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Conserved domains on  [gi|1270051604|ref|XP_022787997.1|]
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retinol dehydrogenase 7-like isoform X2 [Stylophora pistillata]

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 ...
 38-317 6.46e-119

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: 345.03  E-value: 6.46e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLT--SEGQENLTAACSKRLTALHLDVTDSKEIKETYKFVAQYLPEnRGL 115
Cdd:cd09805     1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTknGPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGE-KGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGIAKV-GPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHASAYSISKFGVEA 194
Cdd:cd09805    80 WGLVNNAGILGFgGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAAVEA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 195 FSDALRRELGPTGVKVSIVEPGFFQTKITNPDNL-KGQWQELWANLNHSLKEEYGEKFYETSVKNMLTGMvdTCASPYLY 273
Cdd:cd09805   160 FSDSLRRELQPWGVKVSIIEPGNFKTGITGNSELwEKQAKKLWERLPPEVKKDYGEDYIDELKNKMLKYC--SRASPDLS 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1270051604 274 KVVDAIVHSLTSRYPKTRYMVGWDAKLLWIWISRLPAGVGDAIL 317
Cdd:cd09805   238 PVIDSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 38-317 6.46e-119

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: 345.03  E-value: 6.46e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLT--SEGQENLTAACSKRLTALHLDVTDSKEIKETYKFVAQYLPEnRGL 115
Cdd:cd09805     1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTknGPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGE-KGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGIAKV-GPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHASAYSISKFGVEA 194
Cdd:cd09805    80 WGLVNNAGILGFgGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAAVEA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 195 FSDALRRELGPTGVKVSIVEPGFFQTKITNPDNL-KGQWQELWANLNHSLKEEYGEKFYETSVKNMLTGMvdTCASPYLY 273
Cdd:cd09805   160 FSDSLRRELQPWGVKVSIIEPGNFKTGITGNSELwEKQAKKLWERLPPEVKKDYGEDYIDELKNKMLKYC--SRASPDLS 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1270051604 274 KVVDAIVHSLTSRYPKTRYMVGWDAKLLWIWISRLPAGVGDAIL 317
Cdd:cd09805   238 PVIDSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
35-310 6.86e-61

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 195.86  E-value: 6.86e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK---RLTALHLDVTDSKEIKETYKFVAQylpE 111
Cdd:COG0300     3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAagaRVEVVALDVTDPDAVAALAEAVLA---R 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 NRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKF 190
Cdd:COG0300    80 FGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPlMRARGRGRIVNVSSVAGLRGLPGMAAYAASKA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 191 GVEAFSDALRRELGPTGVKVSIVEPGFFQTKITnpdnlkgqwqelwanlnhslkeeygekfyetsvKNMLTGMVDTCASP 270
Cdd:COG0300   160 ALEGFSESLRAELAPTGVRVTAVCPGPVDTPFT---------------------------------ARAGAPAGRPLLSP 206

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1270051604 271 ylYKVVDAIVHSLTSryPKTRYMVGWDAKLLWIWISRLPA 310
Cdd:COG0300   207 --EEVARAILRALER--GRAEVYVGWDARLLARLLRLLPR 242
PRK06182 PRK06182
short chain dehydrogenase; Validated
 36-318 8.36e-53

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 175.53  E-value: 8.36e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  36 QQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAAcskRLTALHLDVTDSKEIKETykfVAQYLPENRGL 115
Cdd:PRK06182    2 QKKVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLASL---GVHPLSLDVTDEASIKAA---VDTIIAEEGRI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISKFGVEA 194
Cdd:PRK06182   76 DVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIYTPLGAWYHATKFALEG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 195 FSDALRRELGPTGVKVSIVEPGFFQTkitnpdnlkgQWQELWANlnhSLKEEYGEKFYETSVKNMLTGMVDTCAS----- 269
Cdd:PRK06182  156 FSDALRLEVAPFGIDVVVIEPGGIKT----------EWGDIAAD---HLLKTSGNGAYAEQAQAVAASMRSTYGSgrlsd 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1270051604 270 PYLykVVDAIVHSLTSRYPKTRYMVGWDAKLLwIWISR-LPAGVGDAILN 318
Cdd:PRK06182  223 PSV--IADAISKAVTARRPKTRYAVGFGAKPL-IFLRRiLPDRAFDRLIM 269
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 38-227 1.44e-52

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 172.41  E-value: 1.44e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTA---ACSKRLTALHLDVTDSKEIKETYKFVAQYLPenrG 114
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKelgALGGKALFIQGDVTDRAQVKALVEQAVERLG---R 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 115 LWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKFGVE 193
Cdd:pfam00106  78 LDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVI 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1270051604 194 AFSDALRRELGPTGVKVSIVEPGFFQTKITNPDN 227
Cdd:pfam00106 158 GFTRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 40-234 3.04e-31

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: 118.08  E-value: 3.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK----RLTALHLDVTDSKEIKETYKFVAQylpENRGL 115
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGAEEVVEELKalgvKALGVVLDVSDREDVKAVVEEIEE---ELGTI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTK-VFLPLIKKERGRIINLASIGGRTCLPHASAYSISKFGVEA 194
Cdd:TIGR01830  78 DILVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQaVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASKAGVIG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1270051604 195 FSDALRRELGPTGVKVSIVEPGFFQTKITN--PDNLKGQWQE 234
Cdd:TIGR01830 158 FTKSLAKELASRNITVNAVAPGFIDTDMTDklSEKVKKKILS 199
 
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; ...
 38-317 6.46e-119

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: 345.03  E-value: 6.46e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLT--SEGQENLTAACSKRLTALHLDVTDSKEIKETYKFVAQYLPEnRGL 115
Cdd:cd09805     1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTknGPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGE-KGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGIAKV-GPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHASAYSISKFGVEA 194
Cdd:cd09805    80 WGLVNNAGILGFgGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAAVEA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 195 FSDALRRELGPTGVKVSIVEPGFFQTKITNPDNL-KGQWQELWANLNHSLKEEYGEKFYETSVKNMLTGMvdTCASPYLY 273
Cdd:cd09805   160 FSDSLRRELQPWGVKVSIIEPGNFKTGITGNSELwEKQAKKLWERLPPEVKKDYGEDYIDELKNKMLKYC--SRASPDLS 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1270051604 274 KVVDAIVHSLTSRYPKTRYMVGWDAKLLWIWISRLPAGVGDAIL 317
Cdd:cd09805   238 PVIDSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 38-299 9.74e-76

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: 233.66  E-value: 9.74e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKetyKFVAQYLPENRGLWG 117
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIK---AAVKEVIERFGRIDV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 118 LVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKFGVEAFS 196
Cdd:cd05374    78 LVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPlMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEALS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 197 DALRRELGPTGVKVSIVEPGFFQTKITNpdnlkgqwqelwaNLNHSLKEEYGEKFYETSVKNMLTGMV-DTCASPYLYKV 275
Cdd:cd05374   158 ESLRLELAPFGIKVTIIEPGPVRTGFAD-------------NAAGSALEDPEISPYAPERKEIKENAAgVGSNPGDPEKV 224

                         250       260
                  ....*....|....*....|....
gi 1270051604 276 VDAIVHSLTSRYPKTRYMVGWDAK 299
Cdd:cd05374   225 ADVIVKALTSESPPLRYFLGSDAL 248
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
35-310 6.86e-61

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 195.86  E-value: 6.86e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK---RLTALHLDVTDSKEIKETYKFVAQylpE 111
Cdd:COG0300     3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAagaRVEVVALDVTDPDAVAALAEAVLA---R 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 NRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKF 190
Cdd:COG0300    80 FGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPlMRARGRGRIVNVSSVAGLRGLPGMAAYAASKA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 191 GVEAFSDALRRELGPTGVKVSIVEPGFFQTKITnpdnlkgqwqelwanlnhslkeeygekfyetsvKNMLTGMVDTCASP 270
Cdd:COG0300   160 ALEGFSESLRAELAPTGVRVTAVCPGPVDTPFT---------------------------------ARAGAPAGRPLLSP 206

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1270051604 271 ylYKVVDAIVHSLTSryPKTRYMVGWDAKLLWIWISRLPA 310
Cdd:COG0300   207 --EEVARAILRALER--GRAEVYVGWDARLLARLLRLLPR 242
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 36-224 4.22e-58

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: 188.08  E-value: 4.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  36 QQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKEtykFVAQYLPENRGL 115
Cdd:COG4221     4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEA---AVAAAVAEFGRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKFGVEA 194
Cdd:COG4221    81 DVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPaMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRG 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1270051604 195 FSDALRRELGPTGVKVSIVEPGFFQTKITN 224
Cdd:COG4221   161 LSESLRAELRPTGIRVTVIEPGAVDTEFLD 190
PRK06182 PRK06182
short chain dehydrogenase; Validated
 36-318 8.36e-53

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 175.53  E-value: 8.36e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  36 QQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAAcskRLTALHLDVTDSKEIKETykfVAQYLPENRGL 115
Cdd:PRK06182    2 QKKVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLASL---GVHPLSLDVTDEASIKAA---VDTIIAEEGRI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISKFGVEA 194
Cdd:PRK06182   76 DVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIYTPLGAWYHATKFALEG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 195 FSDALRRELGPTGVKVSIVEPGFFQTkitnpdnlkgQWQELWANlnhSLKEEYGEKFYETSVKNMLTGMVDTCAS----- 269
Cdd:PRK06182  156 FSDALRLEVAPFGIDVVVIEPGGIKT----------EWGDIAAD---HLLKTSGNGAYAEQAQAVAASMRSTYGSgrlsd 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1270051604 270 PYLykVVDAIVHSLTSRYPKTRYMVGWDAKLLwIWISR-LPAGVGDAILN 318
Cdd:PRK06182  223 PSV--IADAISKAVTARRPKTRYAVGFGAKPL-IFLRRiLPDRAFDRLIM 269
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 38-227 1.44e-52

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 172.41  E-value: 1.44e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTA---ACSKRLTALHLDVTDSKEIKETYKFVAQYLPenrG 114
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKelgALGGKALFIQGDVTDRAQVKALVEQAVERLG---R 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 115 LWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKFGVE 193
Cdd:pfam00106  78 LDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVI 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1270051604 194 AFSDALRRELGPTGVKVSIVEPGFFQTKITNPDN 227
Cdd:pfam00106 158 GFTRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
PRK06914 PRK06914
SDR family oxidoreductase;
37-308 5.12e-51

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 171.36  E-value: 5.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  37 QKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAAC-----SKRLTALHLDVTDSKEIKETYKFVAQYLPE 111
Cdd:PRK06914    3 KKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQAtqlnlQQNIKVQQLDVTDQNSIHNFQLVLKEIGRI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 NRglwgLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISKF 190
Cdd:PRK06914   83 DL----LVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGLSPYVSSKY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 191 GVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNpdnlKGQWQELWANLNHSLKEEYGEKFYETSVKNmltgmVDTCASP 270
Cdd:PRK06914  159 ALEGFSESLRLELKPFGIDVALIEPGSYNTNIWE----VGKQLAENQSETTSPYKEYMKKIQKHINSG-----SDTFGNP 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1270051604 271 ylYKVVDAIVHSLTSRYPKTRYMVGWDAKLL--------WIWISRL 308
Cdd:PRK06914  230 --IDVANLIVEIAESKRPKLRYPIGKGVKLMilakkilpWRLWEYL 273
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 40-223 6.68e-50

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: 167.08  E-value: 6.68e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK--RLTALHLDVTDSKEIKetyKFVAQYLPENRGLWG 117
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEALggNAVAVQADVSDEEDVE---ALVEEALEEFGRLDI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 118 LVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISKFGVEAFS 196
Cdd:cd05233    78 LVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGgGRIVNISSVAGLRPLPGQAAYAASKAALEGLT 157

                         170       180
                  ....*....|....*....|....*..
gi 1270051604 197 DALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:cd05233   158 RSLALELAPYGIRVNAVAPGLVDTPML 184
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 33-223 4.54e-47

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: 159.95  E-value: 4.54e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  33 TDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK---RLTALHLDVTDSKEIKEtykFVAQYL 109
Cdd:COG1028     2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAaggRALAVAADVTDEAAVEA---LVAAAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 110 PENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSIS 188
Cdd:COG1028    79 AAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPhMRERGGGRIVNISSIAGLRGSPGQAAYAAS 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1270051604 189 KFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:COG1028   159 KAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMT 193
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 36-220 5.54e-41

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 145.06  E-value: 5.54e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  36 QQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKETykfVAQYLPENRGL 115
Cdd:PRK06180    3 SMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAV---VADAEATFGPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISKFGVEA 194
Cdd:PRK06180   80 DVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRrGHIVNITSMGGLITMPGIGYYCGSKFALEG 159

                         170       180
                  ....*....|....*....|....*.
gi 1270051604 195 FSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK06180  160 ISESLAKEVAPFGIHVTAVEPGSFRT 185
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 35-226 6.87e-40

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: 141.57  E-value: 6.87e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAAC----SKRLTALHLDVTDSKEIKetyKFVAQYLP 110
Cdd:cd05332     1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSEClelgAPSPHVVPLDMSDLEDAE---QVVEEALK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 ENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISK 189
Cdd:cd05332    78 LFGGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPhLIERSQGSIVVVSSIAGKIGVPFRTAYAASK 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNPD 226
Cdd:cd05332   158 HALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNA 194
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
34-223 4.57e-39

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 139.14  E-value: 4.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTA---ACSKRLTALHLDVTDSKEIKETYKFVAQylp 110
Cdd:PRK05653    2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAelrAAGGEARVLVFDVSDEAAVRALIEAAVE--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 ENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISK 189
Cdd:PRK05653   79 AFGALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPpMIKARYGRIVNISSVSGVTGNPGQTNYSAAK 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:PRK05653  159 AGVIGFTKALALELASRGITVNAVAPGFIDTDMT 192
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 36-317 1.05e-38

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 138.88  E-value: 1.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  36 QQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAacskrLTALHLDVTDSKEIKetyKFVAQYLPENRGL 115
Cdd:PRK06179    3 NSKVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIPG-----VELLELDVTDDASVQ---AAVDEVIARAGRI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISKFGVEA 194
Cdd:PRK06179   75 DVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGsGRIINISSVLGFLPAPYMALYAASKHAVEG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 195 FSDALRRELGPTGVKVSIVEPGFFQTKI----TNPDnlkgqwqelwanlnhSLKEEYGEKFyeTSVKNMLTGMVDTCASP 270
Cdd:PRK06179  155 YSESLDHEVRQFGIRVSLVEPAYTKTNFdanaPEPD---------------SPLAEYDRER--AVVSKAVAKAVKKADAP 217

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1270051604 271 YLykVVDAIVHSLTSRYPKTRYMVGWDAKLLwiwiSRL----PAGVGDAIL 317
Cdd:PRK06179  218 EV--VADTVVKAALGPWPKMRYTAGGQASLL----SKLrrfmPAGAVDKSL 262
PRK08017 PRK08017
SDR family oxidoreductase;
37-318 4.60e-38

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 136.75  E-value: 4.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  37 QKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTaacSKRLTALHLDVTDSKEIKETYKFVAQyLPENRgLW 116
Cdd:PRK08017    2 QKSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDVARMN---SLGFTGILLDLDDPESVERAADEVIA-LTDNR-LY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 117 GLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKE-RGRIINLASIGGRTCLPHASAYSISKFGVEAF 195
Cdd:PRK08017   77 GLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHgEGRIVMTSSVMGLISTPGRGAYAASKYALEAW 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 196 SDALRRELGPTGVKVSIVEPGFFQTKITNpdnlkgqwqelwaNLNHSLKEEygekfyetSVKNmlTGMVDTCASPyLYKV 275
Cdd:PRK08017  157 SDALRMELRHSGIKVSLIEPGPIRTRFTD-------------NVNQTQSDK--------PVEN--PGIAARFTLG-PEAV 212

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1270051604 276 VDAIVHSLTSRYPKTRYMVGWDAKLLWIWISRLPAGVGDAILN 318
Cdd:PRK08017  213 VPKLRHALESPKPKLRYPVTLVTHAVMVLKRLLPGRMMDKILR 255
PRK05993 PRK05993
SDR family oxidoreductase;
37-318 9.90e-38

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 136.31  E-value: 9.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  37 QKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAacsKRLTALHLDVTDSKEIKEtykFVAQYLPENRG-L 115
Cdd:PRK05993    4 KRSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEA---EGLEAFQLDYAEPESIAA---LVAQVLELSGGrL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKE-RGRIINLASIGGRTCLPHASAYSISKFGVEA 194
Cdd:PRK05993   78 DALFNNGAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQgQGRIVQCSSILGLVPMKYRGAYNASKFAIEG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 195 FSDALRRELGPTGVKVSIVEPGFFQTKITNpDNLKgqWQELWANLNHSL-KEEYG---EKFYETSVKNMLTGMVDTCASP 270
Cdd:PRK05993  158 LSLTLRMELQGSGIHVSLIEPGPIETRFRA-NALA--AFKRWIDIENSVhRAAYQqqmARLEGGGSKSRFKLGPEAVYAV 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1270051604 271 YLykvvdaivHSLTSRYPKTRYMVGWDAKLLWIWISRLPAGVGDAILN 318
Cdd:PRK05993  235 LL--------HALTAPRPRPHYRVTTPAKQGALLKRLLPARWLYRLLR 274
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 33-223 4.27e-37

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 133.78  E-value: 4.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  33 TDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSE-GQENLTA---ACSKRLTALHLDVTDSKEIKETYKFVAQy 108
Cdd:PRK05557    1 MSLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEaGAEALVAeigALGGKALAVQGDVSDAESVERAVDEAKA- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 lpENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTK-VFLPLIKKERGRIINLASIGGRTCLPHASAYSI 187
Cdd:PRK05557   80 --EFGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKaVARPMMKQRSGRIINISSVVGLMGNPGQANYAA 157

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1270051604 188 SKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:PRK05557  158 SKAGVIGFTKSLARELASRGITVNAVAPGFIETDMT 193
PRK05650 PRK05650
SDR family oxidoreductase;
40-238 1.28e-36

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 133.24  E-value: 1.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNVfatCLTSEGQENLTAACsKRLTAL-------HLDVTDSKEIKEtykfVAQYLPEN 112
Cdd:PRK05650    3 VMITGAASGLGRAIALRWAREGWRL---ALADVNEEGGEETL-KLLREAggdgfyqRCDVRDYSQLTA----LAQACEEK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 113 rglWG----LVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSI 187
Cdd:PRK05650   75 ---WGgidvIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKsGRIVNIASMAGLMQGPAMSSYNV 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1270051604 188 SKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKI-----TNPDNLKGQWQELWAN 238
Cdd:PRK05650  152 AKAGVVALSETLLVELADDEIGVHVVCPSFFQTNLldsfrGPNPAMKAQVGKLLEK 207
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 38-224 3.37e-36

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: 131.63  E-value: 3.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTA----LHLDVTDSKEIKetyKFVAQYLPENR 113
Cdd:cd05346     1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPVkvlpLQLDVSDRESIE---AALENLPEEFR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 GLWGLVNNAGIAK-VGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKFG 191
Cdd:cd05346    78 DIDILVNNAGLALgLDPAQEADLEDWETMIDTNVKGLLNVTRLILPiMIARNQGHIINLGSIAGRYPYAGGNVYCATKAA 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1270051604 192 VEAFSDALRRELGPTGVKVSIVEPGFFQTKITN 224
Cdd:cd05346   158 VRQFSLNLRKDLIGTGIRVTNIEPGLVETEFSL 190
PRK05693 PRK05693
SDR family oxidoreductase;
37-220 1.71e-35

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 130.30  E-value: 1.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  37 QKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAAcskRLTALHLDVTDSKEIKetyKFVAQYLPENRGLW 116
Cdd:PRK05693    1 MPVVLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALAAA---GFTAVQLDVNDGAALA---RLAEELEAEHGGLD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 117 GLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHASAYSISKFGVEAFS 196
Cdd:PRK05693   75 VLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHALS 154

                         170       180
                  ....*....|....*....|....
gi 1270051604 197 DALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK05693  155 DALRLELAPFGVQVMEVQPGAIAS 178
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 34-223 5.37e-35

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 128.91  E-value: 5.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENlTAACSKRLTALHLDVTDSKEiketykfVAQYLPENR 113
Cdd:PRK07825    2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKE-TAAELGLVVGGPLDVTDPAS-------FAAFLDAVE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 GLWG----LVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSIS 188
Cdd:PRK07825   74 ADLGpidvLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPrMVPRGRGHVVNVASLAGKIPVPGMATYCAS 153

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1270051604 189 KFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:PRK07825  154 KHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELI 188
PRK12826 PRK12826
SDR family oxidoreductase;
34-220 2.46e-34

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 126.57  E-value: 2.46e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK---RLTALHLDVTDSKEIKEtykFVAQYLP 110
Cdd:PRK12826    3 DLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAaggKARARQVDVRDRAALKA---AVAAGVE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 ENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGR-TCLPHASAYSIS 188
Cdd:PRK12826   80 DFGRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPaLIRAGGGRIVLTSSVAGPrVGYPGLAHYAAS 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1270051604 189 KFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK12826  160 KAGLVGFTRALALELAARNITVNSVHPGGVDT 191
PRK09291 PRK09291
SDR family oxidoreductase;
37-220 7.57e-34

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 125.50  E-value: 7.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  37 QKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKR---LTALHLDVTDSKEIKETykfvAQYLPENr 113
Cdd:PRK09291    2 SKTILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRglaLRVEKLDLTDAIDRAQA----AEWDVDV- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 glwgLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKFGV 192
Cdd:PRK09291   77 ----LLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRkMVARGKGKVVFTSSMAGLITGPFTGAYCASKHAL 152

                         170       180
                  ....*....|....*....|....*...
gi 1270051604 193 EAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK09291  153 EAIAEAMHAELKPFGIQVATVNPGPYLT 180
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 35-223 2.13e-33

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


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 123.67  E-value: 2.13e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGR---ETALRLDSLgfNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKEtykfVAQYLPE 111
Cdd:cd05354     1 IKDKTVLVTGANRGIGKafvESLLAHGAK--KVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKA----AAAQAKD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 nrgLWGLVNNAGIAKV-GPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKK-ERGRIINLASIGGRTCLPHASAYSISK 189
Cdd:cd05354    75 ---VDVVINNAGVLKPaTLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKAnGGGAIVNLNSVASLKNFPAMGTYSASK 151

