNVSSVMGRVSLFG-GGYCISKYGVEAFSDS 189
Cdd:cd11730   72 YAAGAILG-KPLARTKPAAWRRILDANLTGAALVLKHALALL-AAGARLVFLGAYPELVMLPGlSAYAAAKAALEAYVEV 149

                        170       180
                 ....*....|....*....|..
gi 150247226 190 LRRELSyfGVKVAMIEPGYFKT 211
Cdd:cd11730  150 ARKEVR--GLRLTLVRPPAVDT 169
PRK06500 PRK06500
SDR family oxidoreductase;
24-207 3.67e-08

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 53.42  E-value: 3.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  24 LSHLRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECvrd 103
Cdd:PRK06500   1 MSRLQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAAQKALAQALAEA--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 kglWGLVN----NAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNvSSVMGRVSLFGGG-YCI 178
Cdd:PRK06500  78 ---FGRLDavfiNAGVAK-FAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPASIVLN-GSINAHIGMPNSSvYAA 152

                        170       180
                 ....*....|....*....|....*....
gi 150247226 179 SKYGVEAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:PRK06500 153 SKAALLSLAKTLSGELLPRGIRVNAVSPG 181
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 27-207 5.76e-08

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


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 52.71  E-value: 5.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLteKGAEQLRGQTSDRLETVTLDVTK--------TESVAAAAQWVK 98
Cdd:cd05353    3 FDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDL--GGDRKGSGKSSSAADKVVDEIKAaggkavanYDSVEDGEKIVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  99 ECVRDKG-LWGLVNNAGIsLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSLFG-GG 175
Cdd:cd05353   81 TAIDAFGrVDILVNNAGI-LRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKfGRIINTSSAAGLYGNFGqAN 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 150247226 176 YCISKYGVEAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:cd05353  160 YSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA 191
PRK05867 PRK05867
SDR family oxidoreductase;
24-232 7.35e-08

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 52.73  E-value: 7.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  24 LSHLRDKYVFITGCDSGFGKLLARQLDARGLRVLAAC----LTEKGAEQLRGQTSDRLeTVTLDVTKTESVAAAA-QWVK 98
Cdd:PRK05867   4 LFDLHGKRALITGASTGIGKRVALAYVEAGAQVAIAArhldALEKLADEIGTSGGKVV-PVCCDVSQHQQVTSMLdQVTA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  99 ECvrdKGLWGLVNNAGIsLPTAPNELLTKQDFVTILDVNLLGV-IDVTLSLLPLVRRARG-RVVNVSSVMGR---VSLFG 173
Cdd:PRK05867  83 EL---GGIDIAVCNAGI-ITVTPMLDMPLEEFQRLQNTNVTGVfLTAQAAAKAMVKQGQGgVIINTASMSGHiinVPQQV 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 150247226 174 GGYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKerfLKSFLEIWDRSSP 232
Cdd:PRK05867 159 SHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEP---YTEYQPLWEPKIP 214
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 23-211 1.30e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 52.11  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  23 VLSHLRDKYVFITGCDSGFGKLLARQLDARGLRV---------LAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAA 93
Cdd:PRK05875   1 MQLSFQDRTYLVTGGGSGIGKGVAAGLVAAGAAVmivgrnpdkLAAAAEEIEALKGAGAVRYEPADVTDEDQVARAVDAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  94 AQWvkecvrDKGLWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGvidvTLSLLP-----LVRRARGRVVNVSSVMG- 167
Cdd:PRK05875  81 TAW------HGRLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNG----TMYVLKhaareLVRGGGGSFVGISSIAAs 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 150247226 168 RVSLFGGGYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK05875 151 NTHRWFGAYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRT 194
PRK06196 PRK06196
oxidoreductase; Provisional
 27-170 1.43e-07

