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Conserved domains on  [gi|50726952|ref|NP_002896|]
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retinol dehydrogenase 5 [Homo sapiens]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10176849)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase similar to corticosteroid 11-beta-dehydrogenase isozyme 2 that catalyzes the conversion of cortisol to the inactive metabolite cortisone; classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 30-306 1.34e-143

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: 405.89  E-value: 1.34e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  30 FVFITGCDSGFGRLLALQLDQRGFRVLASCLTP--SGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEAGLFG 107
Cdd:cd09805   2 AVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLWG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 LVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLAAN-GGGYCVSKFGLEAFS 186
Cdd:cd09805  82 LVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAFS 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 187 DSLRRDVAHFGIRVSIVEPGFFRTPVTNLESL-EKTLQACWARLPPATQAHYGGafltKYLKMQQRIMNLI---CDPDLT 262
Cdd:cd09805 162 DSLRRELQPWGVKVSIIEPGNFKTGITGNSELwEKQAKKLWERLPPEVKKDYGE----DYIDELKNKMLKYcsrASPDLS 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 50726952 263 KVSRCLEHALTARHPRTRYSPGWDAKLLWLPASYLPASLVDAVL 306
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; ...
 30-306 1.34e-143

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: 405.89  E-value: 1.34e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  30 FVFITGCDSGFGRLLALQLDQRGFRVLASCLTP--SGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEAGLFG 107
Cdd:cd09805   2 AVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLWG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 LVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLAAN-GGGYCVSKFGLEAFS 186
Cdd:cd09805  82 LVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAFS 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 187 DSLRRDVAHFGIRVSIVEPGFFRTPVTNLESL-EKTLQACWARLPPATQAHYGGafltKYLKMQQRIMNLI---CDPDLT 262
Cdd:cd09805 162 DSLRRELQPWGVKVSIIEPGNFKTGITGNSELwEKQAKKLWERLPPEVKKDYGE----DYIDELKNKMLKYcsrASPDLS 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 50726952 263 KVSRCLEHALTARHPRTRYSPGWDAKLLWLPASYLPASLVDAVL 306
Cdd:cd09805 238 PVIDSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
31-310 2.38e-46

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 156.95  E-value: 2.38e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQ---RVASSRLHTTLLDITDPQSVQQAAKWVEMHVkeAGLFG 107
Cdd:COG0300   8 VLITGASSGIGRALARALAARGARVVLVARDAERLEALAaelRAAGARVEVVALDVTDPDAVAALAEAVLARF--GPIDV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 LVNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPL-LQQARGRVINITSVLGRLAANG-GGYCVSKFGLEAF 185
Cdd:COG0300  86 LVNNAGV-GGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLmRARGRGRIVNVSSVAGLRGLPGmAAYAASKAALEGF 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 186 SDSLRRDVAHFGIRVSIVEPGFFRTPVtnleslektlqacWARLPPAtqahyggafltkylkMQQRIMnlicDPDltKVS 265
Cdd:COG0300 165 SESLRAELAPTGVRVTAVCPGPVDTPF-------------TARAGAP---------------AGRPLL----SPE--EVA 210

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 50726952 266 RCLEHALtaRHPRTRYSPGWDAKLLWLPASYLPAsLVDAVLTWVL 310
Cdd:COG0300 211 RAILRAL--ERGRAEVYVGWDARLLARLLRLLPR-LFDRLLRRAL 252
PRK08017 PRK08017
SDR family oxidoreductase;
31-308 1.13e-40

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 142.53  E-value: 1.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPsgaEDLQRVASSRLHTTLLDITDPQSVQQAAKWVeMHVKEAGLFGLVN 110
Cdd:PRK08017   5 VLITGCSSGIGLEAALELKRRGYRVLAACRKP---DDVARMNSLGFTGILLDLDDPESVERAADEV-IALTDNRLYGLFN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  111 NAGVaGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLGRLAANG-GGYCVSKFGLEAFSDS 188
Cdd:PRK08017  81 NAGF-GVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLpAMLPHGEGRIVMTSSVMGLISTPGrGAYAASKYALEAWSDA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  189 LRRDVAHFGIRVSIVEPGFFRTPVTnlESLEKTLQ---------ACWARLPPAtqahyggAFLTKylkmqqrimnlicdp 259
Cdd:PRK08017 160 LRMELRHSGIKVSLIEPGPIRTRFT--DNVNQTQSdkpvenpgiAARFTLGPE-------AVVPK--------------- 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 50726952  260 dltkvsrcLEHALTARHPRTRYSPGWDAKLLWLPASYLPASLVDAVLTW 308
Cdd:PRK08017 216 --------LRHALESPKPKLRYPVTLVTHAVMVLKRLLPGRMMDKILRG 256
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 31-213 7.40e-38