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:cd05354   152 SAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMA 185
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 46-234 5.84e-33

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: 122.54  E-value: 5.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  46 DSGFGRETALRLDSLGFNVFATCLTSEGQENLTAAcSKRL--TALHLDVTDSKEIKETYKFVAQYLPenrGLWGLVNNAG 123
Cdd:pfam13561   5 ESGIGWAIARALAEEGAEVVLTDLNEALAKRVEEL-AEELgaAVLPCDVTDEEQVEALVAAAVEKFG---RLDILVNNAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 124 IA--KVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKkERGRIINLASIGGRTCLPHASAYSISKFGVEAFSDALRR 201
Cdd:pfam13561  81 FApkLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMK-EGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAV 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1270051604 202 ELGPTGVKVSIVEPGFFQT----KITNPDNLKGQWQE 234
Cdd:pfam13561 160 ELGPRGIRVNAISPGPIKTlaasGIPGFDELLAAAEA 196
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 38-232 5.89e-33

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: 122.66  E-value: 5.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTA---ACSKRLTALHLDVTDSKEIKETYKFVAQylpENRG 114
Cdd:cd05333     1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEeikALGGNAAALEADVSDREAVEALVEKVEA---EFGP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 115 LWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTK-VFLPLIKKERGRIINLASIGGRTCLPHASAYSISKFGVE 193
Cdd:cd05333    78 VDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQaVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1270051604 194 AFSDALRRELGPTGVKVSIVEPGFFQTKITN--PDNLKGQW 232
Cdd:cd05333   158 GFTKSLAKELASRGITVNAVAPGFIDTDMTDalPEKVKEKI 198
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 38-216 1.25e-32

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: 122.57  E-value: 1.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRL---DSLGFNVFATCLTSEGQENLTAA----CSKRLTALHLDVTDSKEIKETYKFVAQYLP 110
Cdd:cd09806     1 TVVLITGCSSGIGLHLAVRLasdPSKRFKVYATMRDLKKKGRLWEAagalAGGTLETLQLDVCDSKSVAAAVERVTERHV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 ENrglwgLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISK 189
Cdd:cd09806    81 DV-----LVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGsGRILVTSSVGGLQGLPFNDVYCASK 155

                         170       180
                  ....*....|....*....|....*..
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:cd09806   156 FALEGLCESLAVQLLPFNVHLSLIECG 182
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 41-240 1.56e-32

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 122.45  E-value: 1.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  41 LVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKETykfVAQYLPENRGLWGLVN 120
Cdd:PRK08263    7 FITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAA---VETAVEHFGRLDIVVN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 121 NAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISKFGVEAFSDAL 199
Cdd:PRK08263   84 NAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRsGHIIQISSIGGISAFPMSGIYHASKWALEGMSEAL 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1270051604 200 RRELGPTGVKVSIVEPGFFQT-------KITNP----DNLKGQWQELWANLN 240
Cdd:PRK08263  164 AQEVAEFGIKVTLVEPGGYSTdwagtsaKRATPldayDTLREELAEQWSERS 215
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 35-224 1.02e-31

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


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 119.57  E-value: 1.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTA---ACSKRLTALHLDVTDSKEIKETykfVAQYLPE 111
Cdd:cd08934     1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADeleAEGGKALVLELDVTDEQQVDAA---VERTVEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 NRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIK-KERGRIINLASIGGRTCLPHASAYSISKF 190
Cdd:cd08934    78 LGRLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLlRNKGTIVNISSVAGRVAVRNSAVYNATKF 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1270051604 191 GVEAFSDALRRELGPTGVKVSIVEPGFFQTKITN 224
Cdd:cd08934   158 GVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRD 191
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 40-234 3.04e-31

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: 118.08  E-value: 3.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK----RLTALHLDVTDSKEIKETYKFVAQylpENRGL 115
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGAEEVVEELKalgvKALGVVLDVSDREDVKAVVEEIEE---ELGTI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTK-VFLPLIKKERGRIINLASIGGRTCLPHASAYSISKFGVEA 194
Cdd:TIGR01830  78 DILVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQaVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASKAGVIG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1270051604 195 FSDALRRELGPTGVKVSIVEPGFFQTKITN--PDNLKGQWQE 234
Cdd:TIGR01830 158 FTKSLAKELASRNITVNAVAPGFIDTDMTDklSEKVKKKILS 199
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 38-229 5.12e-31

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


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 116.95  E-value: 5.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFN-VFATCLTSE-GQEnltAAcsKRLTALH-------LDVTDSKEIKETYKFVAQy 108
Cdd:cd05324     1 KVALVTGANRGIGFEIVRQLAKSGPGtVILTARDVErGQA---AV--EKLRAEGlsvrfhqLDVTDDASIEAAADFVEE- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 lpENRGLWGLVNNAGIA-KVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTclphASAYS 186
Cdd:cd05324    75 --KYGGLDILVNNAGIAfKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPaGRIVNVSSGLGSL----TSAYG 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1270051604 187 ISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNPDNLK 229
Cdd:cd05324   149 VSKAALNALTRILAKELKETGIKVNACCPGWVKTDMGGGKAPK 191
PRK07832 PRK07832
SDR family oxidoreductase;
38-230 1.02e-30

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 117.84  E-value: 1.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEG----QENLTAACSKRLTALHLDVTDSKEIKEtykFVAQYLPENR 113
Cdd:PRK07832    1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGlaqtVADARALGGTVPEHRALDISDYDAVAA---FAADIHAAHG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 GLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGR-IINLASIGGRTCLPHASAYSISKFG 191
Cdd:PRK07832   78 SMDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPpMVAAGRGGhLVNVSSAAGLVALPWHAAYSASKFG 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1270051604 192 VEAFSDALRRELGPTGVKVSIVEPGFFQTKITNPDNLKG 230
Cdd:PRK07832  158 LRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVNTVEIAG 196
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 33-217 3.35e-30

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 115.74  E-value: 3.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  33 TDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTS-EGQENLTA---ACSKRLTALHLDVTDSKEIKETykfVAQY 108
Cdd:PRK12825    2 GSLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDeEAAEELVEaveALGRRAQAVQADVTDKAALEAA---VAAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 LPENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTK-VFLPLIKKERGRIINLASIGGRTCLPHASAYSI 187
Cdd:PRK12825   79 VERFGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRaVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAA 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 1270051604 188 SKFGVEAFSDALRRELGPTGVKVSIVEPGF 217
Cdd:PRK12825  159 AKAGLVGLTKALARELAEYGITVNMVAPGD 188
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 40-223 6.30e-30

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: 114.65  E-value: 6.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNV----FATCLTSEGQENLTAACSKrLTALHLDVTDSKEIKETYKFVAQylpENRGL 115
Cdd:cd05339     2 VLITGGGSGIGRLLALEFAKRGAKVvildINEKGAEETANNVRKAGGK-VHYYKCDVSKREEVYEAAKKIKK---EVGDV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKFGVEA 194
Cdd:cd05339    78 TILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPdMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVG 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1270051604 195 FSDALRREL---GPTGVKVSIVEPGFFQTKIT 223
Cdd:cd05339   158 FHESLRLELkayGKPGIKTTLVCPYFINTGMF 189
PRK06181 PRK06181
SDR family oxidoreductase;
38-222 2.07e-29

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 113.92  E-value: 2.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTA---LHLDVTDSKEIKetyKFVAQYLPENRG 114
Cdd:PRK06181    2 KVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEalvVPTDVSDAEACE---RLIEAAVARFGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 115 LWGLVNNAGIAKVGPI-EWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHASAYSISKFGVE 193
Cdd:PRK06181   79 IDILVNNAGITMWSRFdELTDLSVFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTRSGYAASKHALH 158

                         170       180
                  ....*....|....*....|....*....
gi 1270051604 194 AFSDALRRELGPTGVKVSIVEPGFFQTKI 222
Cdd:PRK06181  159 GFFDSLRIELADDGVAVTVVCPGFVATDI 187
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 40-220 2.94e-29

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


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 112.86  E-value: 2.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK---RLTALHLDVTDSKEIKEtykfVAQYLPENRG-- 114
Cdd:cd05360     3 VVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRElggEAIAVVADVADAAQVER----AADTAVERFGri 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 115 -LWglVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKFGV 192
Cdd:cd05360    79 dTW--VNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPhLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAV 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1270051604 193 EAFSDALRRELGPTG--VKVSIVEPGFFQT 220
Cdd:cd05360   157 RGFTESLRAELAHDGapISVTLVQPTAMNT 186
PRK06482 PRK06482
SDR family oxidoreductase;
41-220 4.69e-29

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 113.29  E-value: 4.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  41 LVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKETykfVAQYLPENRGLWGLVN 120
Cdd:PRK06482    6 FITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARYGDRLWVLQLDVTDSAAVRAV---VDRAFAALGRIDVVVS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 121 NAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERG-RIINLASIGGRTCLPHASAYSISKFGVEAFSDAL 199
Cdd:PRK06482   83 NAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGgRIVQVSSEGGQIAYPGFSLYHATKWGIEGFVEAV 162

                         170       180
                  ....*....|....*....|.
gi 1270051604 200 RRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK06482  163 AQEVAPFGIEFTIVEPGPART 183
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 34-225 6.42e-29

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: 112.07  E-value: 6.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSE---GQENLTAACSKRLTALHLDVTDSKEIKetyKFVAQYLP 110
Cdd:cd05347     2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEkaeEAQQLIEKEGVEATAFTCDVSDEEAIK---AAVEAIEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 ENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTK-VFLPLIKKERGRIINLASIGGRTCLPHASAYSISK 189
Cdd:cd05347    79 DFGKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQaVARHMIKQGHGKIINICSLLSELGGPPVPAYAASK 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNP 225
Cdd:cd05347   159 GGVAGLTKALATEWARHGIQVNAIAPGYFATEMTEA 194
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
38-224 6.73e-29

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 112.17  E-value: 6.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQ----ENLTAACSKRLTALHLDVTDSKEIKETykfVAQYLPENR 113
Cdd:PRK12824    3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCakdwFEEYGFTEDQVRLKELDVTDTEECAEA---LAEIEEEEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 GLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISKFGV 192
Cdd:PRK12824   80 PVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGyGRIINISSVNGLKGQFGQTNYSAAKAGM 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1270051604 193 EAFSDALRRELGPTGVKVSIVEPGFFQTKITN 224
Cdd:PRK12824  160 IGFTKALASEGARYGITVNCIAPGYIATPMVE 191
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 33-227 1.65e-28

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 110.93  E-value: 1.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  33 TDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK---RLTALHLDVTDSKEIKETykfVAQYL 109
Cdd:PRK07666    3 QSLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAygvKVVIATADVSDYEEVTAA---IEQLK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 110 PENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSIS 188
Cdd:PRK07666   80 NELGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPsMIERQSGDIINISSTAGQKGAAVTSAYSAS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1270051604 189 KFGVEAFSDALRRELGPTGVKVSIVEPGFFQT--------KITNPDN 227
Cdd:PRK07666  160 KFGVLGLTESLMQEVRKHNIRVTALTPSTVATdmavdlglTDGNPDK 206
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 34-223 5.42e-28

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: 109.78  E-value: 5.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKetyKFVAQYLPENR 113
Cdd:cd05341     2 RLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWT---AVVDTAREAFG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 GLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKE-RGRIINLASIGGRTCLPHASAYSISKFGV 192
Cdd:cd05341    79 RLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAgGGSIINMSSIEGLVGDPALAAYNASKGAV 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1270051604 193 EAFSDALRRELGPT--GVKVSIVEPGFFQTKIT 223
Cdd:cd05341   159 RGLTKSAALECATQgyGIRVNSVHPGYIYTPMT 191
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 38-220 7.86e-28

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


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 108.88  E-value: 7.86e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFatcLTSEGQENLTAACsKRLTALHL-----------DVTDSKEIKETYK-FV 105
Cdd:cd08939     2 KHVLITGGSSGIGKALAKELVKEGANVI---IVARSESKLEEAV-EEIEAEANasgqkvsyisaDLSDYEEVEQAFAqAV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 106 AQYLPENRglwgLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASA 184
Cdd:cd08939    78 EKGGPPDL----VVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRpGHIVFVSSQAALVGIYGYSA 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1270051604 185 YSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:cd08939   154 YCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDT 189
PRK07326 PRK07326
SDR family oxidoreductase;
35-216 1.20e-27

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 108.56  E-value: 1.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVfatCLTSEGQENLTAACSK-----RLTALHLDVTDSKEIKetyKFVAQYL 109
Cdd:PRK07326    4 LKGKVALITGGSKGIGFAIAEALLAEGYKV---AITARDQKELEEAAAElnnkgNVLGLAADVRDEADVQ---RAVDAIV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 110 PENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHASAYSISK 189
Cdd:PRK07326   78 AAFGGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGTNFFAGGAAYNASK 157

                         170       180
                  ....*....|....*....|....*..
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:PRK07326  158 FGLVGFSEAAMLDLRQYGIKVSTIMPG 184
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 35-295 1.77e-27

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: 108.27  E-value: 1.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVfatCLTSEGQENLTA---ACSKR------LTALHLDVTDSKEIKETY-KF 104
Cdd:cd05364     1 LSGKVAIITGSSSGIGAGTAILFARLGARL---ALTGRDAERLEEtrqSCLQAgvsekkILLVVADLTEEEGQDRIIsTT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 105 VAQYlpenRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHASA 184
Cdd:cd05364    78 LAKF----GRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGRSFPGVLY 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 185 YSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNpdnlkgqwqelwanlNHSLKEEYGEKFYETsVKNML---- 260
Cdd:cd05364   154 YCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHR---------------RMGMPEEQYIKFLSR-AKETHplgr 217

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1270051604 261 TGMVDtcaspylyKVVDAIVHsLTSRypKTRYMVG 295
Cdd:cd05364   218 PGTVD--------EVAEAIAF-LASD--ASSFITG 241
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-224 2.21e-27

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 108.01  E-value: 2.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSE--GQENLTAACSKRLTAL--HLDVTDSKEIKetyKFVAQYL 109
Cdd:PRK05565    2 KLMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEeaAQELLEEIKEEGGDAIavKADVSSEEDVE---NLVEQIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 110 PENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSIS 188
Cdd:PRK05565   79 EKFGKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPyMIKRKSGVIVNISSIWGLIGASCEVLYSAS 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1270051604 189 KFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITN 224
Cdd:PRK05565  159 KGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWS 194
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 38-257 7.19e-27

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: 107.08  E-value: 7.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEgqENLTAACSK------RLTALHLDVTDSKEIKETYKFVAQYLPe 111
Cdd:cd05366     3 KVAIITGAAQGIGRAIAERLAADGFNIVLADLNLE--EAAKSTIQEiseagyNAVAVGADVTDKDDVEALIDQAVEKFG- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 nrGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKE--RGRIINLASIGGRTCLPHASAYSISK 189
Cdd:cd05366    80 --SFDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLghGGKIINASSIAGVQGFPNLGAYSASK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPGFFQTkitnpdnlkgqwqELWANLNHSL------KEEYGEKFYETSVK 257
Cdd:cd05366   158 FAVRGLTQTAAQELAPKGITVNAYAPGIVKT-------------EMWDYIDEEVgeiagkPEGEGFAEFSSSIP 218
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 38-230 8.36e-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: 105.91  E-value: 8.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVfatCLTSEGQENL--TAACSKRLTALHLDVTDSKEikeTYKFVAQYLPENRGL 115
Cdd:cd08932     1 KVALVTGASRGIGIEIARALARDGYRV---SLGLRNPEDLaaLSASGGDVEAVPYDARDPED---ARALVDALRDRFGRI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKFGVEA 194
Cdd:cd08932    75 DVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPaLREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRA 154

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1270051604 195 FSDALRRELGPTGVKVSIVEPGFFQTKITNPDNLKG 230
Cdd:cd08932   155 LAHALRQEGWDHGVRVSAVCPGFVDTPMAQGLTLVG 190
FabG-like PRK07231
SDR family oxidoreductase;
34-223 2.85e-26

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 104.91  E-value: 2.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVfatCLTSEGQENLTAACS-----KRLTALHLDVTDSKEIKETykfVAQY 108
Cdd:PRK07231    2 RLEGKVAIVTGASSGIGEGIARRFAAEGARV---VVTDRNEEAAERVAAeilagGRAIAVAADVSDEADVEAA---VAAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 LPENRGLWGLVNNAGIAKV-GPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYS 186
Cdd:PRK07231   76 LERFGSVDILVNNAGTTHRnGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGgGAIVNVASTAGLRPRPGLGWYN 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1270051604 187 ISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:PRK07231  156 ASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLL 192
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 38-216 3.31e-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: 104.51  E-value: 3.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVfatCLTSEGQENLTAACSKRLTALHLDVTDSKEIKETYKFVAQYLPENRGLWG 117
Cdd:cd08929     1 KAALVTGASRGIGEATARLLHAEGYRV---GICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 118 LVNNAGIAKVGPIEWQTIEEFKQ-IADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHASAYSISKFGVEAFS 196
Cdd:cd08929    78 LVNNAGVGVMKPVEELTPEEWRLvLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLS 157

                         170       180
                  ....*....|....*....|
gi 1270051604 197 DALRRELGPTGVKVSIVEPG 216
Cdd:cd08929   158 EAAMLDLREANIRVVNVMPG 177
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 38-225 5.10e-26

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: 103.69  E-value: 5.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAAC-SKRLTALHLDVTDSKEIKETykfVAQYLPENRG-L 115
Cdd:cd08931     1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELgAENVVAGALDVTDRAAWAAA---LADFAAATGGrL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERG-RIINLASIGGRTCLPHASAYSISKFGVEA 194
Cdd:cd08931    78 DALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGaRVINTASSSAIYGQPDLAVYSATKFAVRG 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1270051604 195 FSDALRRELGPTGVKVSIVEPGFFQTKITNP 225
Cdd:cd08931   158 LTEALDVEWARHGIRVADVWPWFVDTPILTK 188
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 38-235 6.33e-26

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: 104.28  E-value: 6.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVfatCLTSEGQENLTAACS------KRLTALHLDVTDSKEIKetyKFVAQYLPE 111
Cdd:cd05344     2 KVALVTAASSGIGLAIARALAREGARV---AICARNRENLERAASelraggAGVLAVVADLTDPEDID---RLVEKAGDA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 NRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISKF 190
Cdd:cd05344    76 FGRVDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLTVKEPEPNLVLSNVARA 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1270051604 191 GVEAFSDALRRELGPTGVKVSIVEPGFFQTkitnpdnlkGQWQEL 235
Cdd:cd05344   156 GLIGLVKTLSRELAPDGVTVNSVLPGYIDT---------ERVRRL 191
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 36-220 6.35e-26

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: 104.54  E-value: 6.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  36 QQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGqenlTAACSKRLTALHL-------DVTDSKEIKETYK-FVAQ 107
Cdd:cd08945     2 DSEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEG----LATTVKELREAGVeadgrtcDVRSVPEIEALVAaAVAR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 108 YLPENRglwgLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP---LIKKERGRIINLASIGGRTCLPHASA 184
Cdd:cd08945    78 YGPIDV----LVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKaggMLERGTGRIINIASTGGKQGVVHAAP 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1270051604 185 YSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:cd08945   154 YSASKHGVVGFTKALGLELARTGITVNAVCPGFVET 189
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 33-223 7.71e-26

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 103.90  E-value: 7.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  33 TDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK---RLTALHLDVTDSKEIKetyKFVAQYL 109
Cdd:PRK12939    3 SNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAaggRAHAIAADLADPASVQ---RFFDAAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 110 PENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSIS 188
Cdd:PRK12939   80 AALGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPhLRDSGRGRIVNLASDTALWGAPKLGAYVAS 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1270051604 189 KFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:PRK12939  160 KGAVIGMTRSLARELGGRGITVNAIAPGLTATEAT 194
PRK08267 PRK08267
SDR family oxidoreductase;
38-310 7.86e-26

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 104.25  E-value: 7.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAAC-SKRLTALHLDVTDSKEIKETykfVAQYLPENRG-L 115
Cdd:PRK08267    2 KSIFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELgAGNAWTGALDVTDRAAWDAA---LADFAAATGGrL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERG-RIINLASIGGRTCLPHASAYSISKFGVEA 194
Cdd:PRK08267   79 DVLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGaRVINTSSASAIYGQPGLAVYSATKFAVRG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 195 FSDALRRELGPTGVKVSIVEPGFFQTKITNpdnlkgqwqelwanlnhslkeEYGEKFYETSVKNmltGMVDTCASPYLYK 274
Cdd:PRK08267  159 LTEALDLEWRRHGIRVADVMPLFVDTAMLD---------------------GTSNEVDAGSTKR---LGVRLTPEDVAEA 214

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1270051604 275 VVDAIVHSltsryPKTRYMVGWDAKLLWIWISRLPA 310
Cdd:PRK08267  215 VWAAVQHP-----TRLHWPVGKQAKLLAFLARLSPG 245
PRK05855 PRK05855
SDR family oxidoreductase;
38-224 9.79e-26

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 108.14  E-value: 9.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENlTAACSKRL----TALHLDVTDSKEIKetyKFVAQYLPENR 113
Cdd:PRK05855  316 KLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAER-TAELIRAAgavaHAYRVDVSDADAME---AFAEWVRAEHG 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 GLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIkkERGR---IINLASIGGRTCLPHASAYSISK 189
Cdd:PRK05855  392 VPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRqMV--ERGTgghIVNVASAAAYAPSRSLPAYATSK 469

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITN 224
Cdd:PRK05855  470 AAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVA 504
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 35-221 1.27e-25

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: 103.12  E-value: 1.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTS-EGQENLTAACSK---RLTALHLDVTDSKEIKETYKFVAQylp 110
Cdd:cd05362     1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNYASSkAAAEEVVAEIEAaggKAIAVQADVSDPSQVARLFDAAEK--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 ENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKkERGRIINLASIGGRTCLPHASAYSISKF 190
Cdd:cd05362    78 AFGGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLR-DGGRIINISSSLTAAYTPNYGAYAGSKA 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1270051604 191 GVEAFSDALRRELGPTGVKVSIVEPGFFQTK 221
Cdd:cd05362   157 AVEAFTRVLAKELGGRGITVNAVAPGPVDTD 187
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 32-321 1.97e-25