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 51.99  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVL-AACLTEKGAEQLRGqtSDRLETVTLDVTKTESVAAAAQWVKECVRDKG 105
Cdd:PRK06196  24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIvPARRPDVAREALAG--IDGVEVVMLDLADLESVRAFAERFLDSGRRID 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150247226 106 LwgLVNNAGIslpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARG-RVVNVSSVMGRVS 170
Cdd:PRK06196 102 I--LINNAGV---MACPETRVGDGWEAQFATNHLGHFALVNLLWPALAAGAGaRVVALSSAGHRRS 162
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-218 2.09e-07

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 51.06  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAacLTEKGAEQLRGQ---TSDRLETVTLDVTKTESVAAAaqwVKECVRD 103
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVG--VGVAEAPETQAQveaLGRKFHFITADLIQQKDIDSI---VSQAVEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 KGLWG-LVNNAGIslptapnelLTKQDFVTILDVNLLGVIDVTLSLLPLVRRA----------RGRVVNVSSVMGrvslF 172
Cdd:PRK12481  81 MGHIDiLINNAGI---------IRRQDLLEFGNKDWDDVININQKTVFFLSQAvakqfvkqgnGGKIINIASMLS----F 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 150247226 173 GGG-----YCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKER 218
Cdd:PRK12481 148 QGGirvpsYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAALR 198
PRK07856 PRK07856
SDR family oxidoreductase;
27-211 2.42e-07

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 51.09  E-value: 2.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGqtsdrLETVTLDVTKTESVAAAaqwVKECVRDKG- 105
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETVDGRP-----AEFHAADVRDPDQVAAL---VDAIVERHGr 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 106 LWGLVNNAGISLP----TAPNELLTKqdfvtILDVNLLGVIDVTLSLLPLVRR--ARGRVVNVSSVMG-RVSLFGGGYCI 178
Cdd:PRK07856  76 LDVLVNNAGGSPYalaaEASPRFHEK-----IVELNLLAPLLVAQAANAVMQQqpGGGSIVNIGSVSGrRPSPGTAAYGA 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 150247226 179 SKYGVEAFSDSLRRELSYfGVKVAMIEPGYFKT 211
Cdd:PRK07856 151 AKAGLLNLTRSLAVEWAP-KVRVNAVVVGLVRT 182
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-218 4.03e-07

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 50.26  E-value: 4.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTE--KGAEQLRgQTSDRLETVTLDVTKTESVAAAaqwVKECVRDK 104
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEptETIEQVT-ALGRRFLSLTADLRKIDGIPAL---LERAVAEF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 GLWG-LVNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLP--LVRRARGRVVNVSSVMGrvslFGGG-----Y 176
Cdd:PRK08993  84 GHIDiLVNNAGLIRREDAIEF-SEKDWDDVMNLNIKSVFFMSQAAAKhfIAQGNGGKIINIASMLS----FQGGirvpsY 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 150247226 177 CISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKER 218
Cdd:PRK08993 159 TASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLR 200
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 34-165 5.47e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 50.41  E-value: 5.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  34 ITGCDSGFGKLLARQLDARGLRV-LAACLTEKG---AEQLRGQTSDRLETV-TLDVTKTESV-AAAAQWVKECVRdkgLW 107
Cdd:PRK06197  21 VTGANTGLGYETAAALAAKGAHVvLAVRNLDKGkaaAARITAATPGADVTLqELDLTSLASVrAAADALRAAYPR---ID 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 150247226 108 GLVNNAGIslpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARG-RVVNVSSV 165
Cdd:PRK06197  98 LLINNAGV---MYTPKQTTADGFELQFGTNHLGHFALTGLLLDRLLPVPGsRVVTVSSG 153
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 27-233 1.05e-06

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


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 49.08  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQ----LRGQTSDRLETVTlDVTKTES----VAAAAQwvk 98
Cdd:cd08936    8 LANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRavatLQGEGLSVTGTVC-HVGKAEDrerlVATAVN--- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  99 ecvRDKGLWGLVNNAGISlPTAPNEL-LTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRVSLFG-GG 175
Cdd:cd08936   84 ---LHGGVDILVSNAAVN-PFFGNILdSTEEVWDKILDVNVKATALMTKAVVPeMEKRGGGSVVIVSSVAAFHPFPGlGP 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150247226 176 YCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTS-------KERFLKSFLEIWDRSSPE 233
Cdd:cd08936  160 YNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSalwmdkaVEESMKETLRIRRLGQPE 224
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 30-226 1.11e-06