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 133.12  E-value: 7.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952    31 VFITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQRVA------SSRLHTTLLDITDPQSVQQAAKWVEMHVKeaG 104
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGAKVV---LVDRSEEKLEAVAkelgalGGKALFIQGDVTDRAQVKALVEQAVERLG--R 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   105 LFGLVNNAGVAGIiGPTPWLTRDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLGRLA-ANGGGYCVSKFGL 182
Cdd:pfam00106  78 LDILVNNAGITGL-GPFSELSDEDWERVIDVNLTGVFNLTRAVLpAMIKGSGGRIVNISSVAGLVPyPGGSAYSASKAAV 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 50726952   183 EAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:pfam00106 157 IGFTRSLALELAPHGIRVNAVAPGGVDTDMT 187
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 30-306 1.34e-143

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: 405.89  E-value: 1.34e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  30 FVFITGCDSGFGRLLALQLDQRGFRVLASCLTP--SGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEAGLFG 107
Cdd:cd09805   2 AVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLWG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 LVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLAAN-GGGYCVSKFGLEAFS 186
Cdd:cd09805  82 LVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAFS 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 187 DSLRRDVAHFGIRVSIVEPGFFRTPVTNLESL-EKTLQACWARLPPATQAHYGGafltKYLKMQQRIMNLI---CDPDLT 262
Cdd:cd09805 162 DSLRRELQPWGVKVSIIEPGNFKTGITGNSELwEKQAKKLWERLPPEVKKDYGE----DYIDELKNKMLKYcsrASPDLS 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 50726952 263 KVSRCLEHALTARHPRTRYSPGWDAKLLWLPASYLPASLVDAVL 306
Cdd:cd09805 238 PVIDSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 30-288 1.84e-59

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: 190.90  E-value: 1.84e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  30 FVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEmhvKEAG-LFGL 108
Cdd:cd05374   2 VVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVI---ERFGrIDVL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 109 VNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLA-ANGGGYCVSKFGLEAFS 186
Cdd:cd05374  79 VNNAGY-GLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGsGRIVNVSSVAGLVPtPFLGPYCASKAALEALS 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 187 DSLRRDVAHFGIRVSIVEPGFFRTPVTNleslektlqacwARLPPATQAHYGG---AFLTKYLKMQQRIMNLICDPDltK 263
Cdd:cd05374 158 ESLRLELAPFGIKVTIIEPGPVRTGFAD------------NAAGSALEDPEISpyaPERKEIKENAAGVGSNPGDPE--K 223

                       250       260
                ....*....|....*....|....*
gi 50726952 264 VSRCLEHALTARHPRTRYSPGWDAK 288
Cdd:cd05374 224 VADVIVKALTSESPPLRYFLGSDAL 248
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
31-310 2.38e-46

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 156.95  E-value: 2.38e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQ---RVASSRLHTTLLDITDPQSVQQAAKWVEMHVkeAGLFG 107
Cdd:COG0300   8 VLITGASSGIGRALARALAARGARVVLVARDAERLEALAaelRAAGARVEVVALDVTDPDAVAALAEAVLARF--GPIDV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 LVNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPL-LQQARGRVINITSVLGRLAANG-GGYCVSKFGLEAF 185
Cdd:COG0300  86 LVNNAGV-GGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLmRARGRGRIVNVSSVAGLRGLPGmAAYAASKAALEGF 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 186 SDSLRRDVAHFGIRVSIVEPGFFRTPVtnleslektlqacWARLPPAtqahyggafltkylkMQQRIMnlicDPDltKVS 265
Cdd:COG0300 165 SESLRAELAPTGVRVTAVCPGPVDTPF-------------TARAGAP---------------AGRPLL----SPE--EVA 210

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 50726952 266 RCLEHALtaRHPRTRYSPGWDAKLLWLPASYLPAsLVDAVLTWVL 310
Cdd:COG0300 211 RAILRAL--ERGRAEVYVGWDARLLARLLRLLPR-LFDRLLRRAL 252
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 31-211 1.05e-43

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: 149.95  E-value: 1.05e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHvkeaglFG--- 107
Cdd:COG4221   8 ALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAE------FGrld 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 -LVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPL-LQQARGRVINITSVLGRLA-ANGGGYCVSKFGLEA 184
Cdd:COG4221  82 vLVNNAGVA-LLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAmRARGSGHIVNISSIAGLRPyPGGAVYAATKAAVRG 160

                       170       180
                ....*....|....*....|....*..
gi 50726952 185 FSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:COG4221 161 LSESLRAELRPTGIRVTVIEPGAVDTE 187
PRK08017 PRK08017
SDR family oxidoreductase;
31-308 1.13e-40