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 104.62  E-value: 1.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  32 LTDLQQKYVLVTGCDSGFGRETALRLDSLGFNVfatCLTSEGQENLTAACSK------RLTALHLDVTDSKEIKEtykfV 105
Cdd:PRK07109    3 LKPIGRQVVVITGASAGVGRATARAFARRGAKV---VLLARGEEGLEALAAEiraaggEALAVVADVADAEAVQA----A 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 106 AQYLPENRG---LWglVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKE-RGRIINLASIGGRTCLPH 181
Cdd:PRK07109   76 ADRAEEELGpidTW--VNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRdRGAIIQVGSALAYRSIPL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 182 ASAYSISKFGVEAFSDALRRELGPTG--VKVSIVEPGFFQTkitnPdnlkgQWQelWAnLNHslkeeygekfyeTSVKNM 259
Cdd:PRK07109  154 QSAYCAAKHAIRGFTDSLRCELLHDGspVSVTMVQPPAVNT----P-----QFD--WA-RSR------------LPVEPQ 209

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270051604 260 LTGMVdtcaspYLYKVV-DAIVHSltSRYPKTRYMVGWDAKLLwIWISRLPAGVGDAILNLLG 321
Cdd:PRK07109  210 PVPPI------YQPEVVaDAILYA--AEHPRRELWVGGPAKAA-ILGNRLAPGLLDRYLARTG 263
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 40-252 3.35e-25

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: 101.60  E-value: 3.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFN-VFATCLTSEGQENLTAACSK--RLTALHLDVTDskEIKETYKFVAQYLPeNRGLW 116
Cdd:cd05325     1 VLITGASRGIGLELVRQLLARGNNtVIATCRDPSAATELAALGAShsRLHILELDVTD--EIAESAEAVAERLG-DAGLD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 117 GLVNNAGIA-KVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKK-ERGRIIN----LASIGGRTCLPHASaYSISKF 190
Cdd:cd05325    78 VLINNAGILhSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKgARAKIINissrVGSIGDNTSGGWYS-YRASKA 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270051604 191 GVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNPD-NLKGQW------QELWANLNHsLKEEYGEKFY 252
Cdd:cd05325   157 ALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFaKNKGPItpeesvAGLLKVIDN-LNEEDSGKFL 224
PRK09072 PRK09072
SDR family oxidoreductase;
34-215 5.37e-25

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 101.94  E-value: 5.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK--RLTALHLDVTDSKEIKEtykfVAQYLPE 111
Cdd:PRK09072    2 DLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYpgRHRWVVADLTSEAGREA----VLARARE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 NRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKK-ERGRIINLASIGGRTCLPHASAYSISKF 190
Cdd:PRK09072   78 MGGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAqPSAMVVNVGSTFGSIGYPGYASYCASKF 157

                         170       180
                  ....*....|....*....|....*
gi 1270051604 191 GVEAFSDALRRELGPTGVKVSIVEP 215
Cdd:PRK09072  158 ALRGFSEALRRELADTGVRVLYLAP 182
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 40-224 8.61e-25

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: 100.87  E-value: 8.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENL---TAACSKRLTALHLDVTDSKEIKETykfVAQYLPENRGLW 116
Cdd:cd05350     1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELkaeLLNPNPSVEVEILDVTDEERNQLV---IAELEAELGGLD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 117 GLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKFGVEAF 195
Cdd:cd05350    78 LVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPqFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSL 157

                         170       180
                  ....*....|....*....|....*....
gi 1270051604 196 SDALRRELGPTGVKVSIVEPGFFQTKITN 224
Cdd:cd05350   158 AESLRYDVKKRGIRVTVINPGFIDTPLTA 186
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 32-216 1.07e-24

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 101.29  E-value: 1.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  32 LTDLQQKYVLVTGCDSGFGRETALRLDSLGFNVfATCLTSEGQENLTAA--CSKRLTALHLDVTDSKEIKETYKFVAQYL 109
Cdd:PRK12829    6 LKPLDGLRVLVTGGASGIGRAIAEAFAEAGARV-HVCDVSEAALAATAArlPGAKVTATVADVADPAQVERVFDTAVERF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 110 PenrGLWGLVNNAGIAK-VGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER--GRIINLASIGGRTCLPHASAYS 186
Cdd:PRK12829   85 G---GLDVLVNNAGIAGpTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGhgGVIIALSSVAGRLGYPGRTPYA 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 1270051604 187 ISKFGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:PRK12829  162 ASKWAVVGLVKSLAIELGPLGIRVNAILPG 191
PRK08264 PRK08264
SDR family oxidoreductase;
33-223 1.13e-24

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 100.35  E-value: 1.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  33 TDLQQKYVLVTGCDSGFGRETALRLDSLG-FNVFATCLTSEGQENLTAacskRLTALHLDVTDSKEIKEtykfVAQYLPE 111
Cdd:PRK08264    2 MDIKGKVVLVTGANRGIGRAFVEQLLARGaAKVYAAARDPESVTDLGP----RVVPLQLDVTDPASVAA----AAEAASD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 nrgLWGLVNNAGIAKVG-PIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKE-RGRIINLASIGGRTCLPHASAYSISK 189
Cdd:PRK08264   74 ---VTILVNNAGIFRTGsLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANgGGAIVNVLSVLSWVNFPNLGTYSASK 150

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:PRK08264  151 AAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMA 184
PRK07454 PRK07454
SDR family oxidoreductase;
35-222 5.29e-24

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 98.88  E-value: 5.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFatcLTSEGQENLTA------ACSKRLTALHLDVTDSKEIKETYK-FVAQ 107
Cdd:PRK07454    4 NSMPRALITGASSGIGKATALAFAKAGWDLA---LVARSQDALEAlaaelrSTGVKAAAYSIDLSNPEAIAPGIAeLLEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 108 YLPENRglwgLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYS 186
Cdd:PRK07454   81 FGCPDV----LINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGgGLIINVSSIAARNAFPQWGAYC 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1270051604 187 ISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKI 222
Cdd:PRK07454  157 VSKAALAAFTKCLAEEERSHGIRVCTITLGAVNTPL 192
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 34-216 9.63e-23

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 95.55  E-value: 9.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTA--ACskrlTALHLDVTDSKEIKETykfvaqyLPE 111
Cdd:PRK07060    6 DFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGetGC----EPLRLDVGDDAAIRAA-------LAA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 NRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKER-GRIINLASIGGRTCLPHASAYSISK 189
Cdd:PRK07060   75 AGAFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARaMIAAGRgGSIVNVSSQAALVGLPDHLAYCASK 154

                         170       180
                  ....*....|....*....|....*..
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:PRK07060  155 AALDAITRVLCVELGPHGIRVNSVNPT 181
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 33-226 1.22e-22

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 94.86  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  33 TDLQQKYVLVTGCDSGFGRETALRLDSLGFNVfatCLTSEGQENLTAACSKRL-TALHLDVTDSKEIKETYKFVAQYLPE 111
Cdd:PRK12828    3 HSLQGKVVAITGGFGGLGRATAAWLAARGARV---ALIGRGAAPLSQTLPGVPaDALRIGGIDLVDPQAARRAVDEVNRQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 NRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKF 190
Cdd:PRK12828   80 FGRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPaLTASGGGRIVNIGAGAALKAGPGMGAYAAAKA 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1270051604 191 GVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNPD 226
Cdd:PRK12828  160 GVARLTEALAAELLDRGITVNAVLPSIIDTPPNRAD 195
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 35-245 1.50e-22

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 94.95  E-value: 1.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKR-LTALHL--DVTDSKEIKETYKFVAQYlpe 111
Cdd:PRK12429    2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAgGKAIGVamDVTDEEAINAGIDYAVET--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 nrglWG----LVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYS 186
Cdd:PRK12429   79 ----FGgvdiLVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGgGRIINMASVHGLVGSAGKAAYV 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1270051604 187 ISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKItnpdnLKGQWQELWANLNHSLKE 245
Cdd:PRK12429  155 SAKHGLIGLTKVVALEGATHGVTVNAICPGYVDTPL-----VRKQIPDLAKERGISEEE 208
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 34-210 2.39e-22

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


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 94.07  E-value: 2.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATcltseG--QENLTAACSKR--LTALHLDVTDSKEIKETYKFVAQYL 109
Cdd:COG3967     2 KLTGNTILITGGTSGIGLALAKRLHARGNTVIIT-----GrrEEKLEEAAAANpgLHTIVLDVADPASIAALAEQVTAEF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 110 PEnrgLWGLVNNAGIAKV-----GPIEWQTIEefkQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHAS 183
Cdd:COG3967    77 PD---LNVLINNAGIMRAedlldEAEDLADAE---REITTNLLGPIRLTAAFLPhLKAQPEAAIVNVSSGLAFVPLAVTP 150

                         170       180
                  ....*....|....*....|....*..
gi 1270051604 184 AYSISKFGVEAFSDALRRELGPTGVKV 210
Cdd:COG3967   151 TYSATKAALHSYTQSLRHQLKDTSVKV 177
PRK06484 PRK06484
short chain dehydrogenase; Validated
 40-220 3.65e-22

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 97.23  E-value: 3.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKETYKfvaqylpENRGLWG-- 117
Cdd:PRK06484  272 VAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFA-------QIQARWGrl 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 118 --LVNNAGIAKV-GPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKErGRIINLASIGGRTCLPHASAYSISKFGVEA 194
Cdd:PRK06484  345 dvLVNNAGIAEVfKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG-GVIVNLGSIASLLALPPRNAYCASKAAVTM 423

                         170       180
                  ....*....|....*....|....*.
gi 1270051604 195 FSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK06484  424 LSRSLACEWAPAGIRVNTVAPGYIET 449
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 38-224 5.46e-22

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: 93.05  E-value: 5.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVfatCLTSEGQENLTAAcskrltalhldvtdSKEIKETY----KFVA------- 106
Cdd:cd05356     2 TWAVVTGATDGIGKAYAEELAKRGFNV---ILISRTQEKLDAV--------------AKEIEEKYgvetKTIAadfsagd 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 107 -QYLPENRGLWG-----LVNNAGIAKVGPIEWQ--TIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRT 177
Cdd:cd05356    65 dIYERIEKELEGldigiLVNNVGISHSIPEYFLetPEDELQDIINVNVMATLKMTRLILPgMVKRKKGAIVNISSFAGLI 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1270051604 178 CLPHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITN 224
Cdd:cd05356   145 PTPLLATYSASKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSK 191
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 33-224 6.91e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 94.27  E-value: 6.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  33 TDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHL--DVTD-------SKEIKETYK 103
Cdd:PRK05872    5 TSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDRVLTVvaDVTDlaamqaaAEEAVERFG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 104 fvaqylpenrGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHAS 183
Cdd:PRK05872   85 ----------GIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSLAAFAAAPGMA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1270051604 184 AYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITN 224
Cdd:PRK05872  155 AYCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDLVR 195
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 35-216 1.07e-21

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 92.50  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTA----ACSKRLTALHLDVTDSKEiketykfVAQYLP 110
Cdd:PRK12937    3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADELVaeieAAGGRAIAVQADVADAAA-------VTRLFD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 ENRGLWG----LVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKkERGRIINLASIGGRTCLPHASAYS 186
Cdd:PRK12937   76 AAETAFGridvLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLG-QGGRIINLSTSVIALPLPGYGPYA 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 1270051604 187 ISKFGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:PRK12937  155 ASKAAVEGLVHVLANELRGRGITVNAVAPG 184
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 35-223 2.18e-21

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 91.77  E-value: 2.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENltAACSKRLTALHLDVTDSKEIKETYKFVAQYLPEnrg 114
Cdd:PRK06463    5 FKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAK--ELREKGVFTIKCDVGNRDQVKKSKEVVEKEFGR--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 115 LWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGG-RTCLPHASAYSISKFGV 192
Cdd:PRK06463   80 VDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKnGAIVNIASNAGiGTAAEGTTFYAITKAGI 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1270051604 193 EAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:PRK06463  160 IILTRRLAFELGKYGIRVNAVAPGWVETDMT 190
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 38-220 2.26e-21

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: 91.74  E-value: 2.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFatcLTSEGQENLTAACSKRLTALH--------LDVTDSKEIKETYKFVAQYL 109
Cdd:cd08940     3 KVALVTGSTSGIGLGIARALAAAGANIV---LNGFGDAAEIEAVRAGLAAKHgvkvlyhgADLSKPAAIEDMVAYAQRQF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 110 PenrGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSIS 188
Cdd:cd08940    80 G---GVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGwGRIINIASVHGLVASANKSAYVAA 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1270051604 189 KFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:cd08940   157 KHGVVGLTKVVALETAGTGVTCNAICPGWVLT 188
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
37-248 2.34e-21

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 91.71  E-value: 2.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  37 QKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK---RLTALHLDVTDSKEIketYKFVAQYLPENR 113
Cdd:PRK08643    2 SKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKdggKAIAVKADVSDRDQV---FAAVRQVVDTFG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 GLWGLVNNAGIAKVGPIEWQTIEEFKQIADVN----LWGLIDVTKVFLPLikKERGRIINLASIGGRTCLPHASAYSISK 189
Cdd:PRK08643   79 DLNVVVNNAGVAPTTPIETITEEQFDKVYNINvggvIWGIQAAQEAFKKL--GHGGKIINATSQAGVVGNPELAVYSSTK 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPGFFQTKitnpdnlkgqwqeLWANLNHSLKEEYG 248
Cdd:PRK08643  157 FAVRGLTQTAARDLASEGITVNAYAPGIVKTP-------------MMFDIAHQVGENAG 202
PRK06484 PRK06484
short chain dehydrogenase; Validated
 36-222 3.02e-21

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 94.53  E-value: 3.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  36 QQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKETYKFVAQYLPEnrgL 115
Cdd:PRK06484    4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGR---I 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGIakVGPIEWQTI----EEFKQIADVNLWGLIDVTKVFLPLIKKER--GRIINLASIGGRTCLPHASAYSISK 189
Cdd:PRK06484   81 DVLVNNAGV--TDPTMTATLdttlEEFARLQAINLTGAYLVAREALRLMIEQGhgAAIVNVASGAGLVALPKRTAYSASK 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPGFFQTKI 222
Cdd:PRK06484  159 AAVISLTRSLACEWAAKGIRVNAVLPGYVRTQM 191
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 34-234 3.50e-21

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 91.10  E-value: 3.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACskrltaLHLDVTDSKEIKETykfVAQYLPENR 113
Cdd:PRK08220    5 DFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDYPFAT------FVLDVSDAAAVAQV---CQRLLAETG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 GLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISKFGV 192
Cdd:PRK08220   76 PLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRsGAIVTVGSNAAHVPRIGMAAYGASKAAL 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1270051604 193 EAFSDALRRELGPTGVKVSIVEPGffqtkITNPDNLKGQWQE 234
Cdd:PRK08220  156 TSLAKCVGLELAPYGVRCNVVSPG-----STDTDMQRTLWVD 192
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 34-231 3.58e-21

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


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 90.44  E-value: 3.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFatcLTSEGQENLTAAcSKRLTALH---LDVTDSKEIKetyKFVAQYLP 110
Cdd:cd05370     2 KLTGNTVLITGGTSGIGLALARKFLEAGNTVI---ITGRREERLAEA-KKELPNIHtivLDVGDAESVE---ALAEALLS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 ENRGLWGLVNNAGIAKvgPIEWQ----TIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASigGRTCLPHASA- 184
Cdd:cd05370    75 EYPNLDILINNAGIQR--PIDLRdpasDLDKADTEIDTNLIGPIRLIKAFLPhLKKQPEATIVNVSS--GLAFVPMAANp 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1270051604 185 -YSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNPDNLKGQ 231
Cdd:cd05370   151 vYCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNPDG 198
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 40-234 4.81e-21

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: 90.61  E-value: 4.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNVFATCLtsegQENLTAACSKRLTALHLDVTDSKEIKETykfVAQYLPENRGLWGLV 119
Cdd:cd05331     1 VIVTGAAQGIGRAVARHLLQAGATVIALDL----PFVLLLEYGDPLRLTPLDVADAAAVREV---CSRLLAEHGPIDALV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 120 NNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISKFGVEAFSDA 198
Cdd:cd05331    74 NCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRtGAIVTVASNAAHVPRISMAAYGASKAALASLSKC 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1270051604 199 LRRELGPTGVKVSIVEPGffqtkITNPDNLKGQWQE 234
Cdd:cd05331   154 LGLELAPYGVRCNVVSPG-----STDTAMQRTLWHD 184
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 32-223 4.85e-21

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 90.78  E-value: 4.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  32 LTDLQQKYVLVTGCDSGFGRETALRLDSLGFNVfatCLTSEGQENLTAAcSKRLTALHL-------DVTDSKEIKETykf 104
Cdd:PRK08213    7 LFDLSGKTALVTGGSRGLGLQIAEALGEAGARV---VLSARKAEELEEA-AAHLEALGIdalwiaaDVADEADIERL--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 105 VAQYLPENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVF--LPLIKKERGRIINLASI----GGRTC 178
Cdd:PRK08213   80 AEETLERFGHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVakRSMIPRGYGRIINVASVaglgGNPPE 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1270051604 179 LPHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:PRK08213  160 VMDTIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMT 204
PRK06139 PRK06139
SDR family oxidoreductase;
35-220 1.53e-20

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 90.94  E-value: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVfatCLTSEGQENLTA------ACSKRLTALHLDVTDSKEIKETYKFVAQY 108
Cdd:PRK06139    5 LHGAVVVITGASSGIGQATAEAFARRGARL---VLAARDEEALQAvaeecrALGAEVLVVPTDVTDADQVKALATQAASF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 LpenrG---LWglVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKE-RGRIINLASIGGRTCLPHASA 184
Cdd:PRK06139   82 G----GridVW--VNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQgHGIFINMISLGGFAAQPYAAA 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1270051604 185 YSISKFGVEAFSDALRRELGP-TGVKVSIVEPGFFQT 220
Cdd:PRK06139  156 YSASKFGLRGFSEALRGELADhPDIHVCDVYPAFMDT 192
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 31-220 1.59e-20

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 89.57  E-value: 1.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  31 FLTDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEG----QENLTAACSKrltALHL--DVTDSKEIKETYKF 104
Cdd:PRK13394    1 MMSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGanavADEINKAGGK---AIGVamDVTNEDAVNAGIDK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 105 VAQYLPEnrgLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER--GRIINLASIGGRTCLPHA 182
Cdd:PRK13394   78 VAERFGS---VDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHSHEASPLK 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1270051604 183 SAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK13394  155 SAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRT 192
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 31-237 2.18e-20

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: 88.93  E-value: 2.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  31 FLTDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK----RLTALHLDVTDSKEIKETYKFVA 106
Cdd:cd05352     2 DLFSLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKkygvKTKAYKCDVSSQESVEKTFKQIQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 107 QYLPEnrgLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVF-LPLIKKERGRIINLASIGGRTC-LP-HAS 183
Cdd:cd05352    82 KDFGK---IDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAaKIFKKQGKGSLIITASMSGTIVnRPqPQA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1270051604 184 AYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITnpDNLKGQWQELWA 237
Cdd:cd05352   159 AYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLT--DFVDKELRKKWE 210
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 35-223 2.94e-20

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: 88.70  E-value: 2.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKEtykFVAQYLPENRG 114
Cdd:cd08944     1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAA---LFERAVEEFGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 115 LWGLVNNAGIAKVGP-IEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKFGV 192
Cdd:cd08944    78 LDLLVNNAGAMHLTPaIIDTDLAVWDQTMAINLRGTFLCCRHAAPrMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAAI 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1270051604 193 EAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:cd08944   158 RNLTRTLAAELRHAGIRCNALAPGLIDTPLL 188
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 40-216 2.96e-20

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 88.66  E-value: 2.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKETykfVAQYLPENRGLWGLV 119
Cdd:PRK10538    3 VLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEM---LASLPAEWRNIDVLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 120 NNAGIA-KVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKFGVEAFSD 197
Cdd:PRK10538   80 NNAGLAlGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPgMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSL 159

                         170
                  ....*....|....*....
gi 1270051604 198 ALRRELGPTGVKVSIVEPG 216
Cdd:PRK10538  160 NLRTDLHGTAVRVTDIEPG 178
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 33-222 4.83e-20

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: 87.91  E-value: 4.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  33 TDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKrLTALHLDVTDSKEIKETykfVAQYLPen 112
Cdd:cd05351     3 LDFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPG-IEPVCVDLSDWDATEEA---LGSVGP-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 113 rgLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER--GRIINLASIGGRTCLPHASAYSISKF 190
Cdd:cd05351    77 --VDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvpGSIVNVSSQASQRALTNHTVYCSTKA 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1270051604 191 GVEAFSDALRRELGPTGVKVSIVEPGFFQTKI 222
Cdd:cd05351   155 ALDMLTKVMALELGPHKIRVNSVNPTVVMTDM 186
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 35-220 7.73e-20

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 87.47  E-value: 7.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFAT---CLTSEGQEN----LTAACSKRLTALHLDVTDSKEIKETYKFVAQ 107
Cdd:PRK12827    4 LDSRRVLITGGSGGLGRAIAVRLAADGADVIVLdihPMRGRAEADavaaGIEAAGGKALGLAFDVRDFAATRAALDAGVE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 108 ylpENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTK-VFLPLIKKER-GRIINLASIGGRTCLPHASAY 185
Cdd:PRK12827   84 ---EFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQaALPPMIRARRgGRIVNIASVAGVRGNRGQVNY 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1270051604 186 SISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK12827  161 AASKAGLIGLTKTLANELAPRGITVNAVAPGAINT 195
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 41-220 7.89e-20