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


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 48.73  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVrdKGLWGL 109
Cdd:cd09761    2 KVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKL--GRIDVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 110 VNNAGISLPTAPNELLTkQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRVSLFGG-GYCISKYGVEAFSD 188
Cdd:cd09761   80 VNNAARGSKGILSSLLL-EEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAFQSEPDSeAYAASKGGLVALTH 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 150247226 189 SLRRELSYFgVKVAMIEPGYFKTAvTSKERFLKSFLEI 226
Cdd:cd09761  159 ALAMSLGPD-IRVNCISPGWINTT-EQQEFTAAPLTQE 194
PLN02253 PLN02253
xanthoxin dehydrogenase
 27-206 1.30e-06

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 49.05  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLET--VTLDVTKTESVAAAAQWVKEcvRDK 104
Cdd:PLN02253  16 LLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNVcfFHCDVTVEDDVSRAVDFTVD--KFG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 GLWGLVNNAGISLPTAPN-ELLTKQDFVTILDVNLLGV-IDVTLSLLPLVRRARGRVVNVSSVMGRVSLFG-GGYCISKY 181
Cdd:PLN02253  94 TLDIMVNNAGLTGPPCPDiRNVELSEFEKVFDVNVKGVfLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGpHAYTGSKH 173

                        170       180
                 ....*....|....*....|....*
gi 150247226 182 GVEAFSDSLRRELSYFGVKVAMIEP 206
Cdd:PLN02253 174 AVLGLTRSVAAELGKHGIRVNCVSP 198
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 28-211 1.36e-06

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 48.64  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  28 RDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVRdkgLW 107
Cdd:cd08951    6 PMKRIFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSSLAETRKLADQVNAIGR---FD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 108 GLVNNAGISLptAPNELLTKQDFVTILDVNLLGVIDVTlsllPLVRRARgRVVNVSSVM---GRVSLFG----------- 173
Cdd:cd08951   83 AVIHNAGILS--GPNRKTPDTGIPAMVAVNVLAPYVLT----ALIRRPK-RLIYLSSGMhrgGNASLDDidwfnrgends 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 150247226 174 GGYCISKYGVEAFSDSLRRelSYFGVKVAMIEPGYFKT 211
Cdd:cd08951  156 PAYSDSKLHVLTLAAAVAR--RWKDVSSNAVHPGWVPT 191
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 31-224 1.75e-06

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 48.71  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  31 YVFITGCDSGFGKLLARQLDARGLRVLaacLTEKGAEQLRgQTSD---------RLETVTLDVTKteSVAAAAQWVKECV 101
Cdd:PLN02780  55 WALVTGPTDGIGKGFAFQLARKGLNLV---LVARNPDKLK-DVSDsiqskysktQIKTVVVDFSG--DIDEGVKRIKETI 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 102 RDKGLWGLVNNAGISLPTA------PNELLTkqdfvTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMGRV---SL 171
Cdd:PLN02780 129 EGLDVGVLINNVGVSYPYArffhevDEELLK-----NLIKVNVEGTTKVTQAVLPgMLKRKKGAIINIGSGAAIVipsDP 203

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 150247226 172 FGGGYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKERflKSFL 224
Cdd:PLN02780 204 LYAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMASIRR--SSFL 254
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 29-207 2.19e-06

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: 48.36  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  29 DKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQ-----LRGQTSDRLETVTLDVTKTESVAAAAQWVKECVRD 103
Cdd:cd09809    1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAavsriLEEWHKARVEAMTLDLASLRSVQRFAEAFKAKNSP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 kgLWGLVNNAGI-SLPTApnelLTKQDFVTILDVNLLGVIDVTLSLLPLVRR-ARGRVVNVSSVMGR------------V 169
Cdd:cd09809   81 --LHVLVCNAAVfALPWT----LTEDGLETTFQVNHLGHFYLVQLLEDVLRRsAPARVIVVSSESHRftdlpdscgnldF 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 150247226 170 SLFGG---------GYCISKYGVEAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:cd09809  155 SLLSPpkkkywsmlAYNRAKLCNILFSNELHRRLSPRGITSNSLHPG 201
PRK05717 PRK05717
SDR family oxidoreductase;
30-218 2.48e-06

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 47.96  E-value: 2.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAaqwVKECVRDKG-LWG 108
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFIAMDVADEAQVAAG---VAEVLGQFGrLDA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 109 LVNNAGISLP-TAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRVSLFGG-GYCISKYGVEAF 186
Cdd:PRK05717  88 LVCNAAIADPhNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHNGAIVNLASTRARQSEPDTeAYAASKGGLLAL 167

                        170       180       190
                 ....*....|....*....|....*....|..
gi 150247226 187 SDSLRRELSYfGVKVAMIEPGYFKTAVTSKER 218
Cdd:PRK05717 168 THALAISLGP-EIRVNAVSPGWIDARDPSQRR 198
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 109-216 3.06e-06

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 47.76  E-value: 3.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 109 LVNNAGISlPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRaRGRVVNVSSVMGRVSLFGG-GYCISKYGVEAFS 187
Cdd:PRK12747  92 LINNAGIG-PGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRD-NSRIINISSAATRISLPDFiAYSMTKGAINTMT 169

                         90       100
                 ....*....|....*....|....*....
gi 150247226 188 DSLRRELSYFGVKVAMIEPGYFKTAVTSK 216
Cdd:PRK12747 170 FTLAKQLGARGITVNAILPGFIKTDMNAE 198
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 32-211 4.62e-06

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: 47.18  E-value: 4.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRG---QTSDRLETVTLDVTKTESVAAAAQW-VKECvrdKGLW 107
Cdd:cd05365    2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAaiqQAGGQAIGLECNVTSEQDLEAVVKAtVSQF---GGIT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 108 GLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRAR-GRVVNVSSVMGRVSLFG-GGYCISKYGVEA 185
Cdd:cd05365   79 ILVNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGgGAILNISSMSSENKNVRiAAYGSSKAAVNH 158

                        170       180
                 ....*....|....*....|....*.
gi 150247226 186 FSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:cd05365  159 MTRNLAFDLGPKGIRVNAVAPGAVKT 184
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 26-211 7.66e-06

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 46.38  E-value: 7.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  26 HLRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSD---RLETVTLDVTKTESVAAAAQWVKEcvR 102
Cdd:PRK06113   8 RLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQlggQAFACRCDITSEQELSALADFALS--K 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 DKGLWGLVNNAGISLPTAPNelLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVV-NVSSVMG-----RVSLFGGgy 176
Cdd:PRK06113  86 LGKVDILVNNAGGGGPKPFD--MPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVIlTITSMAAenkniNMTSYAS-- 161

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 150247226 177 ciSKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK06113 162 --SKAAASHLVRNMAFDLGEKNIRVNGIAPGAILT 194
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 27-174 8.88e-06

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: 46.99  E-value: 8.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAAC------LTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQwvkEC 100
Cdd:cd05274  148 GLDGTYLITGGLGGLGLLVARWLAARGARHLVLLsrrgpaPRAAARAALLRAGGARVSVVRCDVTDPAALAALLA---EL 224

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150247226 101 VRDKGLWGLVNNAGIsLPTAPNELLTKQDFVTILDVNLLGvidvTLSLLPLVRRARG-RVVNVSSVMgrvSLFGG 174
Cdd:cd05274  225 AAGGPLAGVIHAAGV-LRDALLAELTPAAFAAVLAAKVAG----ALNLHELTPDLPLdFFVLFSSVA---ALLGG 291
PRK09730 PRK09730
SDR family oxidoreductase;
34-211 1.17e-05