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: 87.34  E-value: 7.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  41 LVTGCDSGFGRETALRLDSLGFNVFATCLTSEgQENLTAACSKRLTALHLDVTDSKEIKETYKF-VAQYLPenrgLWGLV 119
Cdd:cd05371     6 VVTGGASGLGLATVERLLAQGAKVVILDLPNS-PGETVAKLGDNCRFVPVDVTSEKDVKAALALaKAKFGR----LDIVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 120 NNAGIAKVGPI------EWQTIEEFKQIADVNLWGLIDVTKVFL-------PLIKKERGRIINLASIGGRTCLPHASAYS 186
Cdd:cd05371    81 NCAGIAVAAKTynkkgqQPHSLELFQRVINVNLIGTFNVIRLAAgamgknePDQGGERGVIINTASVAAFEGQIGQAAYS 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1270051604 187 ISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:cd05371   161 ASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDT 194
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
29-225 1.24e-19

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 87.10  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  29 EEFLTD---LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQE--NLTAACSKRLTALHLDVTDSKEIKEtyk 103
Cdd:PRK06935    4 DKFSMDffsLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWDEtrRLIEKEGRKVTFVQVDLTKPESAEK--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 104 fVAQYLPENRG-LWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLI----DVTKVFlplIKKERGRIINLASI----G 174
Cdd:PRK06935   81 -VVKEALEEFGkIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYhlsqAVAKVM---AKQGSGKIINIASMlsfqG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1270051604 175 GRTcLPhasAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNP 225
Cdd:PRK06935  157 GKF-VP---AYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAP 203
PRK08589 PRK08589
SDR family oxidoreductase;
35-253 1.89e-19

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 86.76  E-value: 1.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK--RLTALHLDVTDSKEIKEtykFVAQYLPEN 112
Cdd:PRK08589    4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDKIKSNggKAKAYHVDISDEQQVKD---FASEIKEQF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 113 RGLWGLVNNAGI-AKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHASAYSISKFG 191
Cdd:PRK08589   81 GRVDVLFNNAGVdNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAADLYRSGYNAAKGA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270051604 192 VEAFSDALRRELGPTGVKVSIVEPGFFQTKITnpDNLKGqwqelwanlnhSLKEEYGEKFYE 253
Cdd:PRK08589  161 VINFTKSIAIEYGRDGIRANAIAPGTIETPLV--DKLTG-----------TSEDEAGKTFRE 209
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 38-232 2.62e-19

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: 85.82  E-value: 2.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVF------ATCLTSEGQENLTAACSKRLTAlhlDVTDSKEIketykfvAQYLPE 111
Cdd:cd05323     1 KVAIITGGASGIGLATAKLLLKKGAKVAildrneNPGAAAELQAINPKVKATFVQC---DVTSWEQL-------AAAFKK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 NRGLWG----LVNNAGIAKvGPIEWQTIEEFKQIA---DVNLWGLIDVTKVFLPLIKKER----GRIINLASIGGRTCLP 180
Cdd:cd05323    71 AIEKFGrvdiLINNAGILD-EKSYLFAGKLPPPWEktiDVNLTGVINTTYLALHYMDKNKggkgGVIVNIGSVAGLYPAP 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1270051604 181 HASAYSISKFGVEAFSDALRREL-GPTGVKVSIVEPGFFQTKITNPDNLKGQW 232
Cdd:cd05323   150 QFPVYSASKHGVVGFTRSLADLLeYKTGVRVNAICPGFTNTPLLPDLVAKEAE 202
PRK08219 PRK08219
SDR family oxidoreductase;
40-216 3.53e-19

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 84.98  E-value: 3.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLdSLGFNVFATCLTSEGQENLTAACSkRLTALHLDVTDSKEIketykfvAQYLPENRGLWGLV 119
Cdd:PRK08219    6 ALITGASRGIGAAIAREL-APTHTLLLGGRPAERLDELAAELP-GATPFPVDLTDPEAI-------AAAVEQLGRLDVLV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 120 NNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHASAYSISKFGVEAFSDAL 199
Cdd:PRK08219   77 HNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRANPGWGSYAASKFALRALADAL 156

                         170
                  ....*....|....*..
gi 1270051604 200 RRElGPTGVKVSIVEPG 216
Cdd:PRK08219  157 REE-EPGNVRVTSVHPG 172
PRK07775 PRK07775
SDR family oxidoreductase;
40-237 4.50e-19

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 85.96  E-value: 4.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNV------------FATCLTSEGQENLtaacskrltALHLDVTDSKEIKEtykFVAQ 107
Cdd:PRK07775   13 ALVAGASSGIGAATAIELAAAGFPValgarrvekceeLVDKIRADGGEAV---------AFPLDVTDPDSVKS---FVAQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 108 YLPENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYS 186
Cdd:PRK07775   81 AEEALGEIEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPgMIERRRGDLIFVGSDVALRQRPHMGAYG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1270051604 187 ISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKI--TNPDNLKGQWQELWA 237
Cdd:PRK07775  161 AAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGMgwSLPAEVIGPMLEDWA 213
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 35-226 4.61e-19

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


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 85.51  E-value: 4.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK----RLTALHLDVTDSKEIKetyKFVAQYLP 110
Cdd:cd05358     1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEDAAEEVVEEIKavggKAIAVQADVSKEEDVV---ALFQSAIK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 ENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER--GRIINLASIGGRTCLPHASAYSIS 188
Cdd:cd05358    78 EFGTLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKikGKIINMSSVHEKIPWPGHVNYAAS 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1270051604 189 KFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNPD 226
Cdd:cd05358   158 KGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEA 195
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 34-229 4.76e-19

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 85.35  E-value: 4.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKetyKFVAQYLPENR 113
Cdd:PRK12936    3 DLSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANLSDRDEVK---ALGQKAEADLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 GLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFL-PLIKKERGRIINLASIGGRTCLPHASAYSISKFGV 192
Cdd:PRK12936   80 GVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELThPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGM 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1270051604 193 EAFSDALRRELGPTGVKVSIVEPGFFQTKITNPDNLK 229
Cdd:PRK12936  160 IGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDK 196
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 35-225 5.35e-19

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: 85.19  E-value: 5.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFaTCltSEGQENLTAACSK------RLTALHLDVTDSKEIKETYKFVAQY 108
Cdd:cd05329     4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVY-TC--ARNQKELDECLTEwrekgfKVEGSVCDVSSRSERQELMDTVASH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 LPENRGLwgLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKK-ERGRIINLASIGGRTCLPHASAYSI 187
Cdd:cd05329    81 FGGKLNI--LVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKAsGNGNIVFISSVAGVIAVPSGAPYGA 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1270051604 188 SKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNP 225
Cdd:cd05329   159 TKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEP 196
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-223 6.53e-19

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 85.01  E-value: 6.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKR---LTALHLDVTDSKEIKETYKFVAQYLp 110
Cdd:PRK08217    2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALgteVRGYAANVTDEEDVEATFAQIAEDF- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 enRGLWGLVNNAGI--------AKVGPIEWQ-TIEEFKQIADVNLwglidvTKVFL-------PLIK-KERGRIINLASI 173
Cdd:PRK08217   81 --GQLNGLINNAGIlrdgllvkAKDGKVTSKmSLEQFQSVIDVNL------TGVFLcgreaaaKMIEsGSKGVIINISSI 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1270051604 174 GgRTCLPHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:PRK08217  153 A-RAGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMT 201
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 35-229 8.79e-19

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: 84.49  E-value: 8.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK-----RLTALHLDVTDSKEIKetyKFVAQYL 109
Cdd:cd05330     1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEiapdaEVLLIKADVSDEAQVE---AYVDATV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 110 PENRGLWGLVNNAGI-AKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSI 187
Cdd:cd05330    78 EQFGRIDGFFNNAGIeGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGsGMIVNTASVGGIRGVGNQSGYAA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1270051604 188 SKFGVEAFSDALRRELGPTGVKVSIVEPGFFQT-------KITNPDNLK 229
Cdd:cd05330   158 AKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTpmvegslKQLGPENPE 206
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 34-215 1.30e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 83.94  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKETykfVAQYLPENR 113
Cdd:PRK06841   12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAA---VAAVISAFG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 GLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKFGV 192
Cdd:PRK06841   89 RIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRhMIAAGGGKIVNLASQAGVVALERHVAYCASKAGV 168

                         170       180
                  ....*....|....*....|...
gi 1270051604 193 EAFSDALRRELGPTGVKVSIVEP 215
Cdd:PRK06841  169 VGMTKVLALEWGPYGITVNAISP 191
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
35-290 2.62e-18

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 86.05  E-value: 2.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTAL--HLDVTDSKEIKETY-KFVAQYlpe 111
Cdd:PRK08324  420 LAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPDRALgvACDVTDEAAVQAAFeEAALAF--- 496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 nRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKE--RGRIINLASIGGRTCLPHASAYSISK 189
Cdd:PRK08324  497 -GGVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQglGGSIVFIASKNAVNPGPNFGAYGAAK 575

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 190 fgveAFSDALRR----ELGPTGVKVSIVepgffqtkitNPDNL---KGQWQELWANL---NHSLKEEYGEKFYETsvKNM 259
Cdd:PRK08324  576 ----AAELHLVRqlalELGPDGIRVNGV----------NPDAVvrgSGIWTGEWIEAraaAYGLSEEELEEFYRA--RNL 639

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1270051604 260 LTgmVDTCASpylyKVVDAIVHSLTSRYPKT 290
Cdd:PRK08324  640 LK--REVTPE----DVAEAVVFLASGLLSKT 664
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 39-216 8.15e-18

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


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 81.56  E-value: 8.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  39 YVLVTGCDSGFGRETALRLDSLGFNVFATCLT-SEGQENLTAA---CSKRLTALHLDVTDSKEIKETYkfvaQYLPENRG 114
Cdd:cd05367     1 VIILTGASRGIGRALAEELLKRGSPSVVVLLArSEEPLQELKEelrPGLRVTTVKADLSDAAGVEQLL----EAIRKLDG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 115 -LWGLVNNAG-IAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER--GRIINLASIGGRTCLPHASAYSISKF 190
Cdd:cd05367    77 eRDLLINNAGsLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGlkKTVVNVSSGAAVNPFKGWGLYCSSKA 156

                         170       180
                  ....*....|....*....|....*.
gi 1270051604 191 GVEAFSDALRRELgpTGVKVSIVEPG 216
Cdd:cd05367   157 ARDMFFRVLAAEE--PDVRVLSYAPG 180
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 32-231 1.17e-17

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 81.20  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  32 LTDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTS-EGQENLTAACSKR---LTALHLDVTDSKEIKetykfvaQ 107
Cdd:PRK12935    1 MVQLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSkEAAENLVNELGKEghdVYAVQADVSKVEDAN-------R 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 108 YLPENRGLWG----LVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHA 182
Cdd:PRK12935   74 LVEEAVNHFGkvdiLVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPyITEAEEGRIISISSIIGQAGGFGQ 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1270051604 183 SAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITN--PDNLKGQ 231
Cdd:PRK12935  154 TNYSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAevPEEVRQK 204
PRK12743 PRK12743
SDR family oxidoreductase;
41-227 1.24e-17

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 81.23  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  41 LVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTA----ACSKRLTALHLDVTDskeIKETYKFVAQYLPENRGLW 116
Cdd:PRK12743    6 IVTASDSGIGKACALLLAQQGFDIGITWHSDEEGAKETAeevrSHGVRAEIRQLDLSD---LPEGAQALDKLIQRLGRID 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 117 GLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGlidvtkVFL-------PLIKKER-GRIINLASIGGRTCLPHASAYSIS 188
Cdd:PRK12743   83 VLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDG------AFLcsqiaarHMVKQGQgGRIINITSVHEHTPLPGASAYTAA 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1270051604 189 KFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNPDN 227
Cdd:PRK12743  157 KHALGGLTKAMALELVEHGILVNAVAPGAIATPMNGMDD 195
PRK07063 PRK07063
SDR family oxidoreductase;
35-223 2.15e-17

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 80.87  E-value: 2.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK-----RLTALHLDVTDSKEIKETykfVAQYL 109
Cdd:PRK07063    5 LAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARdvagaRVLAVPADVTDAASVAAA---VAAAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 110 PENRGLWGLVNNAGIAKVG-PIEwQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSI 187
Cdd:PRK07063   82 EAFGPLDVLVNNAGINVFAdPLA-MTDEDWRRCFAVDLDGAWNGCRAVLPgMVERGRGSIVNIASTHAFKIIPGCFPYPV 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1270051604 188 SKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:PRK07063  161 AKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLT 196
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 38-290 2.35e-17

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: 80.51  E-value: 2.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHL--DVTDSKEIKETY-KFVAQYlpenRG 114
Cdd:cd08943     2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQGGPRALGVqcDVTSEAQVQSAFeQAVLEF----GG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 115 LWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER--GRIINLASIGGRTCLPHASAYSISKfgv 192
Cdd:cd08943    78 LDIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGigGNIVFNASKNAVAPGPNAAAYSAAK--- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 193 eAFSDALRR----ELGPTGVKVSIVEP-GFFQTKITnpdnlkgqWQELWANlNHSLKEEYGEKFYETsvKNMLTgmVDTC 267
Cdd:cd08943   155 -AAEAHLARclalEGGEDGIRVNTVNPdAVFRGSKI--------WEGVWRA-ARAKAYGLLEEEYRT--RNLLK--REVL 220

                         250       260
                  ....*....|....*....|...
gi 1270051604 268 ASpylyKVVDAIVHSLTSRYPKT 290
Cdd:cd08943   221 PE----DVAEAVVAMASEDFGKT 239
PRK07069 PRK07069
short chain dehydrogenase; Validated
 41-225 2.67e-17

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 80.52  E-value: 2.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  41 LVTGCDSGFGRETALRLDSLGFNVFatcLTSEGQENLTAACSKRLTALH---------LDVTDSKEIKETykfVAQYLPE 111
Cdd:PRK07069    3 FITGAAGGLGRAIARRMAEQGAKVF---LTDINDAAGLDAFAAEINAAHgegvafaavQDVTDEAQWQAL---LAQAADA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 NRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISKF 190
Cdd:PRK07069   77 MGGLSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQpASIVNISSVAAFKAEPDYTAYNASKA 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1270051604 191 GVEAFS-----DALRRELgptGVKVSIVEPGFFQTKITNP 225
Cdd:PRK07069  157 AVASLTksialDCARRGL---DVRCNSIHPTFIRTGIVDP 193
PRK06124 PRK06124
SDR family oxidoreductase;
34-224 2.97e-17

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 80.14  E-value: 2.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK---RLTALHLDVTDSKEIKETYkfvAQYLP 110
Cdd:PRK06124    8 SLAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAaggAAEALAFDIADEEAVAAAF---ARIDA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 ENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISK 189
Cdd:PRK06124   85 EHGRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGyGRIIAITSIAGQVARAGDAVYPAAK 164

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPGFFQTKiTN 224
Cdd:PRK06124  165 QGLTGLMRALAAEFGPHGITSNAIAPGYFATE-TN 198
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 38-224 3.41e-17

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: 80.35  E-value: 3.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQEnlTAACS-------KRLTALHLDVTDSKEIKetyKFVAQYLP 110
Cdd:cd05327     2 KVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGE--EAAAEikketgnAKVEVIQLDLSSLASVR---QFAEEFLA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 ENRGLWGLVNNAGIAKVGpiEWQTIEEF-KQIAdVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRT--------CLP 180
Cdd:cd05327    77 RFPRLDILINNAGIMAPP--RRLTKDGFeLQFA-VNYLGHFLLTNLLLPVLKASApSRIVNVSSIAHRAgpidfndlDLE 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1270051604 181 HAS------AYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITN 224
Cdd:cd05327   154 NNKeyspykAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLR 203
PRK06138 PRK06138
SDR family oxidoreductase;
34-225 3.50e-17

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 80.20  E-value: 3.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK--RLTALHLDVTDSKEIKETYKFVAqylpe 111
Cdd:PRK06138    2 RLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAggRAFARQGDVGSAEAVEALVDFVA----- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 nrGLWG----LVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYS 186
Cdd:PRK06138   77 --ARWGrldvLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPiMQRQGGGSIVNTASQLALAGGRGRAAYV 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1270051604 187 ISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNP 225
Cdd:PRK06138  155 ASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRR 193
PRK06947 PRK06947
SDR family oxidoreductase;
38-222 4.29e-17

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 79.85  E-value: 4.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK----RLTALHLDVTDSKEIKETYKFVAQYLPenr 113
Cdd:PRK06947    3 KVVLITGASRGIGRATAVLAAARGWSVGINYARDAAAAEETADAVRaaggRACVVAGDVANEADVIAMFDAVQSAFG--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 GLWGLVNNAGI-AKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERG----RIINLASIGGRTCLPHASA-YSI 187
Cdd:PRK06947   80 RLDALVNNAGIvAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGgrggAIVNVSSIASRLGSPNEYVdYAG 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1270051604 188 SKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKI 222
Cdd:PRK06947  160 SKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEI 194
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 38-221 4.55e-17

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: 79.55  E-value: 4.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKET-YKFVAQYlpenRGLW 116
Cdd:cd09761     2 KVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVvYAMLEKL----GRID 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 117 GLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHASAYSISKFGVEAFS 196
Cdd:cd09761    78 VLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAFQSEPDSEAYAASKGGLVALT 157

                         170       180
                  ....*....|....*....|....*
gi 1270051604 197 DALRRELGPTgVKVSIVEPGFFQTK 221
Cdd:cd09761   158 HALAMSLGPD-IRVNCISPGWINTT 181
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 38-220 5.07e-17

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: 79.44  E-value: 5.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAacSKRLTALHLDVTDSKEIKETYKfvaqylpENRGLWG 117
Cdd:cd05368     3 KVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELER--GPGITTRVLDVTDKEQVAALAK-------EEGRIDV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 118 LVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGR-TCLPHASAYSISKFGVEAF 195
Cdd:cd05368    74 LFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPkMLARKDGSIINMSSVASSiKGVPNRFVYSTTKAAVIGL 153

                         170       180
                  ....*....|....*....|....*
gi 1270051604 196 SDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:cd05368   154 TKSVAADFAQQGIRCNAICPGTVDT 178
PRK06194 PRK06194
hypothetical protein; Provisional
 32-223 5.36e-17

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 80.06  E-value: 5.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  32 LTDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTA---ACSKRLTALHLDVTDSKEI----KETYK- 103
Cdd:PRK06194    1 MKDFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAelrAQGAEVLGVRTDVSDAAQVealaDAALEr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 104 FVAQYLpenrglwgLVNNAGIAKVGPIeWQ-TIEEFKQIADVNLWGLIDVTKVFLPLI----KKE---RGRIINLASIGG 175
Cdd:PRK06194   81 FGAVHL--------LFNNAGVGAGGLV-WEnSLADWEWVLGVNLWGVIHGVRAFTPLMlaaaEKDpayEGHIVNTASMAG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1270051604 176 RTCLPHASAYSISKFGVEAFSDALRRELGPTG--VKVSIVEPGFFQTKIT 223
Cdd:PRK06194  152 LLAPPAMGIYNVSKHAVVSLTETLYQDLSLVTdqVGASVLCPYFVPTGIW 201
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 38-220 5.93e-17

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: 79.48  E-value: 5.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKR----LTALHLDVTDSKEIKETYKFVaqylpenR 113
Cdd:cd05343     7 RVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAgyptLFPYQCDLSNEEQILSMFSAI-------R 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 GLWG----LVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKK---ERGRIINLASIGGRT--CLPHASA 184
Cdd:cd05343    80 TQHQgvdvCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKErnvDDGHIININSMSGHRvpPVSVFHF 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1270051604 185 YSISKFGVEAFSDALRREL--GPTGVKVSIVEPGFFQT 220
Cdd:cd05343   160 YAATKHAVTALTEGLRQELreAKTHIRATSISPGLVET 197
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 34-225 6.27e-17

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 79.72  E-value: 6.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALH---LDVTDSKEIKEtykFVAQYLP 110
Cdd:PRK07097    7 SLKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHgyvCDVTDEDGVQA---MVSQIEK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 ENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIG---GRTCLphaSAYS 186
Cdd:PRK07097   84 EVGVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPsMIKKGHGKIINICSMMselGRETV---SAYA 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1270051604 187 ISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNP 225
Cdd:PRK07097  161 AAKGGLKMLTKNIASEYGEANIQCNGIGPGYIATPQTAP 199
PRK05867 PRK05867
SDR family oxidoreductase;
32-233 1.11e-16

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 78.54  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  32 LTDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLT---AACSKRLTALHLDVTDSKEIKetyKFVAQY 108
Cdd:PRK05867    4 LFDLHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLAdeiGTSGGKVVPVCCDVSQHQQVT---SMLDQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 LPENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNlwglidVTKVFL-------PLIKKER-GRIINLASIGGRTC-L 179
Cdd:PRK05867   81 TAELGGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTN------VTGVFLtaqaaakAMVKQGQgGVIINTASMSGHIInV 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1270051604 180 P-HASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNP-DNLKGQWQ 233
Cdd:PRK05867  155 PqQVSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEPyTEYQPLWE 210
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 35-217 2.11e-16

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 78.08  E-value: 2.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVfatCLTSEGQENLTAACSK------RLTALHLDVTDSKEIKetyKFVAQY 108
Cdd:PRK07890    3 LKGKVVVVSGVGPGLGRTLAVRAARAGADV---VLAARTAERLDEVAAEiddlgrRALAVPTDITDEDQCA---NLVALA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 LPENRGLWGLVNNA-GIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHASAYSI 187
Cdd:PRK07890   77 LERFGRVDALVNNAfRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMINSMVLRHSQPKYGAYKM 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1270051604 188 SKFGVEAFSDALRRELGPTGVKVSIVEPGF 217
Cdd:PRK07890  157 AKGALLAASQSLATELGPQGIRVNSVAPGY 186
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 35-215 2.68e-16

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: 77.43  E-value: 2.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKETykfVAQYLPENRG 114
Cdd:cd05345     3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAM---VEAALSKFGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 115 LWGLVNNAGIA-KVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISKFGV 192
Cdd:cd05345    80 LDILVNNAGIThRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGgGVIINIASTAGLRPRPGLTWYNASKGWV 159

                         170       180
                  ....*....|....*....|...
gi 1270051604 193 EAFSDALRRELGPTGVKVSIVEP 215
Cdd:cd05345   160 VTATKAMAVELAPRNIRVNCLCP 182
PRK06172 PRK06172
SDR family oxidoreductase;
34-220 2.84e-16