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 46.00  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  34 ITGCDSGFGKLLARQLDARGLRVLAACL-TEKGAEQLRGQ---TSDRLETVTLDVTKTESVAAAAQWVKEcvRDKGLWGL 109
Cdd:PRK09730   6 VTGGSRGIGRATALLLAQEGYTVAVNYQqNLHAAQEVVNLitqAGGKAFVLQADISDENQVVAMFTAIDQ--HDEPLAAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 110 VNNAGISLPTAPNELLTKQDFVTILDVNLLGVIdvtLSLLPLVRRAR-------GRVVNVSSVMGRVSLFGG--GYCISK 180
Cdd:PRK09730  84 VNNAGILFTQCTVENLTAERINRVLSTNVTGYF---LCCREAVKRMAlkhggsgGAIVNVSSAASRLGAPGEyvDYAASK 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 150247226 181 YGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK09730 161 GAIDTLTTGLSLEVAAQGIRVNCVRPGFIYT 191
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 27-207 1.39e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 45.72  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRV-LAACLTEK---GAEQLRGQTSDRLeTVTLDVTKTESVAAAAQWVKECvr 102
Cdd:PRK07576   7 FAGKNVVVVGGTSGINLGIAQAFARAGANVaVASRSQEKvdaAVAQLQQAGPEGL-GVSADVRDYAAVEAAFAQIADE-- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 103 dkglWG----LVNNAGISLPtAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRV-SLFGGGYC 177
Cdd:PRK07576  84 ----FGpidvLVSGAAGNFP-APAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPGASIIQISAPQAFVpMPMQAHVC 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 150247226 178 ISKYGVEAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:PRK07576 159 AAKAGVDMLTRTLALEWGPEGIRVNSIVPG 188
PRK09186 PRK09186
flagellin modification protein A; Provisional
 27-167 3.13e-05

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 44.60  E-value: 3.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQL-----RGQTSDRLETVTLDVTKTESVAAAaqwVKECV 101
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELleslgKEFKSKKLSLVELDITDQESLEEF---LSKSA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150247226 102 RDKG-LWGLVNNAgisLPTAPN-----ELLTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVVNVSSVMG 167
Cdd:PRK09186  79 EKYGkIDGAVNCA---YPRNKDygkkfFDVSLDDFNENLSLHLGSSFLFSQQFAKyFKKQGGGNLVNISSIYG 148
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-211 5.93e-05

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 43.94  E-value: 5.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAAclTEKGAEQ-------LRGQTSDRLeTVTLDVTKTEsvaAAAQWVKE 99
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVN--AKKRAEEmnetlkmVKENGGEGI-GVLADVSTRE---GCETLAKA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 100 CVRD-KGLWGLVNNAGISLPT----APNELLTKQdfvtiLDVNLLGVIDVTLSLLPLVRRArGRVVNVSSVMGRVSLFG- 173
Cdd:PRK06077  78 TIDRyGVADILVNNAGLGLFSpflnVDDKLIDKH-----ISTDFKSVIYCSQELAKEMREG-GAIVNIASVAGIRPAYGl 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 150247226 174 GGYCISKYGVEAFSDSLRRELSYfGVKVAMIEPGYFKT 211
Cdd:PRK06077 152 SIYGAMKAAVINLTKYLALELAP-KIRVNAIAPGFVKT 188
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 32-202 6.66e-05

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: 43.53  E-value: 6.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLET----VTLDVTKTESVAAAAQWVKECVRDKGLw 107
Cdd:cd05373    2 AAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGsakaVPTDARDEDEVIALFDLIEEEIGPLEV- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 108 gLVNNAGISLPTAPNELlTKQDFVTILDVNLLGVIDVTLSLLP-LVRRARGRVV---NVSSVMGRVSL--FGGGycisKY 181
Cdd:cd05373   81 -LVYNAGANVWFPILET-TPRVFEKVWEMAAFGGFLAAREAAKrMLARGRGTIIftgATASLRGRAGFaaFAGA----KF 154

                        170       180
                 ....*....|....*....|.
gi 150247226 182 GVEAFSDSLRRELSYFGVKVA 202
Cdd:cd05373  155 ALRALAQSMARELGPKGIHVA 175
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 27-207 1.71e-04

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


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 42.28  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKgaEQLRGQTSDRLE-------TVTLDVTKtESVAAAAqwVKE 99
Cdd:cd05355   24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEE--EDDAEETKKLIEeegrkclLIPGDLGD-ESFCRDL--VKE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 100 CVRDKG-LWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRArGRVVNVSSVM---GRVSLFggG 175
Cdd:cd05355   99 VVKEFGkLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKKG-SSIINTTSVTaykGSPHLL--D 175

                        170       180       190
                 ....*....|....*....|....*....|..
gi 150247226 176 YCISKYGVEAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:cd05355  176 YAATKGAIVAFTRGLSLQLAEKGIRVNAVAPG 207
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 30-207 1.78e-04

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


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 42.26  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLAACLT-EKGAEQLRGQTSDRLETVTL---DVTKTESVA-----AAAQWvkec 100
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRsEAEAQRLKDELNALRNSAVLvqaDLSDFAACAdlvaaAFRAF---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 101 vrdKGLWGLVNNAGISLPTAPNELLTkQDFVTILDVNLLGVIDVTLSLLPLVR-RARGRVVNVSSVMGRVSLFGG-GYCI 178
Cdd:cd05357   77 ---GRCDVLVNNASAFYPTPLGQGSE-DAWAELFGINLKAPYLLIQAFARRLAgSRNGSIINIIDAMTDRPLTGYfAYCM 152

                        170       180
                 ....*....|....*....|....*....
gi 150247226 179 SKYGVEAFSDSLRRELSYFgVKVAMIEPG 207
Cdd:cd05357  153 SKAALEGLTRSAALELAPN-IRVNGIAPG 180
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 30-207 2.19e-04

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 41.97  E-value: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  30 KYVFITGCDSGFGKLLARQLDARGLRVLaacLTEKGAEQLR------GQTSDRLETVTLDVTKTESVAAAaqwVKECVRD 103
Cdd:PRK07677   2 KVVIITGGSSGMGKAMAKRFAEEGANVV---ITGRTKEKLEeakleiEQFPGQVLTVQMDVRNPEDVQKM---VEQIDEK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 KG-LWGLVNNAGISLpTAPNELLTKQDFVTILDVNLLGVIDVTLSLLP--LVRRARGRVVNVssvmgrVSLF----GGGY 176
Cdd:PRK07677  76 FGrIDALINNAAGNF-ICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKywIEKGIKGNIINM------VATYawdaGPGV 148

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 150247226 177 CIS---KYGVEAFSDSLRRELSY-FGVKVAMIEPG 207
Cdd:PRK07677 149 IHSaaaKAGVLAMTRTLAVEWGRkYGIRVNAIAPG 183
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 27-207 3.58e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 41.45  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  27 LRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQ-TSDRLETVTL--DVtktESVAAAAQWVKECVRD 103
Cdd:PRK07478   4 LNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEiRAEGGEAVALagDV---RDEAYAKALVALAVER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 104 KG-LWGLVNNAGISLPTAPNELLTKQDFVTILDVNLlgvidvTLSLL-------PLVRRARGRVVNVSSVMGRVSLFGG- 174
Cdd:PRK07478  81 FGgLDIAFNNAGTLGEMGPVAEMSLEGWRETLATNL------TSAFLgakhqipAMLARGGGSLIFTSTFVGHTAGFPGm 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 150247226 175 -GYCISKYGVEAFSDSLRRELSYFGVKVAMIEPG 207
Cdd:PRK07478 155 aAYAASKAGLIGLTQVLAAEYGAQGIRVNALLPG 188
PRK06123 PRK06123
SDR family oxidoreductase;
29-211 4.75e-04