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 77.48  E-value: 2.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCL-TSEGQEnlTAACSKRL----TALHLDVTDSKEIKETY-KFVAQ 107
Cdd:PRK06172    4 TFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRdAAGGEE--TVALIREAggeaLFVACDVTRDAEVKALVeQTIAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 108 YlpeNRgLWGLVNNAGIA-KVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAY 185
Cdd:PRK06172   82 Y---GR-LDYAFNNAGIEiEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPlMLAQGGGAIVNTASVAGLGAAPKMSIY 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1270051604 186 SISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK06172  158 AASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDT 192
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 35-249 4.02e-16

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: 77.18  E-value: 4.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQEnLTAACSKRLTALHLDVTDSKEIKETYKFVAQYLPENRG 114
Cdd:cd08937     2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHE-VLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 115 LWGLVNNAG---IAKvgPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTClpHASAYSISKF 190
Cdd:cd08937    81 VDVLINNVGgtiWAK--PYEHYEEEQIEAEIRRSLFPTLWCCRAVLPhMLERQQGVIVNVSSIATRGI--YRIPYSAAKG 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270051604 191 GVEAFSDALRRELGPTGVKVSIVEPGFFQTK----ITNPDNLKGQWQELW-----ANLNHSLKEEYGE 249
Cdd:cd08937   157 GVNALTASLAFEHARDGIRVNAVAPGGTEAPprkiPRNAAPMSEQEKVWYqrivdQTLDSSLMGRYGT 224
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 38-222 4.41e-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: 77.12  E-value: 4.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAAC-----SKRLTALHLDVTDSKEIKEtykFVAQYLPEN 112
Cdd:cd09807     2 KTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIrrdtlNHEVIVRHLDLASLKSIRA---FAAEFLAEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 113 RGLWGLVNNAGIAKVgPiEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKK-ERGRIINLASI---GGRTCLP-------- 180
Cdd:cd09807    79 DRLDVLINNAGVMRC-P-YSKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKsAPSRIVNVSSLahkAGKINFDdlnseksy 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1270051604 181 -HASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKI 222
Cdd:cd09807   157 nTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTEL 199
PRK06500 PRK06500
SDR family oxidoreductase;
35-220 5.27e-16

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 76.53  E-value: 5.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKEtykfVAQYLPENRG 114
Cdd:PRK06500    4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAAQKA----LAQALAEAFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 115 -LWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINlASIGGRTCLPHASAYSISKFGVE 193
Cdd:PRK06500   80 rLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPASIVLN-GSINAHIGMPNSSVYAASKAALL 158

                         170       180
                  ....*....|....*....|....*..
gi 1270051604 194 AFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK06500  159 SLAKTLSGELLPRGIRVNAVSPGPVQT 185
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 34-216 6.32e-16

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 76.59  E-value: 6.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENltaacsKRLTALHLDVTDSKEIKETykfVAQYLPENR 113
Cdd:PRK06171    6 NLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQH------ENYQFVPTDVSSAEEVNHT---VAEIIEKFG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 GLWGLVNNAGI----------AKVGPIEWQTiEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHA 182
Cdd:PRK06171   77 RIDGLVNNAGIniprllvdekDPAGKYELNE-AAFDKMFNINQKGVFLMSQAVARqMVKQHDGVIVNMSSEAGLEGSEGQ 155

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1270051604 183 SAYSISKFGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:PRK06171  156 SCYAATKAALNSFTRSWAKELGKHNIRVVGVAPG 189
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
35-227 6.97e-16

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 76.38  E-value: 6.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK--RLTALHLDVTDSKEIKETYKfvAQYLPEN 112
Cdd:PRK08226    4 LTGKTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADELCGRghRCTAVVADVRDPASVAAAIK--RAKEKEG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 113 RgLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCL-PHASAYSISKF 190
Cdd:PRK08226   82 R-IDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPeMIARKDGRIVMMSSVTGDMVAdPGETAYALTKA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1270051604 191 GVEAFSDALRRELGPTGVKVSIVEPGFFQTKI-------TNPDN 227
Cdd:PRK08226  161 AIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMaesiarqSNPED 204
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 35-221 9.66e-16

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 75.70  E-value: 9.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVfatCLTSEGQENLTAACSK-------RLTALHLDVTDSKEIKETykfVAQ 107
Cdd:cd05369     1 LKGKVAFITGGGTGIGKAIAKAFAELGASV---AIAGRKPEVLEAAAEEissatggRAHPIQCDVRDPEAVEAA---VDE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 108 YLPENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKER-GRIINLASIGGRTCLP---HA 182
Cdd:cd05369    75 TLKEFGKIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKrLIEAKHgGSILNISATYAYTGSPfqvHS 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1270051604 183 SAysiSKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTK 221
Cdd:cd05369   155 AA---AKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTT 190
PRK06949 PRK06949
SDR family oxidoreductase;
34-222 1.19e-15

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 75.95  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALH---LDVTDSKEIKETykfVAQYLP 110
Cdd:PRK06949    6 NLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGAAHvvsLDVTDYQSIKAA---VAHAET 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 ENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLI----DVTKVFLPLIK-----KERGRIINLASIGGRTCLPH 181
Cdd:PRK06949   83 EAGTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFfvaqEVAKRMIARAKgagntKPGGRIINIASVAGLRVLPQ 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1270051604 182 ASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKI 222
Cdd:PRK06949  163 IGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEI 203
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 35-229 1.88e-15

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 74.91  E-value: 1.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFatcLTSEGQENLTA-------ACSKRLTALHLDVTDSKEikETYKFVAQ 107
Cdd:PRK08945   10 LKDRIILVTGAGDGIGREAALTYARHGATVI---LLGRTEEKLEAvydeieaAGGPQPAIIPLDLLTATP--QNYQQLAD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 108 YLPENRG-LWGLVNNAGI-AKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKK-ERGRIINLASIGGRTCLPHASA 184
Cdd:PRK08945   85 TIEEQFGrLDGVLHNAGLlGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKsPAASLVFTSSSVGRQGRANWGA 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1270051604 185 YSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKI-------TNPDNLK 229
Cdd:PRK08945  165 YAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAMrasafpgEDPQKLK 216
PRK06398 PRK06398
aldose dehydrogenase; Validated
 34-220 2.51e-15

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 74.87  E-value: 2.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLtSEGQENltaacskRLTALHLDVTDSKEIKETYKFVA-QYlpeN 112
Cdd:PRK06398    3 GLKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDI-KEPSYN-------DVDYFKVDVSNKEQVIKGIDYVIsKY---G 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 113 RgLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKFG 191
Cdd:PRK06398   72 R-IDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPyMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHA 150

                         170       180
                  ....*....|....*....|....*....
gi 1270051604 192 VEAFSDALRRELGPTgVKVSIVEPGFFQT 220
Cdd:PRK06398  151 VLGLTRSIAVDYAPT-IRCVAVCPGSIRT 178
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 40-220 2.73e-15

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: 74.31  E-value: 2.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNVFATCLTS-EGQENLTAACSK---RLTALHLDVTDSKEIKEtykFVAQYLPENRGL 115
Cdd:cd05359     1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSkDAAAEVAAEIEElggKAVVVRADVSQPQDVEE---MFAAVKERFGRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISKFGVEA 194
Cdd:cd05359    78 DVLVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGgGRIVAISSLGSIRALPNYLAVGTAKAALEA 157

                         170       180
                  ....*....|....*....|....*.
gi 1270051604 195 FSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:cd05359   158 LVRYLAVELGPRGIRVNAVSPGVIDT 183
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
35-228 3.32e-15

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 74.28  E-value: 3.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRL----TALHLDVTDSKEIKETYKFVAQYLP 110
Cdd:PRK12938    1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRRVKWLEDQKALgfdfIASEGNVGDWDSTKAAFDKVKAEVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 EnrgLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTK-VFLPLIKKERGRIINLASIGGRTCLPHASAYSISK 189
Cdd:PRK12938   81 E---IDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKqVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAK 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPGFFQT---KITNPDNL 228
Cdd:PRK12938  158 AGIHGFTMSLAQEVATKGVTVNTVSPGYIGTdmvKAIRPDVL 199
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 35-216 4.49e-15

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: 74.25  E-value: 4.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQ-----ENLTAACSKRLTALHLDVTDSKEIKETYKFVAQyl 109
Cdd:cd05355    24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEDdaeetKKLIEEEGRKCLLIPGDLGDESFCRDLVKEVVK-- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 110 pENRGLWGLVNNAGIAKVGP-IEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKeRGRIINLASIGGRTCLPHASAYSIS 188
Cdd:cd05355   102 -EFGKLDILVNNAAYQHPQEsIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKK-GSSIINTTSVTAYKGSPHLLDYAAT 179

                         170       180
                  ....*....|....*....|....*...
gi 1270051604 189 KFGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:cd05355   180 KGAIVAFTRGLSLQLAEKGIRVNAVAPG 207
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 40-228 5.16e-15

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: 72.55  E-value: 5.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGfnvfatcltsegqenltaacskrltALHLDVTDSKEIketykfvaqylpenrglwgLV 119
Cdd:cd02266     1 VLVTGGSGGIGGAIARWLASRG-------------------------SPKVLVVSRRDV-------------------VV 36

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 120 NNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISKFGVEAFSDA 198
Cdd:cd02266    37 HNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRlGRFILISSVAGLFGAPGLGGYAASKAALDGLAQQ 116

                         170       180       190
                  ....*....|....*....|....*....|
gi 1270051604 199 LRRELGPTGVKVSIVEPGFFQTKITNPDNL 228
Cdd:cd02266   117 WASEGWGNGLPATAVACGTWAGSGMAKGPV 146
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 41-230 5.37e-15

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 74.22  E-value: 5.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  41 LVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKETYKFVAQYLPENRGLWGLVN 120
Cdd:PRK05876   10 VITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDVVFS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 121 NAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP--LIKKERGRIINLASIGGrtCLPHA--SAYSISKFGVEAFS 196
Cdd:PRK05876   90 NAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPrlLEQGTGGHVVFTASFAG--LVPNAglGAYGVAKYGVVGLA 167

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1270051604 197 DALRRELGPTGVKVSIVEPGFFQTK-ITNPDNLKG 230
Cdd:PRK05876  168 ETLAREVTADGIGVSVLCPMVVETNlVANSERIRG 202
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 35-216 7.71e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 73.91  E-value: 7.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAAC----SKRLTALHLDVTDSKEIKETykfVAQYLP 110
Cdd:PRK06701   44 LKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDANETKQRvekeGVKCLLIPGDVSDEAFCKDA---VEETVR 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 ENRGLWGLVNNAGIAK-VGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKErGRIINLASIGGRTCLPHASAYSISK 189
Cdd:PRK06701  121 ELGRLDILVNNAAFQYpQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLKQG-SAIINTGSITGYEGNETLIDYSATK 199

                         170       180
                  ....*....|....*....|....*..
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:PRK06701  200 GAIHAFTRSLAQSLVQKGIRVNAVAPG 226
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 35-229 1.63e-14

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


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 72.22  E-value: 1.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLT------AACSKRLTALHLDVTDSKEIKETYKFVAQY 108
Cdd:cd05340     2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVAdhineeGGRQPQWFILDLLTCTSENCQQLAQRIAVN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 LPEnrgLWGLVNNAG-IAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKK-ERGRIINLASIGGRTCLPHASAYS 186
Cdd:cd05340    82 YPR---LDGVLHNAGlLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKsDAGSLVFTSSSVGRQGRANWGAYA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1270051604 187 ISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKI-------TNPDNLK 229
Cdd:cd05340   159 VSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMrasafptEDPQKLK 208
PRK06101 PRK06101
SDR family oxidoreductase;
40-224 1.84e-14

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 72.21  E-value: 1.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNVFAtCLTSEGQENLTAACSKRLTALHLDVTDSKEIKETYKfVAQYLPENrglWglV 119
Cdd:PRK06101    4 VLITGATSGIGKQLALDYAKQGWQVIA-CGRNQSVLDELHTQSANIFTLAFDVTDHPGTKAALS-QLPFIPEL---W--I 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 120 NNAGIAKV---GPIEWQTIEefkQIADVNLWGLIDVTKVFLPLIkkERG-RIINLASIGGRTCLPHASAYSISKFGVEAF 195
Cdd:PRK06101   77 FNAGDCEYmddGKVDATLMA---RVFNVNVLGVANCIEGIQPHL--SCGhRVVIVGSIASELALPRAEAYGASKAAVAYF 151

                         170       180
                  ....*....|....*....|....*....
gi 1270051604 196 SDALRRELGPTGVKVSIVEPGFFQTKITN 224
Cdd:PRK06101  152 ARTLQLDLRPKGIEVVTVFPGFVATPLTD 180
PRK07074 PRK07074
SDR family oxidoreductase;
40-221 1.89e-14

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 72.49  E-value: 1.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACS-KRLTALHLDVTDSKEIKETykfVAQYLPENRGLWGL 118
Cdd:PRK07074    5 ALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGdARFVPVACDLTDAASLAAA---LANAAAERGPVDVL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 119 VNNAGIAKVGPIEWQTIEEFKQIADVNLWG-LIDVTKVFLPLIKKERGRIINLASIGGRTCLPHAsAYSISKFGVEAFSD 197
Cdd:PRK07074   82 VANAGAARAASLHDTTPASWRADNALNLEAaYLCVEAVLEGMLKRSRGAVVNIGSVNGMAALGHP-AYSAAKAGLIHYTK 160

                         170       180
                  ....*....|....*....|....
gi 1270051604 198 ALRRELGPTGVKVSIVEPGFFQTK 221
Cdd:PRK07074  161 LLAVEYGRFGIRANAVAPGTVKTQ 184
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 34-226 2.00e-14

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


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 72.49  E-value: 2.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTA---ACSKRLTALHLDVTDSKEIKETYK-FVAQyl 109
Cdd:cd08935     2 SLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKeitALGGRAIALAADVLDRASLERAREeIVAQ-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 110 penrglWG----LVNNAG------IAKVGPIEWQTI--------EEFKQIADVNLWGLIDVTKVFL-PLIKKERGRIINL 170
Cdd:cd08935    80 ------FGtvdiLINGAGgnhpdaTTDPEHYEPETEqnffdldeEGWEFVFDLNLNGSFLPSQVFGkDMLEQKGGSIINI 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1270051604 171 ASIGGRTCLPHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTK-----ITNPD 226
Cdd:cd08935   154 SSMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPqnrklLINPD 214
PRK06114 PRK06114
SDR family oxidoreductase;
32-220 2.06e-14

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 72.12  E-value: 2.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  32 LTDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTA----ACSKRLTALHLDVTDSKEIKETykfVAQ 107
Cdd:PRK06114    3 LFDLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETAehieAAGRRAIQIAADVTSKADLRAA---VAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 108 YLPENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGlidvtkVFLP-------LIKKERGRIINLASIGG----R 176
Cdd:PRK06114   80 TEAELGALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTG------VFLScqaearaMLENGGGSIVNIASMSGiivnR 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1270051604 177 TCLphASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK06114  154 GLL--QAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTAT 195
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
35-216 2.48e-14

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 71.98  E-value: 2.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKetyKFVAQYLPENRG 114
Cdd:PRK07067    4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSID---RIVAAAVERFGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 115 LWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTK-VFLPLIKKERG-RIINLASIGGRTCLPHASAYSISKFGV 192
Cdd:PRK07067   81 IDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQaVARHMVEQGRGgKIINMASQAGRRGEALVSHYCATKAAV 160

                         170       180
                  ....*....|....*....|....
gi 1270051604 193 EAFSDALRRELGPTGVKVSIVEPG 216
Cdd:PRK07067  161 ISYTQSAALALIRHGINVNAIAPG 184
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-226 4.05e-14

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 70.76  E-value: 4.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFAtcLTSEGQENLTaacsKRLTALHLDVTDskEIKETYKFVAQYLPenr 113
Cdd:PRK06550    2 EFMTKTVLITGAASGIGLAQARAFLAQGAQVYG--VDKQDKPDLS----GNFHFLQLDLSD--DLEPLFDWVPSVDI--- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 glwgLVNNAGIAK-VGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKFG 191
Cdd:PRK06550   71 ----LCNTAGILDdYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPqMLERKSGIIINMCSIASFVAGGGGAAYTASKHA 146

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1270051604 192 VEAFSDALRRELGPTGVKVSIVEPGFFQTKITNPD 226
Cdd:PRK06550  147 LAGFTKQLALDYAKDGIQVFGIAPGAVKTPMTAAD 181
PRK07774 PRK07774
SDR family oxidoreductase;
32-223 4.84e-14

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 70.93  E-value: 4.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  32 LTDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACS-KRLTALHLDVtDSKEIKETYKFVAQYLP 110
Cdd:PRK07774    1 MGRFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVaDGGTAIAVQV-DVSDPDSAKAMADATVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 ENRGLWGLVNNAGI---AKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGrtcLPHASAYS 186
Cdd:PRK07774   80 AFGGIDYLVNNAAIyggMKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKhMAKRGGGAIVNQSSTAA---WLYSNFYG 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1270051604 187 ISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:PRK07774  157 LAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEAT 193
PRK07201 PRK07201
SDR family oxidoreductase;
38-213 4.92e-14

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 73.06  E-value: 4.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFatcLTSEGQENLTAACSK------RLTALHLDVTDSKEIKetyKFVAQYLPE 111
Cdd:PRK07201  372 KVVLITGASSGIGRATAIKVAEAGATVF---LVARNGEALDELVAEirakggTAHAYTCDLTDSAAVD---HTVKDILAE 445

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 NRGLWGLVNNAGIAKVGPIEWQT--IEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSIS 188
Cdd:PRK07201  446 HGHVDYLVNNAGRSIRRSVENSTdrFHDYERTMAVNYFGAVRLILGLLPhMRERRFGHVVNVSSIGVQTNAPRFSAYVAS 525

                         170       180
                  ....*....|....*....|....*
gi 1270051604 189 KFGVEAFSDALRRELGPTGVKVSIV 213
Cdd:PRK07201  526 KAALDAFSDVAASETLSDGITFTTI 550
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 36-216 5.25e-14

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: 70.83  E-value: 5.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  36 QQKYVLVTGCDSGFGRETALRLDSLGFNVFatcLTSEGQENLTAAC-------SKRLTALHLDVTDSKEIKETYKfvaQY 108
Cdd:cd08930     1 EDKIILITGAAGLIGKAFCKALLSAGARLI---LADINAPALEQLKeeltnlyKNRVIALELDITSKESIKELIE---SY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 LPENRGLWGLVNNAGI---AKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKE-RGRIINLASIGG--------- 175
Cdd:cd08930    75 LEKFGRIDILINNAYPspkVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQgKGSIINIASIYGviapdfriy 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1270051604 176 RTCLPHASA-YSISKFGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:cd08930   155 ENTQMYSPVeYSVIKAGIIHLTKYLAKYYADTGIRVNAISPG 196
PRK06128 PRK06128
SDR family oxidoreductase;
35-220 9.79e-14

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 71.04  E-value: 9.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQE-----NLTAACSKRLTALHLDVTDSKEIKEtykFVAQYL 109
Cdd:PRK06128   53 LQGRKALITGADSGIGRATAIAFAREGADIALNYLPEEEQDaaevvQLIQAEGRKAVALPGDLKDEAFCRQ---LVERAV 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 110 PENRGLWGLVNNAGI-AKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKErGRIINLASIGGRTCLPHASAYSIS 188
Cdd:PRK06128  130 KELGGLDILVNIAGKqTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPG-ASIINTGSIQSYQPSPTLLDYAST 208

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1270051604 189 KFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK06128  209 KAAIVAFTKALAKQVAEKGIRVNAVAPGPVWT 240
PRK07062 PRK07062
SDR family oxidoreductase;
34-239 1.08e-13

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 70.07  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVfATCltSEGQENLTAACSK--------RLTALHLDVTDSKEIKEtykFV 105
Cdd:PRK07062    5 QLEGRVAVVTGGSSGIGLATVELLLEAGASV-AIC--GRDEERLASAEARlrekfpgaRLLAARCDVLDEADVAA---FA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 106 AQYLPENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKK-ERGRIINLASIGGRTCLPHASA 184
Cdd:PRK07062   79 AAVEARFGGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRAsAAASIVCVNSLLALQPEPHMVA 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 185 YSISKFGVEAFSDALRRELGPTGVKVS-----IVEPGFFQTKITNPDNLKGQWQELWANL 239
Cdd:PRK07062  159 TSAARAGLLNLVKSLATELAPKGVRVNsillgLVESGQWRRRYEARADPGQSWEAWTAAL 218
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 118-238 1.19e-13

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: 70.26  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 118 LVNNAGI-AKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHASAYSISKFGVEAFS 196
Cdd:cd08933    91 LVNNAGWhPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIGQKQAAPYVATKGAITAMT 170

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1270051604 197 DALRRELGPTGVKVSIVEPGFFQTKItnpdnlkgqWQELWAN 238
Cdd:cd08933   171 KALAVDESRYGVRVNCISPGNIWTPL---------WEELAAQ 203
PRK12746 PRK12746
SDR family oxidoreductase;
32-222 1.22e-13

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 70.06  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  32 LTDLQQKYVLVTGCDSGFGRETALRLDSLG--FNVFATCLTSEGQENLTAACSKRLTALHLDvTDSKEIKETYKFVAQYL 109
Cdd:PRK12746    1 MKNLDGKVALVTGASRGIGRAIAMRLANDGalVAIHYGRNKQAADETIREIESNGGKAFLIE-ADLNSIDGVKKLVEQLK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 110 PENRGLWG------LVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKErGRIINLASIGGRTCLPHAS 183
Cdd:PRK12746   80 NELQIRVGtseidiLVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAE-GRVINISSAEVRLGFTGSI 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1270051604 184 AYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKI 222
Cdd:PRK12746  159 AYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDI 197
PRK09242 PRK09242
SDR family oxidoreductase;
35-230 1.70e-13

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 69.39  E-value: 1.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENL-----TAACSKRLTALHLDVTDSKEIKETYKFVAQYL 109
Cdd:PRK09242    7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQArdelaEEFPEREVHGLAADVSDDEDRRAILDWVEDHW 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 110 penRGLWGLVNNAG--IAKVGpIEWqTIEEFKQIADVNLWGLIDVTKVFLPLIKK-ERGRIINLASIGGRTCLPHASAYS 186
Cdd:PRK09242   87 ---DGLHILVNNAGgnIRKAA-IDY-TEDEWRGIFETNLFSAFELSRYAHPLLKQhASSAIVNIGSVSGLTHVRSGAPYG 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1270051604 187 ISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT-----NPDNLKG 230
Cdd:PRK09242  162 MTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTsgplsDPDYYEQ 210
PRK07985 PRK07985
SDR family oxidoreductase;
35-216 2.68e-13

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 69.64  E-value: 2.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQE-----NLTAACSKRLTALHLDVTDSKEIKetyKFVAQYL 109
Cdd:PRK07985   47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISYLPVEEEDaqdvkKIIEECGRKAVLLPGDLSDEKFAR---SLVHEAH 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 110 PENRGLWGLVNNAGI-AKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKErGRIINLASIGGRTCLPHASAYSIS 188
Cdd:PRK07985  124 KALGGLDIMALVAGKqVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPKG-ASIITTSSIQAYQPSPHLLDYAAT 202

                         170       180
                  ....*....|....*....|....*...
gi 1270051604 189 KFGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:PRK07985  203 KAAILNYSRGLAKQVAEKGIRVNIVAPG 230
PRK07577 PRK07577
SDR family oxidoreductase;
38-222 3.23e-13

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 68.21  E-value: 3.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFAtcLTSEGQENLTA---ACskrltalhlDVTDSKEIKETykfVAQYLpENRG 114
Cdd:PRK07577    4 RTVLVTGATKGIGLALSLRLANLGHQVIG--IARSAIDDFPGelfAC---------DLADIEQTAAT---LAQIN-EIHP 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 115 LWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIK-KERGRIINLASiggRTCL--PHASAYSISKFG 191
Cdd:PRK07577   69 VDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKlREQGRIVNICS---RAIFgaLDRTSYSAAKSA 145

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1270051604 192 VEAFSDALRRELGPTGVKVSIVEPGFFQTKI 222
Cdd:PRK07577  146 LVGCTRTWALELAEYGITVNAVAPGPIETEL 176
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 33-222 4.07e-13

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 68.60  E-value: 4.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  33 TDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK----RLTALHLDVTDSKEIKetyKFVAQY 108
Cdd:PRK08936    3 SDLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEANDVAEEIKkaggEAIAVKGDVTVESDVV---NLIQTA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 LPENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLI----DVTKVFLPLIKKerGRIINLASIGGRTCLPHASA 184
Cdd:PRK08936   80 VKEFGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFlgsrEAIKYFVEHDIK--GNIINMSSVHEQIPWPLFVH 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1270051604 185 YSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKI 222
Cdd:PRK08936  158 YAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPI 195
PRK05717 PRK05717
SDR family oxidoreductase;
38-221 6.82e-13

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 67.61  E-value: 6.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKETykfVAQYLPENRGLWG 117
Cdd:PRK05717   11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFIAMDVADEAQVAAG---VAEVLGQFGRLDA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 118 LVNNAGIA--KVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHASAYSISKFGVEAF 195
Cdd:PRK05717   88 LVCNAAIAdpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHNGAIVNLASTRARQSEPDTEAYAASKGGLLAL 167

                         170       180
                  ....*....|....*....|....*.
gi 1270051604 196 SDALRRELGPTgVKVSIVEPGFFQTK 221
Cdd:PRK05717  168 THALAISLGPE-IRVNAVSPGWIDAR 192
PRK08251 PRK08251
SDR family oxidoreductase;
38-223 6.85e-13

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 67.65  E-value: 6.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVfATC------LTSEGQENLTAACSKRLTALHLDVTDSKEIKETYKFVAQYLPe 111
Cdd:PRK08251    3 QKILITGASSGLGAGMAREFAAKGRDL-ALCarrtdrLEELKAELLARYPGIKVAVAALDVNDHDQVFEVFAEFRDELG- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 nrGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKE-RGRIINLASIGGRTCLP-HASAYSISK 189
Cdd:PRK08251   81 --GLDRVIVNAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQgSGHLVLISSVSAVRGLPgVKAAYAASK 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:PRK08251  159 AGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMN 192
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 41-225 7.37e-13

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 67.68  E-value: 7.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  41 LVTGCDSGFGRETALRLDSLGFNVFATCLT-SEGQENLTAACSK---RLTALHLDVTDSKEIKETykfVAQYLPENRGLW 116
Cdd:PRK12745    6 LVTGGRRGIGLGIARALAAAGFDLAINDRPdDEELAATQQELRAlgvEVIFFPADVADLSAHEAM---LDAAQAAWGRID 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 117 GLVNNAGIAKV--GPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGR------IINLASIGGRTCLPHASAYSI 187
Cdd:PRK12745   83 CLVNNAGVGVKvrGDLLDLTPESFDRVLAINLRGPFFLTQAVAKrMLAQPEPEelphrsIVFVSSVNAIMVSPNRGEYCI 162

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1270051604 188 SKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNP 225
Cdd:PRK12745  163 SKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAP 200
PRK07024 PRK07024
SDR family oxidoreductase;
40-225 9.49e-13

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 67.26  E-value: 9.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNVfatcltsegqenltAACSKRLTALH----------------LDVTDSKEIKETYK 103
Cdd:PRK07024    5 VFITGASSGIGQALAREYARQGATL--------------GLVARRTDALQafaarlpkaarvsvyaADVRDADALAAAAA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 104 -FVAQY-LPENrglwgLVNNAGIAkVGPI--EWQTIEEFKQIADVNLWGLIDVTKVFL-PLIKKERGRIINLASIGGRTC 178
Cdd:PRK07024   71 dFIAAHgLPDV-----VIANAGIS-VGTLteEREDLAVFREVMDTNYFGMVATFQPFIaPMRAARRGTLVGIASVAGVRG 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1270051604 179 LPHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT--NP 225
Cdd:PRK07024  145 LPGAGAYSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPMTahNP 193
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 35-222 1.11e-12

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: 67.10  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLG-FNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKETykfVAQYLPENR 113
Cdd:cd05326     2 LDGKVAIITGGASGIGEATARLFAKHGaRVVIADIDDDAGQAVAAELGDPDISFVHCDVTVEADVRAA---VDTAVARFG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 GLWGLVNNAGI--AKVGPIEWQTIEEFKQIADVNLWGLIDVTK-VFLPLIKKERGRIINLASIGGRT--CLPHAsaYSIS 188
Cdd:cd05326    79 RLDIMFNNAGVlgAPCYSILETSLEEFERVLDVNVYGAFLGTKhAARVMIPAKKGSIVSVASVAGVVggLGPHA--YTAS 156

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1270051604 189 KFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKI 222
Cdd:cd05326   157 KHAVLGLTRSAATELGEHGIRVNCVSPYGVATPL 190
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 40-220 1.30e-12

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: 66.82  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK---RLTALHLDVTDSKEIKETYKFVaqyLPENRGLW 116
Cdd:cd05365     2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQaggQAIGLECNVTSEQDLEAVVKAT---VSQFGGIT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 117 GLVNNAGIAKVGPIEW-QTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAYSISKFGVEA 194
Cdd:cd05365    79 ILVNNAGGGGPKPFDMpMTEEDFEWAFKLNLFSAFRLSQLCAPhMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNH 158

                         170       180
                  ....*....|....*....|....*.
gi 1270051604 195 FSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:cd05365   159 MTRNLAFDLGPKGIRVNAVAPGAVKT 184
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 38-216 1.36e-12

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 66.98  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLT-----ALHLDVTDSKEIKETYKFVAQylpen 112
Cdd:PRK12384    3 QVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGegmayGFGADATSEQSVLALSRGVDE----- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 113 rgLWG----LVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLI----DVTKVFLPliKKERGRIINLASIGGRTCLPHASA 184
Cdd:PRK12384   78 --IFGrvdlLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFlcarEFSRLMIR--DGIQGRIIQINSKSGKVGSKHNSG 153

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1270051604 185 YSISKFGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:PRK12384  154 YSAAKFGGVGLTQSLALDLAEYGITVHSLMLG 185
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
38-220 1.36e-12

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 66.63  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFatCLTSEGQENLTAACSKRLTALH---LDVTDSKEIKETYK-FVAQYLPENR 113
Cdd:PRK06924    2 RYVIITGTSQGLGEAIANQLLEKGTHVI--SISRTENKELTKLAEQYNSNLTfhsLDLQDVHELETNFNeILSSIQEDNV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 GLWGLVNNAGI-AKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERG--RIINLASIGGRTCLPHASAYSISKF 190
Cdd:PRK06924   80 SSIHLINNAGMvAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKVdkRVINISSGAAKNPYFGWSAYCSSKA 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1270051604 191 GVEAFSD--ALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK06924  160 GLDMFTQtvATEQEEEEYPVKIVAFSPGVMDT 191
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 32-223 1.68e-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: 66.35  E-value: 1.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  32 LTDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK--RLTALHLDVTDSKEIKetyKFVAQYL 109
Cdd:cd08942     1 LFSVAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAygECIAIPADLSSEEGIE---ALVARVA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 110 PENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKK-----ERGRIINLASIGG-RTCLPHAS 183
Cdd:cd08942    78 ERSDRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAaataeNPARVINIGSIAGiVVSGLENY 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1270051604 184 AYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:cd08942   158 SYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMT 197
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
35-220 1.90e-12

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 66.28  E-value: 1.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTA----ACSKRLTALHLDVTDSKEIKETYkfvAQYLP 110
Cdd:PRK08063    2 FSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAAEETAeeieALGRKALAVKANVGDVEKIKEMF---AQIDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 ENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISK 189
Cdd:PRK08063   79 EFGRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGgGKIISLSSLGSIRYLENYTTVGVSK 158

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK08063  159 AALEALTRYLAVELAPKGIAVNAVSGGAVDT 189
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 41-225 2.67e-12

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: 65.95  E-value: 2.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  41 LVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRL----TALHLDVTDSKEIKETYKFVAQYLpenRGLW 116
Cdd:cd05337     5 IVTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAgrraIYFQADIGELSDHEALLDQAWEDF---GRLD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 117 GLVNNAGIA--KVGPIEWQTIEEFKQIADVNLWG-----------LIDVTKVFLPLikkeRGRIINLASIGGRTCLPHAS 183
Cdd:cd05337    82 CLVNNAGIAvrPRGDLLDLTEDSFDRLIAINLRGpffltqavarrMVEQPDRFDGP----HRSIIFVTSINAYLVSPNRG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1270051604 184 AYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNP 225
Cdd:cd05337   158 EYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAP 199
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 35-226 3.06e-12

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


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 65.88  E-value: 3.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTA---------------ACSKRLTALHLDVTDSKEIK 99
Cdd:cd05338     1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEGDNGSAkslpgtieetaeeieAAGGQALPIVVDVRDEDQVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 100 etyKFVAQYLPENRGLWGLVNNAGIakvgpIEWQTIEE-----FKQIADVNLWGLIDVTKVFLPLIKK-ERGRIINLASI 173
Cdd:cd05338    81 ---ALVEATVDQFGRLDILVNNAGA-----IWLSLVEDtpakrFDLMQRVNLRGTYLLSQAALPHMVKaGQGHILNISPP 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1270051604 174 GGRTCLPHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGffqTKITNPD 226
Cdd:cd05338   153 LSLRPARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPS---TAIETPA 202
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 32-225 3.37e-12

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 65.55  E-value: 3.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  32 LTDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK---RLTALHLDVTDSKEIKETYKFVAQY 108
Cdd:PRK08085    4 LFSLAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQegiKAHAAPFNVTHKQEVEAAIEHIEKD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 LPenrGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTK-VFLPLIKKERGRIINLAS----IGGRTCLPHAS 183
Cdd:PRK08085   84 IG---PIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQaVARYMVKRQAGKIINICSmqseLGRDTITPYAA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1270051604 184 aysiSKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNP 225
Cdd:PRK08085  161 ----SKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKA 198
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 34-216 4.86e-12

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


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 65.45  E-value: 4.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKETykfVAQYLPENR 113
Cdd:cd05348     1 WLKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERA---VARCVERFG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 GLWGLVNNAGI----AKVGPIEWQTIEE-FKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHASAYSIS 188
Cdd:cd05348    78 KLDCFIGNAGIwdysTSLVDIPEEKLDEaFDELFHINVKGYILGAKAALPALYATEGSVIFTVSNAGFYPGGGGPLYTAS 157

                         170       180
                  ....*....|....*....|....*...
gi 1270051604 189 KFGVEAFSDALRRELGPTgVKVSIVEPG 216
Cdd:cd05348   158 KHAVVGLVKQLAYELAPH-IRVNGVAPG 184
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 38-220 7.41e-12

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: 64.40  E-value: 7.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTS-EGQENLTAACSKRLTALHLDVTDSKEIKETYKFVAQYLpenrglw 116
Cdd:cd05349     1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYRStESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHF------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 117 G----LVNNAGIAKV------GPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAY 185
Cdd:cd05349    74 GpvdtIVNNALIDFPfdpdqrKTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGsGRVINIGTNLFQNPVVPYHDY 153

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1270051604 186 SISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:cd05349   154 TTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKV 188
PRK05866 PRK05866
SDR family oxidoreductase;
34-213 1.03e-11

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 64.76  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATcltSEGQENLtAACSKRLT-------ALHLDVTDSKEIKEtykFVA 106
Cdd:PRK05866   37 DLTGKRILLTGASSGIGEAAAEQFARRGATVVAV---ARREDLL-DAVADRITraggdamAVPCDLSDLDAVDA---LVA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 107 QYLPENRGLWGLVNNAGIAKVGPIE-----WQTIEEFKQiadVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRT-CL 179
Cdd:PRK05866  110 DVEKRIGGVDILINNAGRSIRRPLAesldrWHDVERTMV---LNYYAPLRLIRGLAPgMLERGDGHIINVATWGVLSeAS 186

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1270051604 180 PHASAYSISKFGVEAFSDALRRELGPTGVKVSIV 213
Cdd:PRK05866  187 PLFSVYNASKAALSAVSRVIETEWGDRGVHSTTL 220
PRK12742 PRK12742
SDR family oxidoreductase;
32-227 1.10e-11

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 64.01  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  32 LTDLQQKYVLVTGCDSGFGRETALRLDSLGFNV-FATCLTSEGQENLTAACSKrlTALHLDVTDSKEIKETykfVAQYLP 110
Cdd:PRK12742    1 MGAFTGKKVLVLGGSRGIGAAIVRRFVTDGANVrFTYAGSKDAAERLAQETGA--TAVQTDSADRDAVIDV---VRKSGA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 enrgLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNlwglidVTKVFLPLIKKER-----GRIINLASIGG-RTCLPHASA 184
Cdd:PRK12742   76 ----LDILVVNAGIAVFGDALELDADDIDRLFKIN------IHAPYHASVEAARqmpegGRIIIIGSVNGdRMPVAGMAA 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1270051604 185 YSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKItNPDN 227
Cdd:PRK12742  146 YAASKSALQGMARGLARDFGPRGITINVVQPGPIDTDA-NPAN 187
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 35-238 1.12e-11

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: 64.10  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFatcLTSEGQENLTAACSKrLTALHLDVTDS------KEIKEtyKFVAQY 108
Cdd:cd08936     8 LANKVALVTASTDGIGLAIARRLAQDGAHVV---VSSRKQQNVDRAVAT-LQGEGLSVTGTvchvgkAEDRE--RLVATA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 LPENRGLWGLVNNAGIAKV-GPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERG-RIINLASIGGRTCLPHASAYS 186
Cdd:cd08936    82 VNLHGGVDILVSNAAVNPFfGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGgSVVIVSSVAAFHPFPGLGPYN 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1270051604 187 ISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITnpdnlkgqwQELWAN 238
Cdd:cd08936   162 VSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFS---------SALWMD 204
PRK07035 PRK07035
SDR family oxidoreductase;
32-229 1.20e-11

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 63.88  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  32 LTDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFatcLTSEGQENLTAACSK------RLTALHLDVTDSKEIKETYKFV 105
Cdd:PRK07035    3 LFDLTGKIALVTGASRGIGEAIAKLLAQQGAHVI---VSSRKLDGCQAVADAivaaggKAEALACHIGEMEQIDALFAHI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 106 aqylpenRGLWG----LVNNAGI-AKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKE-RGRIINLASIGGRTCL 179
Cdd:PRK07035   80 -------RERHGrldiLVNNAAAnPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQgGGSIVNVASVNGVSPG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1270051604 180 PHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTK-----ITNPDNLK 229
Cdd:PRK07035  153 DFQGIYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKfasalFKNDAILK 207
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 35-216 1.25e-11

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: 64.18  E-value: 1.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKetyKFVAQYLPENRG 114
Cdd:cd05363     1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASID---RCVAALVDRWGS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 115 LWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWG-LIDVTKVFLPLIKKERG-RIINLASIGGRTCLPHASAYSISKFGV 192
Cdd:cd05363    78 IDILVNNAALFDLAPIVDITRESYDRLFAINVSGtLFMMQAVARAMIAQGRGgKIINMASQAGRRGEALVGVYCATKAAV 157

                         170       180
                  ....*....|....*....|....
gi 1270051604 193 EAFSDALRRELGPTGVKVSIVEPG 216
Cdd:cd05363   158 ISLTQSAGLNLIRHGINVNAIAPG 181
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 35-222 1.39e-11

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 63.94  E-value: 1.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLG--FNVFATCLTSEGQENLTAACSKRLTALHL--DVTDSKEIKETYKFVAQYLP 110
Cdd:PRK12747    2 LKGKVALVTGASRGIGRAIAKRLANDGalVAIHYGNRKEEAEETVYEIQSNGGSAFSIgaNLESLHGVEALYSSLDNELQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 ENRGLWG---LVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKkERGRIINLASIGGRTCLPHASAYSI 187
Cdd:PRK12747   82 NRTGSTKfdiLINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLR-DNSRIINISSAATRISLPDFIAYSM 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1270051604 188 SKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKI 222
Cdd:PRK12747  161 TKGAINTMTFTLAKQLGARGITVNAILPGFIKTDM 195
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 32-244 1.72e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 63.80  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  32 LTDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK---RLTALHLDVTDskeikETY--KFVA 106
Cdd:PRK07478    1 MMRLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAeggEAVALAGDVRD-----EAYakALVA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 107 QYLPENRGLWGLVNNAGI-AKVGPIEWQTIEEFKQIADVNLwglidvTKVFL-------PLIKKERGRIINLASIGGRTC 178
Cdd:PRK07478   76 LAVERFGGLDIAFNNAGTlGEMGPVAEMSLEGWRETLATNL------TSAFLgakhqipAMLARGGGSLIFTSTFVGHTA 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1270051604 179 -LPHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNPDNLKGQWQELWANLnHSLK 244
Cdd:PRK07478  150 gFPGMAAYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMGDTPEALAFVAGL-HALK 215
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 33-216 2.91e-11

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 63.10  E-value: 2.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  33 TDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKETykfVAQYLPEN 112
Cdd:PRK08265    2 IGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERA---VATVVARF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 113 RGLWGLVNNA------GIAkvgpiewQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHASAYS 186
Cdd:PRK08265   79 GRVDILVNLActylddGLA-------SSRADWLAALDVNLVSAAMLAQAAHPHLARGGGAIVNFTSISAKFAQTGRWLYP 151

                         170       180       190
                  ....*....|....*....|....*....|
gi 1270051604 187 ISKFGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:PRK08265  152 ASKAAIRQLTRSMAMDLAPDGIRVNSVSPG 181
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-222 4.96e-11

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 62.43  E-value: 4.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVF--ATCLTSEGQEnlTAACSKRLTALHLDVTDSKEIKETYKFVAQYLPE 111
Cdd:PRK06077    3 SLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVvnAKKRAEEMNE--TLKMVKENGGEGIGVLADVSTREGCETLAKATID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 N-RGLWGLVNNAGIAKVGP---IEWQTIEefKQIaDVNLWGLIDVTKVFLPLIKkERGRIINLASIGGRTCLPHASAYSI 187
Cdd:PRK06077   81 RyGVADILVNNAGLGLFSPflnVDDKLID--KHI-STDFKSVIYCSQELAKEMR-EGGAIVNIASVAGIRPAYGLSIYGA 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1270051604 188 SKFGVEAFSDALRRELGPTgVKVSIVEPGFFQTKI 222
Cdd:PRK06077  157 MKAAVINLTKYLALELAPK-IRVNAIAPGFVKTKL 190
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 38-217 5.86e-11

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: 61.91  E-value: 5.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTA----ACSKRLTALHLDVTDSKEIKEtykFVAQYLPENR 113
Cdd:cd05357     1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQRLKdelnALRNSAVLVQADLSDFAACAD---LVAAAFRAFG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 GLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKK-ERGRIINLASIGGRTCLPHASAYSISKFGV 192
Cdd:cd05357    78 RCDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGsRNGSIINIIDAMTDRPLTGYFAYCMSKAAL 157

                         170       180
                  ....*....|....*....|....*
gi 1270051604 193 EAFSDALRRELGPTgVKVSIVEPGF 217
Cdd:cd05357   158 EGLTRSAALELAPN-IRVNGIAPGL 181
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 35-220 7.94e-11

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 61.79  E-value: 7.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK---RLTALHLDVTDSKEIKETYKFVaqyLPE 111
Cdd:PRK06113    9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQlggQAFACRCDITSEQELSALADFA---LSK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 NRGLWGLVNNAGIAKVGPIEwQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERG-RIINLASIGGRTCLPHASAYSISKF 190
Cdd:PRK06113   86 LGKVDILVNNAGGGGPKPFD-MPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGgVILTITSMAAENKNINMTSYASSKA 164

                         170       180       190
                  ....*....|....*....|....*....|
gi 1270051604 191 GVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK06113  165 AASHLVRNMAFDLGEKNIRVNGIAPGAILT 194
PLN02253 PLN02253
xanthoxin dehydrogenase
 35-225 7.95e-11