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 40.92  E-value: 4.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  29 DKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEK-GAEQLRGQTSDRLET---VTLDVTKTESVAAAAQWVKecvRDK 104
Cdd:PRK06123   2 RKVMIITGASRGIGAATALLAAERGYAVCLNYLRNRdAAEAVVQAIRRQGGEalaVAADVADEADVLRLFEAVD---REL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226 105 G-LWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIdvtLSLLPLVRR-------ARGRVVNVSSVMGRVSLFGG-- 174
Cdd:PRK06123  79 GrLDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSF---LCAREAVKRmstrhggRGGAIVNVSSMAARLGSPGEyi 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 150247226 175 GYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKT 211
Cdd:PRK06123 156 DYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYT 192
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
45-167 5.57e-04

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 40.76  E-value: 5.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  45 LARQLDARGLRVLAACLTEKGAeqlrgqTSDrlETVTLDVTKTESVAAAAQWVkecvrDKGLWGLVNNAGISlPTAPNEL 124
Cdd:PRK12428   1 TARLLRFLGARVIGVDRREPGM------TLD--GFIQADLGDPASIDAAVAAL-----PGRIDALFNIAGVP-GTAPVEL 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 150247226 125 ltkqdfvtILDVNLLGVIDVTLSLLPLVRRArGRVVNVSSVMG 167
Cdd:PRK12428  67 --------VARVNFLGLRHLTEALLPRMAPG-GAIVNVASLAG 100
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 32-95 5.82e-03

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


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 37.22  E-value: 5.82e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150247226  32 VFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTsdrLETVTLDVTKTESVAAAAQ 95
Cdd:cd05243    2 VLVVGATGKVGRHVVRELLDRGYQVRALVRDPSQAEKLEAAG---AEVVVGDLTDAESLAAALE 62
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 32-95 6.89e-03

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


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 37.13  E-value: 6.89e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150247226  32 VFITGCdSGF-GKLLARQLDARGLRVLAAClteKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQ 95
Cdd:COG0702    2 ILVTGA-TGFiGRRVVRALLARGHPVRALV---RDPEKAAALAAAGVEVVQGDLDDPESLAAALA 62
PRK07806 PRK07806
SDR family oxidoreductase;
25-113 8.00e-03

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 37.39  E-value: 8.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  25 SHLRDKYVFITGCDSGFGKLLARQLDARGLRVLA-----ACLTEKGAEQLR---GQTSdrleTVTLDVTKTESVAAAAQW 96
Cdd:PRK07806   2 GDLPGKTALVTGSSRGIGADTAKILAGAGAHVVVnyrqkAPRANKVVAEIEaagGRAS----AVGADLTDEESVAALMDT 77

                         90
                 ....*....|....*..
gi 150247226  97 VKEcvRDKGLWGLVNNA 113
Cdd:PRK07806  78 ARE--EFGGLDALVLNA 92
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 31-218 9.63e-03

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


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 37.20  E-value: 9.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226   31 YVFITGCDSGFGKLLARQLDARGLR-----VLAA---CLTEKGAEQLRGQTSD-RLETVTLDVTKTESVAAAAQWVKECV 101
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKCLKSpgsvlVLSArndEALRQLKAEIGAERSGlRVVRVSLDLGAEAGLEQLLKALRELP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150247226  102 RDKGLWG--LVNNAGISLPTAPNEL-LTKQDFVT-ILDVNLLGVIDVTLSLLPLVRRARG---RVVNVSSVMGrVSLFGG 174
Cdd:TIGR01500  82 RPKGLQRllLINNAGTLGDVSKGFVdLSDSTQVQnYWALNLTSMLCLTSSVLKAFKDSPGlnrTVVNISSLCA-IQPFKG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 150247226  175 G--YCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKER 218
Cdd:TIGR01500 161 WalYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQQVR 206
 
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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