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 62.15  E-value: 7.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGrETALRL--------------DSLGFNVfatCLTSEGQENltaACskrltALHLDVTDSKEIKE 100
Cdd:PLN02253   16 LLGKVALVTGGATGIG-ESIVRLfhkhgakvcivdlqDDLGQNV---CDSLGGEPN---VC-----FFHCDVTVEDDVSR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 101 TYKFVAqylpENRG-LWGLVNNAGI--AKVGPIEWQTIEEFKQIADVNLWGLI----DVTKVFLPLikkERGRIINLASI 173
Cdd:PLN02253   84 AVDFTV----DKFGtLDIMVNNAGLtgPPCPDIRNVELSEFEKVFDVNVKGVFlgmkHAARIMIPL---KKGSIVSLCSV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1270051604 174 GGRT--CLPHAsaYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNP 225
Cdd:PLN02253  157 ASAIggLGPHA--YTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALA 208
PRK09730 PRK09730
SDR family oxidoreductase;
41-222 9.10e-11

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 61.40  E-value: 9.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  41 LVTGCDSGFGRETALRLDSLGFNVFATCLTSE--GQE--NLTAACSKRLTALHLDVTDSKEIKETYKFVAQylpENRGLW 116
Cdd:PRK09730    5 LVTGGSRGIGRATALLLAQEGYTVAVNYQQNLhaAQEvvNLITQAGGKAFVLQADISDENQVVAMFTAIDQ---HDEPLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 117 GLVNNAGIA-KVGPIEWQTIEEFKQIADVNlwglidVTKVFL---PLIKK-------ERGRIINLASIGGRTCLPHASA- 184
Cdd:PRK09730   82 ALVNNAGILfTQCTVENLTAERINRVLSTN------VTGYFLccrEAVKRmalkhggSGGAIVNVSSAASRLGAPGEYVd 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1270051604 185 YSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKI 222
Cdd:PRK09730  156 YAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEM 193
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 36-216 9.82e-11

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: 61.33  E-value: 9.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  36 QQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQEN----LTAACSKRLTALHLDVTDSKEIKETYKFVAQylpE 111
Cdd:cd05322     1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKvadeINAEYGEKAYGFGADATNEQSVIALSKGVDE---I 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 NRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKE--RGRIINLASIGGRTCLPHASAYSISK 189
Cdd:cd05322    78 FKRVDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDgiQGRIIQINSKSGKVGSKHNSGYSAAK 157

                         170       180
                  ....*....|....*....|....*..
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:cd05322   158 FGGVGLTQSLALDLAEHGITVNSLMLG 184
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 40-231 1.25e-10

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: 60.86  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK----RLTALHLDVTDSKEIKETYKFVAQYL--PEnr 113
Cdd:cd05373     2 AAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRdaggSAKAVPTDARDEDEVIALFDLIEEEIgpLE-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 glwGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRII---NLASIGGRtclPHASAYSISK 189
Cdd:cd05373    80 ---VLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKrMLARGRGTIIftgATASLRGR---AGFAAFAGAK 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1270051604 190 FGVEAFSDALRRELGPTGVKV------SIVEPGFFQTKITNPDNLKGQ 231
Cdd:cd05373   154 FALRALAQSMARELGPKGIHVahviidGGIDTDFIRERFPKRDERKEE 201
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 32-220 1.63e-10

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 60.94  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  32 LTDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFatcLTSEGQENLTAACS------KRLTALHLDVTDSKEIKETykfV 105
Cdd:PRK07523    5 LFDLTGRRALVTGSSQGIGYALAEGLAQAGAEVI---LNGRDPAKLAAAAEslkgqgLSAHALAFDVTDHDAVRAA---I 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 106 AQYLPENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTK-VFLPLIKKERGRIINLASIGGRTCLPHASA 184
Cdd:PRK07523   79 DAFEAEIGPIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQaVARHMIARGAGKIINIASVQSALARPGIAP 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1270051604 185 YSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK07523  159 YTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDT 194
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 35-223 4.69e-10

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 60.62  E-value: 4.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETAlrldslgfNVFA------TCLTSEGQENLTAACSKRL--TALHLDVTDskeiKETYKFVA 106
Cdd:PRK08261  208 LAGKVALVTGAARGIGAAIA--------EVLArdgahvVCLDVPAAGEALAAVANRVggTALALDITA----PDAPARIA 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 107 QYLPEN-RGLWGLVNNAGI------AKVGPIEWQtieefkQIADVNLWGLIDVTKVFL-PLIKKERGRIINLASIG---- 174
Cdd:PRK08261  276 EHLAERhGGLDIVVHNAGItrdktlANMDEARWD------SVLAVNLLAPLRITEALLaAGALGDGGRIVGVSSISgiag 349

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1270051604 175 --GRTclphasAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:PRK08261  350 nrGQT------NYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQMT 394
PRK08278 PRK08278
SDR family oxidoreductase;
34-211 7.40e-10

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 59.15  E-value: 7.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENL-----------TAACSKRLtALHLDVTDSKEIKETy 102
Cdd:PRK08278    3 SLSGKTLFITGASRGIGLAIALRAARDGANIVIAAKTAEPHPKLpgtihtaaeeiEAAGGQAL-PLVGDVRDEDQVAAA- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 103 kfVAQYLPENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKK-ERGRIINLA---SIGGRTC 178
Cdd:PRK08278   81 --VAKAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKsENPHILTLSpplNLDPKWF 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1270051604 179 LPHAsAYSISKFGVEAFSDALRRELGPTGVKVS 211
Cdd:PRK08278  159 APHT-AYTMAKYGMSLCTLGLAEEFRDDGIAVN 190
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 30-226 7.65e-10

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 59.14  E-value: 7.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  30 EFLTDLQQKYVLVTGCDSGFGRETALRLDSLGFNV------------FATCLTSEGQENLtaacskrltALHLDVTDSKE 97
Cdd:PRK08277    3 PNLFSLKGKVAVITGGGGVLGGAMAKELARAGAKVaildrnqekaeaVVAEIKAAGGEAL---------AVKADVLDKES 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  98 IKETYKFVAQYlpenrglWG----LVNNAG----------IAKVGPIEWQT-----IEEFKQIADVNLWGLIDVTKVFL- 157
Cdd:PRK08277   74 LEQARQQILED-------FGpcdiLINGAGgnhpkattdnEFHELIEPTKTffdldEEGFEFVFDLNLLGTLLPTQVFAk 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1270051604 158 PLIKKERGRIINLASIGGRTCLPHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTK-----ITNPD 226
Cdd:PRK08277  147 DMVGRKGGNIINISSMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEqnralLFNED 220
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 35-225 1.11e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 58.66  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFatcLTSEGQENLTAAcSKRLTAL------HLDVTDSKEIKETYKFVAQY 108
Cdd:PRK05875    5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVM---IVGRNPDKLAAA-AEEIEALkgagavRYEPADVTDEDQVARAVDAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 LPENRGLWGLVNNAGIAK-VGPIEWQTIEEFKQIADVNLWGLIDVTK-VFLPLIKKERGRIINLASIGGRTCLPHASAYS 186
Cdd:PRK05875   81 TAWHGRLHGVVHCAGGSEtIGPITQIDSDAWRRTVDLNVNGTMYVLKhAARELVRGGGGSFVGISSIAASNTHRWFGAYG 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1270051604 187 ISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNP 225
Cdd:PRK05875  161 VTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAP 199
PRK08628 PRK08628
SDR family oxidoreductase;
34-215 1.14e-09

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 58.43  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLG-----FNVFAtcLTSEGQENLTAAcSKRLTALHLDVTDSKEIKetyKFVAQY 108
Cdd:PRK08628    4 NLKDKVVIVTGGASGIGAAISLRLAEEGaipviFGRSA--PDDEFAEELRAL-QPRAEFVQVDLTDDAQCR---DAVEQT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 LPENRGLWGLVNNAGIA-KVGpIEwQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHASAYSI 187
Cdd:PRK08628   78 VAKFGRIDGLVNNAGVNdGVG-LE-AGREAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISSKTALTGQGGTSGYAA 155

                         170       180
                  ....*....|....*....|....*...
gi 1270051604 188 SKFGVEAFSDALRRELGPTGVKVSIVEP 215
Cdd:PRK08628  156 AKGAQLALTREWAVALAKDGVRVNAVIP 183
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-220 1.19e-09

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 58.18  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTS-EGQENLTAACSKRLTALHLDVTDSKEIKETYKFVAQYLpeN 112
Cdd:PRK08642    2 QISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSeDAAEALADELGDRAIALQADVTDREQVQAMFATATEHF--G 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 113 RGLWGLVNNAGIA---------KVGPIEWqtiEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINlasIGgrTCLPHA 182
Cdd:PRK08642   80 KPITTVVNNALADfsfdgdarkKADDITW---EDFQQQLEGSVKGALNTIQAALPgMREQGFGRIIN---IG--TNLFQN 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1270051604 183 SA-----YSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK08642  152 PVvpyhdYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRT 194
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 35-216 1.28e-09

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 58.04  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTD----SKEIKETykfVAQYlp 110
Cdd:PRK06200    4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSyadnQRAVDQT---VDAF-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 enRGLWGLVNNAGI----AKVGPIEWQTIEE-FKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASI------GGRTCl 179
Cdd:PRK06200   79 --GKLDCFVGNAGIwdynTSLVDIPAETLDTaFDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLSNssfypgGGGPL- 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1270051604 180 phasaYSISKFGVEAFSDALRRELGPtGVKVSIVEPG 216
Cdd:PRK06200  156 -----YTASKHAVVGLVRQLAYELAP-KIRVNGVAPG 186
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 35-220 1.64e-09

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


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 57.84  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAA-CSKRLTALHLDVTDSKEIKETYKFVAQYLPENR 113
Cdd:cd09763     1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILPQLPGTAEeIEARGGKCIPVRCDHSDDDEVEALFERVAREQQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 G-LWGLVNNA------GIAKVGPIEWQtiEEFKQIADVNLWGLID--VTKVF-LPLIKKE-RGRIINLASIGGRTCLpHA 182
Cdd:cd09763    81 GrLDILVNNAyaavqlILVGVAKPFWE--EPPTIWDDINNVGLRAhyACSVYaAPLMVKAgKGLIVIISSTGGLEYL-FN 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1270051604 183 SAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:cd09763   158 VAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRT 195
PRK09135 PRK09135
pteridine reductase; Provisional
 33-216 5.06e-09

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 56.09  E-value: 5.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  33 TDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEG-----QENLTAACSKRLTALHLDVTDSKEIKEtykFVAQ 107
Cdd:PRK09135    2 MTDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRSAAeadalAAELNALRPGSAAALQADLLDPDALPE---LVAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 108 YLPENRGLWGLVNNAG------IAKVGPIEWQtieefkQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPH 181
Cdd:PRK09135   79 CVAAFGRLDALVNNASsfyptpLGSITEAQWD------DLFASNLKAPFFLSQAAAPQLRKQRGAIVNITDIHAERPLKG 152

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1270051604 182 ASAYSISKFGVEAFSDALRRELGPTgVKVSIVEPG 216
Cdd:PRK09135  153 YPVYCAAKAALEMLTRSLALELAPE-VRVNAVAPG 186
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 35-216 1.19e-08

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 55.08  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCD--SGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSK--------------RLTALHLDVTDSkei 98
Cdd:PRK12748    3 LMKKIALVTGASrlNGIGAAVCRRLAAKGIDIFFTYWSPYDKTMPWGMHDKepvllkeeiesygvRCEHMEIDLSQP--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  99 kETYKFVAQYLPENRG-LWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGR 176
Cdd:PRK12748   80 -YAPNRVFYAVSERLGdPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKqYDGKAGGRIINLTSGQSL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1270051604 177 TCLPHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:PRK12748  159 GPMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPG 198
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 36-216 1.25e-08

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 55.34  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  36 QQKYVLVTGCDSGFGRETALRLDSLGFNVFAT---CLTSEGQENLTAAcSKRLTALHLDVtdskeikETYKFVAQYLPEN 112
Cdd:PRK12823    7 AGKVVVVTGAAQGIGRGVALRAAAEGARVVLVdrsELVHEVAAELRAA-GGEALALTADL-------ETYAGAQAAMAAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 113 RGLWG----LVNNAGiakvGPIEWQTIEEFK--QI-ADVN------LWGLIDVtkvfLP-LIKKERGRIINLASIGGRTC 178
Cdd:PRK12823   79 VEAFGridvLINNVG----GTIWAKPFEEYEeeQIeAEIRrslfptLWCCRAV----LPhMLAQGGGAIVNVSSIATRGI 150

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1270051604 179 lpHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:PRK12823  151 --NRVPYSAAKGGVNALTASLAFEYAEHGIRVNAVAPG 186
PRK07831 PRK07831
SDR family oxidoreductase;
35-228 1.36e-08

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 55.04  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGC-DSGFGRETALRLDSLGfnvfATCLTS--------EGQENLTAAC-SKRLTALHLDVTDSKEIKETYKF 104
Cdd:PRK07831   15 LAGKVVLVTAAaGTGIGSATARRALEEG----ARVVISdiherrlgETADELAAELgLGRVEAVVCDVTSEAQVDALIDA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 105 VAQYLPenrGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIK--KERGRIINLASIGGRTCLPHA 182
Cdd:PRK07831   91 AVERLG---RLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRarGHGGVIVNNASVLGWRAQHGQ 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1270051604 183 SAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGF----FQTKITNPDNL 228
Cdd:PRK07831  168 AHYAAAKAGVMALTRCSALEAAEYGVRINAVAPSIamhpFLAKVTSAELL 217
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 35-216 2.99e-08

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 54.02  E-value: 2.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCD--SGFGRETALRLDSLGFNVFATCLTSEG---------------QENLTAAcSKRLTALHLDVTDSKE 97
Cdd:PRK12859    4 LKNKVAVVTGVSrlDGIGAAICKELAEAGADIFFTYWTAYDkempwgvdqdeqiqlQEELLKN-GVKVSSMELDLTQNDA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  98 IKETYKFVAQYL--PENrglwgLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERG-RIINLASIG 174
Cdd:PRK12859   83 PKELLNKVTEQLgyPHI-----LVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKKSGgRIINMTSGQ 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1270051604 175 GRTCLPHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:PRK12859  158 FQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPG 199
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 34-232 4.02e-08

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


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 53.48  E-value: 4.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCL--TSEGQENLTAACSKrltalhldVTDskEIKETY-KFVAQY-- 108
Cdd:cd05353     2 RFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLggDRKGSGKSSSAADK--------VVD--EIKAAGgKAVANYds 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 -----------LPENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGR 176
Cdd:cd05353    72 vedgekivktaIDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKfGRIINTSSAAGL 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1270051604 177 TCLPHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEP--GFFQTKITNPDNLKGQW 232
Cdd:cd05353   152 YGNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPaaGSRMTETVMPEDLFDAL 209
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
34-223 9.02e-08

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 52.57  E-value: 9.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLT--SEGQENLTAAcSKRLTALHLDVTDSKEIKEtykFVAQYLPE 111
Cdd:PRK08993    7 SLEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVepTETIEQVTAL-GRRFLSLTADLRKIDGIPA---LLERAVAE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 NRGLWGLVNNAG-IAKVGPIEWQTiEEFKQIADVNLWGLI----DVTKVFLPliKKERGRIINLASIGGRTCLPHASAYS 186
Cdd:PRK08993   83 FGHIDILVNNAGlIRREDAIEFSE-KDWDDVMNLNIKSVFfmsqAAAKHFIA--QGNGGKIINIASMLSFQGGIRVPSYT 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1270051604 187 ISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:PRK08993  160 ASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNT 196
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 35-217 1.40e-07

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 51.69  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKrLTALHL---DVTDSKEIKETYKFVAQYLPe 111
Cdd:PRK05786    3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSK-YGNIHYvvgDVSSTESARNVIEKAAKVLN- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 112 nrGLWGLVNNAGiakvGPIEwQTIEEFKQIADV---NLWGLIDVTKVFLPLIKkERGRIINLASIGG-RTCLPHASAYSI 187
Cdd:PRK05786   81 --AIDGLVVTVG----GYVE-DTVEEFSGLEEMltnHIKIPLYAVNASLRFLK-EGSSIVLVSSMSGiYKASPDQLSYAV 152

                         170       180       190
                  ....*....|....*....|....*....|
gi 1270051604 188 SKFGVEAFSDALRRELGPTGVKVSIVEPGF 217
Cdd:PRK05786  153 AKAGLAKAVEILASELLGRGIRVNGIAPTT 182
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 40-225 1.60e-07

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: 51.37  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNVfatcLTSEGQENLTAACSKRLTALHL--DVTDSKEIKEtykfVAQYLPEnrgLWG 117
Cdd:cd11730     1 ALILGATGGIGRALARALAGRGWRL----LLSGRDAGALAGLAAEVGALARpaDVAAELEVWA----LAQELGP---LDL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 118 LVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLiKKERGRIINLASIGGRTCLPHASAYSISKFGVEAFSD 197
Cdd:cd11730    70 LVYAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHALAL-LAAGARLVFLGAYPELVMLPGLSAYAAAKAALEAYVE 148

                         170       180
                  ....*....|....*....|....*...
gi 1270051604 198 ALRRELgpTGVKVSIVEPGFFQTKITNP 225
Cdd:cd11730   149 VARKEV--RGLRLTLVRPPAVDTGLWAP 174
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
34-223 1.72e-07

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 51.83  E-value: 1.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQ-ENLTAACSKRLTALHLDVTDSKEIKEtykFVAQYLPEN 112
Cdd:PRK12481    5 DLNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEAPEtQAQVEALGRKFHFITADLIQQKDIDS---IVSQAVEVM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 113 RGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLI----DVTKVFLPliKKERGRIINLASIGGRTCLPHASAYSIS 188
Cdd:PRK12481   82 GHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFflsqAVAKQFVK--QGNGGKIINIASMLSFQGGIRVPSYTAS 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1270051604 189 KFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:PRK12481  160 KSAVMGLTRALATELSQYNINVNAIAPGYMATDNT 194
PRK07856 PRK07856
SDR family oxidoreductase;
34-220 1.91e-07

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 51.47  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFaTCLTSEGQENLTA-----ACskrltalhlDVTDSKEIKetyKFVAQY 108
Cdd:PRK07856    3 DLTGRVVLVTGGTRGIGAGIARAFLAAGATVV-VCGRRAPETVDGRpaefhAA---------DVRDPDQVA---ALVDAI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 LPENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKE--RGRIINLASIGGRTCLPHASAYS 186
Cdd:PRK07856   70 VERHGRLDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQpgGGSIVNIGSVSGRRPSPGTAAYG 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1270051604 187 ISKFGVEAFSDALRRELGPTgVKVSIVEPGFFQT 220
Cdd:PRK07856  150 AAKAGLLNLTRSLAVEWAPK-VRVNAVVVGLVRT 182
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 38-223 4.11e-07

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 50.85  E-value: 4.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRL--DSLGFNVFATCLTSEGQENLTAACSK----------RLTALHLDVTD-------SKEI 98
Cdd:cd08941     2 KVVLVTGANSGLGLAICERLlaEDDENPELTLILACRNLQRAEAACRAllashpdarvVFDYVLVDLSNmvsvfaaAKEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  99 KETYKFVaQYLPENRGLWGlvnNAGIAKVG--------PIEWQTIEEFK----------QIADVNLWGLIDVTKVF---- 156
Cdd:cd08941    82 KKRYPRL-DYLYLNAGIMP---NPGIDWIGaikevltnPLFAVTNPTYKiqaegllsqgDKATEDGLGEVFQTNVFghyy 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 157 -----LPLIKKER--GRIINLASIGGRT---------CLPHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:cd08941   158 lirelEPLLCRSDggSQIIWTSSLNASPkyfslediqHLKGPAPYSSSKYLVDLLSLALNRKFNKLGVYSYVVHPGICTT 237


                  ...
gi 1270051604 221 KIT 223
Cdd:cd08941   238 NLT 240
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 34-220 5.67e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 50.04  E-value: 5.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALrldslgfnVFAT--C---LTSEGQENLTAACSK-------RLTALHLDVTDSKEIKET 101
Cdd:PRK06125    4 HLAGKRVLITGASKGIGAAAAE--------AFAAegChlhLVARDADALEALAADlraahgvDVAVHALDLSSPEAREQL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 102 YKFVAQYLPenrglwgLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIK-KERGRIINLASIGGRTCLP 180
Cdd:PRK06125   76 AAEAGDIDI-------LVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKaRGSGVIVNVIGAAGENPDA 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1270051604 181 HASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK06125  149 DYICGSAGNAALMAFTRALGGKSLDDGVRVVGVNPGPVAT 188
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 40-220 7.68e-07

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent 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: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 49.12  E-value: 7.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETAlrldslgfnvfaTCLTSEGQENLTAACSKRltALHLDVTDSKEIKETYK----FVAqylpenrgl 115
Cdd:cd11731     1 IIVIGATGTIGLAVA------------QLLSAHGHEVITAGRSSG--DYQVDITDEASIKALFEkvghFDA--------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 wgLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIkKERGRIINLASIGGRTCLPHASAYSISKFGVEAF 195
Cdd:cd11731    58 --IVSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYL-NDGGSITLTSGILAQRPIPGGAAAATVNGALEGF 134

                         170       180
                  ....*....|....*....|....*
gi 1270051604 196 SDALRRELgPTGVKVSIVEPGFFQT 220
Cdd:cd11731   135 VRAAAIEL-PRGIRINAVSPGVVEE 158
PRK08703 PRK08703
SDR family oxidoreductase;
35-192 8.67e-07

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 49.54  E-value: 8.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQEN----LTAACSKRLTALHLDVTDSKEiKETYKFVAQYLP 110
Cdd:PRK08703    4 LSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKvydaIVEAGHPEPFAIRFDLMSAEE-KEFEQFAATIAE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 ENRG-LWGLVNNAG-IAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKE-RGRIINLASIGGRTCLPHASAYSI 187
Cdd:PRK08703   83 ATQGkLDGIVHCAGyFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSpDASVIFVGESHGETPKAYWGGFGA 162


                  ....*
gi 1270051604 188 SKFGV 192
Cdd:PRK08703  163 SKAAL 167
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 34-216 1.47e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 48.80  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVfatCLTSEGQENLTAAcSKRLTALH-------LDVTDskeiketYKFVA 106
Cdd:PRK07576    6 DFAGKNVVVVGGTSGINLGIAQAFARAGANV---AVASRSQEKVDAA-VAQLQQAGpeglgvsADVRD-------YAAVE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 107 QYLPENRGLWG----LVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASigGRTCLP-- 180
Cdd:PRK07576   75 AAFAQIADEFGpidvLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPGASIIQISA--PQAFVPmp 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1270051604 181 ---HASAysiSKFGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:PRK07576  153 mqaHVCA---AKAGVDMLTRTLALEWGPEGIRVNSIVPG 188
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
40-218 1.74e-06

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 48.82  E-value: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCdSGF-GRETALRLDSLGFNVFATCLTSEGQENLTAAcsKRLTALHLDVTDSKEIKEtykFVAQylPEnrglwGL 118
Cdd:COG0451     2 ILVTGG-AGFiGSHLARRLLARGHEVVGLDRSPPGAANLAAL--PGVEFVRGDLRDPEALAA---ALAG--VD-----AV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 119 VNNAGIAKVGpiewqtIEEFKQIADVNLWGLIDVtkvfLPLIKKER-GRIINLASIG--GRTCLP--------HASAYSI 187
Cdd:COG0451    69 VHLAAPAGVG------EEDPDETLEVNVEGTLNL----LEAARAAGvKRFVYASSSSvyGDGEGPidedtplrPVSPYGA 138

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1270051604 188 SKFGVEAFSDALRRElgpTGVKVSIVEPGFF 218
Cdd:COG0451   139 SKLAAELLARAYARR---YGLPVTILRPGNV 166
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 40-223 4.36e-06

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: 47.49  E-value: 4.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  40 VLVTGCDSGFGRETALRLDSLGFNVFATCLtsegqenltaacskRLTALHLDVTDSKEIKETykfVAQYLPENRGLW-GL 118
Cdd:cd05328     2 IVITGAASGIGAATAELLEDAGHTVIGIDL--------------READVIADLSTPEGRAAA---IADVLARCSGVLdGL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 119 VNNAGIAKVGPIEwqtieefkQIADVNLWGLIDVTKVFLPLIKK-ERGRIINLASI---GGRTCLP-------------- 180
Cdd:cd05328    65 VNCAGVGGTTVAG--------LVLKVNYFGLRALMEALLPRLRKgHGPAAVVVSSIagaGWAQDKLelakalaagteara 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1270051604 181 -----HA-----SAYSISKfgvEAFSDALRReLGPT-----GVKVSIVEPGFFQTKIT 223
Cdd:cd05328   137 valaeHAgqpgyLAYAGSK---EALTVWTRR-RAATwlygaGVRVNTVAPGPVETPIL 190
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
88-220 5.24e-06

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 47.40  E-value: 5.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  88 LHLDVTDSKEIKETYKFVAQYlpenrglWG----LVNNAGIAK----VGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPL 159
Cdd:PRK07370   64 LPCDVQDDAQIEETFETIKQK-------WGkldiLVHCLAFAGkeelIGDFSATSREGFARALEISAYSLAPLCKAAKPL 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1270051604 160 IKkERGRIINLASIGGRTCLPHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK07370  137 MS-EGGSIVTLTYLGGVRAIPNYNVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRT 196
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 75-210 7.51e-06

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site 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: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 46.81  E-value: 7.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  75 ENLTAACSKRLTALHLDVTDSKEIKETYKFVAQylpENRGLWGLVNNAG----IAKVGPIEWQTIEEFKQIADVNLWGLI 150
Cdd:cd05372    44 EKLAERLGESALVLPCDVSNDEEIKELFAEVKK---DWGKLDGLVHSIAfapkVQLKGPFLDTSRKGFLKALDISAYSLV 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 151 DVTKVFLPLIKkERGRIINLASIGGRTCLPHASAYSISKFGVEAFSDALRRELGPTGVKV 210
Cdd:cd05372   121 SLAKAALPIMN-PGGSIVTLSYLGSERVVPGYNVMGVAKAALESSVRYLAYELGRKGIRV 179
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 35-215 1.25e-05

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 45.90  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSE-----------GQENLTAACSKRLtALHLDVTDSKEIKETyk 103
Cdd:cd09762     1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEphpklpgtiytAAEEIEAAGGKAL-PCIVDIRDEDQVRAA-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 104 fVAQYLPENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERG-RIINLA---SIGGRTCL 179
Cdd:cd09762    78 -VEKAVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNpHILNLSpplNLNPKWFK 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1270051604 180 PHaSAYSISKFGVEAFSDALRRELGPTGVKVSIVEP 215
Cdd:cd09762   157 NH-TAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 39-224 1.60e-05

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 46.01  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  39 YVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLD--VTD-SKEIKETYKFVAQYLpENRGL 115
Cdd:PLN02780   55 WALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSKTQIKtvVVDfSGDIDEGVKRIKETI-EGLDV 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGIAKVGPIEWQTIEE--FKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASiGGRTCLPHASAYSI---SK 189
Cdd:PLN02780  134 GVLINNVGVSYPYARFFHEVDEelLKNLIKVNVEGTTKVTQAVLPgMLKRKKGAIINIGS-GAAIVIPSDPLYAVyaaTK 212

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1270051604 190 FGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITN 224
Cdd:PLN02780  213 AYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMAS 247
PRK07102 PRK07102
SDR family oxidoreductase;
38-237 2.26e-05

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 45.30  E-value: 2.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFatcLTSEGQENLT------AACSKRLTALH-LDVTDSKEIKETYKfvaqylp 110
Cdd:PRK07102    2 KKILIIGATSDIARACARRYAAAGARLY---LAARDVERLErladdlRARGAVAVSTHeLDILDTASHAAFLD------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 111 enrGLWGLVNNAGIAkVGPIEWQT-----IEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASA 184
Cdd:PRK07102   72 ---SLPALPDIVLIA-VGTLGDQAaceadPALALREFRTNFEGPIALLTLLANRFEARGsGTIVGISSVAGDRGRASNYV 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1270051604 185 YSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKITNPDNLKGQwqeLWA 237
Cdd:PRK07102  148 YGSAKAALTAFLSGLRNRLFKSGVHVLTVKPGFVRTPMTAGLKLPGP---LTA 197
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 41-174 2.51e-05

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 45.28  E-value: 2.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  41 LVTGCDSGFGRETALRLDSLGFNVFATCLTS----EGQENLTAACSKRLTALH-LDVTDSKEIketYKFVAQYLPENRGL 115
Cdd:cd09808     5 LITGANSGIGKAAALAIAKRGGTVHMVCRNQtraeEARKEIETESGNQNIFLHiVDMSDPKQV---WEFVEEFKEEGKKL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 116 WGLVNNAGiAKVGPIEwQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERG-RIINLASIG 174
Cdd:cd09808    82 HVLINNAG-CMVNKRE-LTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDpRVITVSSGG 139
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 118-220 3.29e-05

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 44.87  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 118 LVNNAGIAK-VGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER-GRIINLASIGGRTCLPHASAYSISKFGVEAF 195
Cdd:cd05361    76 LVSNDYIPRpMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGgGSIIFITSAVPKKPLAYNSLYGPARAAAVAL 155

                          90       100
                  ....*....|....*....|....*
gi 1270051604 196 SDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:cd05361   156 AESLAKELSRDNILVYAIGPNFFNS 180
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 38-216 6.53e-05

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 43.90  E-value: 6.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVfatCLTSEGQENLTAACSK------RLTALHLDVTD----SKEIKETYKFVAQ 107
Cdd:PRK07677    2 KVVIITGGSSGMGKAMAKRFAEEGANV---VITGRTKEKLEEAKLEieqfpgQVLTVQMDVRNpedvQKMVEQIDEKFGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 108 ylpenrgLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTK-VFLPLIKKE-RGRIINLASI----GGRTCLPH 181
Cdd:PRK07677   79 -------IDALINNAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQaVGKYWIEKGiKGNIINMVATyawdAGPGVIHS 151

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1270051604 182 ASAysisKFGVEAFSDALRRELGPT-GVKVSIVEPG 216
Cdd:PRK07677  152 AAA----KAGVLAMTRTLAVEWGRKyGIRVNAIAPG 183
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
134-220 7.55e-05

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 43.96  E-value: 7.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 134 TIEEFKQIADVNLWGLIDVTKVFLPLIKkERGRIINLASIGGRTCLPHASAYSISKFGVEAFSDALRRELGPTGVKVSIV 213
Cdd:PRK08415  107 SKEAFNIAMEISVYSLIELTRALLPLLN-DGASVLTLSYLGGVKYVPHYNVMGVAKAALESSVRYLAVDLGKKGIRVNAI 185


                  ....*..
gi 1270051604 214 EPGFFQT 220
Cdd:PRK08415  186 SAGPIKT 192
PRK06953 PRK06953
SDR family oxidoreductase;
38-177 7.63e-05

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 43.52  E-value: 7.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKrltALHLDVTDSKEIKetykfvaqylpenrGL-W 116
Cdd:PRK06953    2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQALGAE---ALALDVADPASVA--------------GLaW 64

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1270051604 117 GL--------VNNAGI--AKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLAS----IGGRT 177
Cdd:PRK06953   65 KLdgealdaaVYVAGVygPRTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSrmgsIGDAT 139
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 34-220 8.33e-05

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 43.69  E-value: 8.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFatcLTSEGQENLTAACSKRLTALHLDV-------TDSKEIKETYKFVA 106
Cdd:PRK08339    5 DLSGKLAFTTASSKGIGFGVARVLARAGADVI---LLSRNEENLKKAREKIKSESNVDVsyivadlTKREDLERTVKELK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 107 QYLPENRGLWglvnNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLP-LIKKERGRIINLASIGGRTCLPHASAY 185
Cdd:PRK08339   82 NIGEPDIFFF----STGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPaMERKGFGRIIYSTSVAIKEPIPNIALS 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1270051604 186 SISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK08339  158 NVVRISMAGLVRTLAKELGPKGITVNGIMPGIIRT 192
DUF1776 pfam08643
Fungal family of unknown function (DUF1776); This is a fungal family of unknown function. One ...
 51-312 3.79e-04

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


Pssm-ID: 370028  Cd Length: 295  Bit Score: 41.64  E-value: 3.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  51 RETALRLDSLGFNVFaTCLTSEGQENLTAA-CSKRLTALHLDVTDSKEIKETYKFVAQYLPENRGLWGLVNN-----AGI 124
Cdd:pfam08643  18 RAIALDLERRGFIVF-VTVTSAKDYKTVESeQRPDIRPLSLDDTAPSSIEASLEEFLQLLETPHVPFPGAKPhvlrlRGV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 125 AKV-------GPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIK--KERGRIINL-ASIGGRTCLPHASAYSISKFGVEA 194
Cdd:pfam08643  97 ILVpslsyptGPIENIPPSSWASEFNSRLLNYYLTLQGLLPLLRsrSQKAQIIVFnPSISSSLNLPYHAPEALVSSALST 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 195 FSDALRRELGPTGVKVSIVEPGFFQTKITNPDNLKgqwqelWANLNHSL--------KEEYGEKFYETSVKNMLTGMVDT 266
Cdd:pfam08643 177 LFTTLKRELRPHGIDVTQIKLGNLDLSNGSASNYK------YLNIAGSEvlswseimRALYGPNYVSIQSKAIGIRSTRG 250

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1270051604 267 CAspyLYKVVDAIVHSLTSRYPKTRYMVGWDAKlLWIWISR-LPAGV 312
Cdd:pfam08643 251 SS---LRELHNALFDLLYGSSPKPVVYCGKGAR-LYSWVGKwLPEWL 293
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 30-215 3.79e-04

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 41.69  E-value: 3.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  30 EFLTDLQQKYVLVTGCDSGFGRETALRLDSLG----FNVFATCLTSEGQENLTAACSKRLTALHLDVTD---SKEIKETy 102
Cdd:PRK07792    5 TNTTDLSGKVAVVTGAAAGLGRAEALGLARLGatvvVNDVASALDASDVLDEIRAAGAKAVAVAGDISQratADELVAT- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 103 kfvAQYLPenrGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTK---VFLPLIKKER-----GRIINLASIG 174
Cdd:PRK07792   84 ---AVGLG---GLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRnaaAYWRAKAKAAggpvyGRIVNTSSEA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1270051604 175 GRTCLPHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEP 215
Cdd:PRK07792  158 GLVGPVGQANYGAAKAGITALTLSAARALGRYGVRANAICP 198
PRK07023 PRK07023
SDR family oxidoreductase;
41-220 4.15e-04

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 41.54  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  41 LVTGCDSGFGRETALRLDSLGFNVFatCLTSEGQENLTAACSKRLTALHLDVTDSKEIKE-TYKFVAQYLPENRGLWGLV 119
Cdd:PRK07023    5 IVTGHSRGLGAALAEQLLQPGIAVL--GVARSRHPSLAAAAGERLAEVELDLSDAAAAAAwLAGDLLAAFVDGASRVLLI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 120 NNAGIAK-VGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKK--ERgRIINLASIGGRTCLPHASAYSISKFGVEAFS 196
Cdd:PRK07023   83 NNAGTVEpIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDaaER-RILHISSGAARNAYAGWSVYCATKAALDHHA 161

                         170       180
                  ....*....|....*....|....
gi 1270051604 197 DALRRElGPTGVKVSIVEPGFFQT 220
Cdd:PRK07023  162 RAVALD-ANRALRIVSLAPGVVDT 184
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 39-223 5.52e-04

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


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 41.05  E-value: 5.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  39 YVLVTGCDSGFGRETALRLdslgfnvfATCLTSEG----------------QENLTAACS-KRLTALHLDVTDSKEIKET 101
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQEL--------AKCLKSPGsvlvlsarndealrqlKAEIGAERSgLRVVRVSLDLGAEAGLEQL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 102 YKFVAQYL-PENRGLWGLVNNAG-IAKVGPIEwQTIEEFKQIA---DVNLWGLIDVTKVFLPLIKKERG---RIINLASI 173
Cdd:TIGR01500  74 LKALRELPrPKGLQRLLLINNAGtLGDVSKGF-VDLSDSTQVQnywALNLTSMLCLTSSVLKAFKDSPGlnrTVVNISSL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1270051604 174 GGRTCLPHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQTKIT 223
Cdd:TIGR01500 153 CAIQPFKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQ 202
PRK06196 PRK06196
oxidoreductase; Provisional
 34-225 5.69e-04

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 41.21  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACsKRLTALHLDVTDSKEIKEtykFVAQYLPENR 113
Cdd:PRK06196   23 DLSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGI-DGVEVVMLDLADLESVRA---FAERFLDSGR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 114 GLWGLVNNAGI-----AKVGPiEWQTieefkQIAdVNLWGLIDVTKVFLPLIKKERG-RIINLASIGGRTCL-----PHA 182
Cdd:PRK06196   99 RIDILINNAGVmacpeTRVGD-GWEA-----QFA-TNHLGHFALVNLLWPALAAGAGaRVVALSSAGHRRSPirwddPHF 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1270051604 183 S-------AYSISKFGVEAFSDALRRELGPTGVKVSIVEPGffqtKITNP 225
Cdd:PRK06196  172 TrgydkwlAYGQSKTANALFAVHLDKLGKDQGVRAFSVHPG----GILTP 217
PRK12744 PRK12744
SDR family oxidoreductase;
34-218 9.91e-04

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 40.49  E-value: 9.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  34 DLQQKYVLVTGCDSGFGRETALRLDSLGFNVFA---TCLTSEGQENLTAACSK----RLTALHLDVTDSKEIKETYKFVA 106
Cdd:PRK12744    5 SLKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAihyNSAASKADAEETVAAVKaagaKAVAFQADLTTAAAVEKLFDDAK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 107 QYLpenrglwGLVNNAgIAKVG-----PIEWQTIEEFKQIADVNlwglidvTKVFLPLIKK------ERGRIINLAS--I 173
Cdd:PRK12744   85 AAF-------GRPDIA-INTVGkvlkkPIVEISEAEYDEMFAVN-------SKSAFFFIKEagrhlnDNGKIVTLVTslL 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1270051604 174 GGRTclPHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPG-----FF 218
Cdd:PRK12744  150 GAFT--PFYSAYAGSKAPVEHFTRAASKEFGARGISVTAVGPGpmdtpFF 197
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
35-220 1.06e-03

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 40.34  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDS----GFGRETALRLD--SLGFNVFATCLTSEGQENLTAACSKrlTALHLDVTDSKEIKETYKFVAQY 108
Cdd:PRK08690    4 LQGKKILITGMISersiAYGIAKACREQgaELAFTYVVDKLEERVRKMAAELDSE--LVFRCDVASDDEINQVFADLGKH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 LPenrGLWGLVNNAGIAKVGPIEWQTI-----EEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLPHAS 183
Cdd:PRK08690   82 WD---GLDGLVHSIGFAPKEALSGDFLdsisrEAFNTAHEISAYSLPALAKAARPMMRGRNSAIVALSYLGAVRAIPNYN 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1270051604 184 AYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK08690  159 VMGMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKT 195
PRK07814 PRK07814
SDR family oxidoreductase;
35-216 1.22e-03

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 40.15  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIKETYKFVAQYLPENRG 114
Cdd:PRK07814    8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 115 LWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKER--GRIINLASIGGRTCLPHASAYSISKFGV 192
Cdd:PRK07814   88 LDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSggGSVINISSTMGRLAGRGFAAYGTAKAAL 167

                         170       180
                  ....*....|....*....|....
gi 1270051604 193 EAFSDALRRELGPTgVKVSIVEPG 216
Cdd:PRK07814  168 AHYTRLAALDLCPR-IRVNAIAPG 190
PRK09186 PRK09186
flagellin modification protein A; Provisional
 35-216 1.61e-03

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 39.59  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  35 LQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEG----QENLTAAC-SKRLTALHLDVTDSKEIKETYKFVAQYL 109
Cdd:PRK09186    2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEAlnelLESLGKEFkSKKLSLVELDITDQESLEEFLSKSAEKY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 110 PEnrgLWGLVNNA-----GIAKVgpIEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKK-ERGRIINLASIGG-------- 175
Cdd:PRK09186   82 GK---IDGAVNCAyprnkDYGKK--FFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKqGGGNLVNISSIYGvvapkfei 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1270051604 176 --RTCLPHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:PRK09186  157 yeGTSMTSPVEYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPG 199
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 33-201 1.62e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 39.60  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  33 TDLQQKYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAAcskRLTALHLDV----TDSKEIKETYKFVAQY 108
Cdd:PRK06198    2 GRLDGKVALVTGGTQGLGAAIARAFAERGAAGLVICGRNAEKGEAQAA---ELEALGAKAvfvqADLSDVEDCRRVVAAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 109 LPENRGLWGLVNNAGIAKVGPIEWQTIEEFKQIADVNLWG---LI-DVTKVFLPliKKERGRIINLASIGGRTCLPHASA 184
Cdd:PRK06198   79 DEAFGRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRApffLMqEAIKLMRR--RKAEGTIVNIGSMSAHGGQPFLAA 156

                         170       180
                  ....*....|....*....|.
gi 1270051604 185 YSISKFGVEAFSD----ALRR 201
Cdd:PRK06198  157 YCASKGALATLTRnaayALLR 177
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
132-223 2.23e-03

decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 39.31  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 132 WQTIEEFKQIADVNLWGLIDVtKVFLPLIKKERG--RIINLASIGGRTCLPHASAYSISKFGVEAFSDALRRELGPTGVK 209
Cdd:PRK07904  105 WQNQRKAVQIAEINYTAAVSV-GVLLGEKMRAQGfgQIIAMSSVAGERVRRSNFVYGSTKAGLDGFYLGLGEALREYGVR 183

                          90
                  ....*....|....
gi 1270051604 210 VSIVEPGFFQTKIT 223
Cdd:PRK07904  184 VLVVRPGQVRTRMS 197
PRK08177 PRK08177
SDR family oxidoreductase;
38-220 2.65e-03

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 38.86  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLTSEGQENLTAACSKRLTALHLDVTDSKEIketykfVAQYLPENRgLWG 117
Cdd:PRK08177    2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIEKLDMNDPASLDQ------LLQRLQGQR-FDL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 118 LVNNAGIAkvGP----IEWQTIEEFKQIADVNLWGLIDVTKVFLPLIKKERGRIINLASIGGRTCLP---HASAYSISKF 190
Cdd:PRK08177   75 LFVNAGIS--GPahqsAADATAAEIGQLFLTNAIAPIRLARRLLGQVRPGQGVLAFMSSQLGSVELPdggEMPLYKASKA 152

                         170       180       190
                  ....*....|....*....|....*....|
gi 1270051604 191 GVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK08177  153 ALNSMTRSFVAELGEPTLTVLSMHPGWVKT 182
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 38-216 3.08e-03

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 39.12  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604  38 KYVLVTGCDSGFGRETALRLDSLGFNVFATCLT----SEGQENLTAACSK-RLTALHLDVTDSKEIKetyKFVAQYLPEN 112
Cdd:cd09809     2 KVIIITGANSGIGFETARSFALHGAHVILACRNmsraSAAVSRILEEWHKaRVEAMTLDLASLRSVQ---RFAEAFKAKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270051604 113 RGLWGLVNNAGIAKvgpIEWQ-TIEEFKQIADVNLWG-------LIDVTKVFLP----LIKKERGRIINLASIGGRTCLP 180
Cdd:cd09809    79 SPLHVLVCNAAVFA---LPWTlTEDGLETTFQVNHLGhfylvqlLEDVLRRSAParviVVSSESHRFTDLPDSCGNLDFS 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1270051604 181 HAS----------AYSISKFGVEAFSDALRRELGPTGVKVSIVEPG 216
Cdd:cd09809   156 LLSppkkkywsmlAYNRAKLCNILFSNELHRRLSPRGITSNSLHPG 201
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
143-220 6.30e-03

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 37.78  E-value: 6.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270051604 143 DVNLWGLIDVTKVFLPLIKKeRGRIINLASIGGRTCLPHASAYSISKFGVEAFSDALRRELGPTGVKVSIVEPGFFQT 220
Cdd:PRK06079  116 DISAYSLIAVAKYARPLLNP-GASIVTLTYFGSERAIPNYNVMGIAKAALESSVRYLARDLGKKGIRVNAISAGAVKT 192
 
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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