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 142.53  E-value: 1.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPsgaEDLQRVASSRLHTTLLDITDPQSVQQAAKWVeMHVKEAGLFGLVN 110
Cdd:PRK08017   5 VLITGCSSGIGLEAALELKRRGYRVLAACRKP---DDVARMNSLGFTGILLDLDDPESVERAADEV-IALTDNRLYGLFN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  111 NAGVaGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLGRLAANG-GGYCVSKFGLEAFSDS 188
Cdd:PRK08017  81 NAGF-GVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLpAMLPHGEGRIVMTSSVMGLISTPGrGAYAASKYALEAWSDA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  189 LRRDVAHFGIRVSIVEPGFFRTPVTnlESLEKTLQ---------ACWARLPPAtqahyggAFLTKylkmqqrimnlicdp 259
Cdd:PRK08017 160 LRMELRHSGIKVSLIEPGPIRTRFT--DNVNQTQSdkpvenpgiAARFTLGPE-------AVVPK--------------- 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 50726952  260 dltkvsrcLEHALTARHPRTRYSPGWDAKLLWLPASYLPASLVDAVLTW 308
Cdd:PRK08017 216 --------LRHALESPKPKLRYPVTLVTHAVMVLKRLLPGRMMDKILRG 256
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 31-213 7.40e-38

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 133.12  E-value: 7.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952    31 VFITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQRVA------SSRLHTTLLDITDPQSVQQAAKWVEMHVKeaG 104
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGAKVV---LVDRSEEKLEAVAkelgalGGKALFIQGDVTDRAQVKALVEQAVERLG--R 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   105 LFGLVNNAGVAGIiGPTPWLTRDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLGRLA-ANGGGYCVSKFGL 182
Cdd:pfam00106  78 LDILVNNAGITGL-GPFSELSDEDWERVIDVNLTGVFNLTRAVLpAMIKGSGGRIVNISSVAGLVPyPGGSAYSASKAAV 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 50726952   183 EAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:pfam00106 157 IGFTRSLALELAPHGIRVNAVAPGGVDTDMT 187
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 31-211 1.35e-37

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


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 133.95  E-value: 1.35e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDL--QRVASSRLHTTLLDITDPQSVQQAAKWVEMHvkEAGLFGL 108
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELaaIEALGGNAVAVQADVSDEEDVEALVEEALEE--FGRLDIL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 109 VNNAGVAGIiGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLA-ANGGGYCVSKFGLEAFS 186
Cdd:cd05233  79 VNNAGIARP-GPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGgGRIVNISSVAGLRPlPGQAAYAASKAALEGLT 157

                       170       180
                ....*....|....*....|....*
gi 50726952 187 DSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:cd05233 158 RSLALELAPYGIRVNAVAPGLVDTP 182
PRK06914 PRK06914
SDR family oxidoreductase;
32-301 3.41e-37

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 134.00  E-value: 3.41e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   32 FITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDL-----QRVASSRLHTTLLDITDPQSVQQAAKWVEMHvkeAGLF 106
Cdd:PRK06914   7 IVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLlsqatQLNLQQNIKVQQLDVTDQNSIHNFQLVLKEI---GRID 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  107 GLVNNAGVA--GIIGPTPwltRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLAANG-GGYCVSKFGL 182
Cdd:PRK06914  84 LLVNNAGYAngGFVEEIP---VEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGlSPYVSSKYAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  183 EAFSDSLRRDVAHFGIRVSIVEPGFFRTPVtnlesLEKTLQAcwARLPPATQAHYgGAFLTKYLKMQQRIMNLICDPDlt 262
Cdd:PRK06914 161 EGFSESLRLELKPFGIDVALIEPGSYNTNI-----WEVGKQL--AENQSETTSPY-KEYMKKIQKHINSGSDTFGNPI-- 230

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 50726952  263 KVSRCLEHALTARHPRTRYSPGWDAKLLWLPASYLPASL 301
Cdd:PRK06914 231 DVANLIVEIAESKRPKLRYPIGKGVKLMILAKKILPWRL 269
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 32-210 1.72e-36

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 131.96  E-value: 1.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   32 FITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHvkeaglFG---- 107
Cdd:PRK06180   8 LITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEAT------FGpidv 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 LVNNAGVA--GIIGPTPwltRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLAANG-GGYCVSKFGLE 183
Cdd:PRK06180  82 LVNNAGYGheGAIEESP---LAEMRRQFEVNVFGAVAMTKAVLPGMRARRrGHIVNITSMGGLITMPGiGYYCGSKFALE 158

                        170       180
                 ....*....|....*....|....*..
gi 50726952  184 AFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK06180 159 GISESLAKEVAPFGIHVTAVEPGSFRT 185
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 31-306 8.32e-36

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 130.02  E-value: 8.32e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVassrlhTTL-LDITDPQSVQQAAKWVemhVKEAGLFG-L 108
Cdd:PRK06179   7 ALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIPGV------ELLeLDVTDDASVQAAVDEV---IARAGRIDvL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  109 VNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLAANGGG-YCVSKFGLEAFS 186
Cdd:PRK06179  78 VNNAGV-GLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGsGRIINISSVLGFLPAPYMAlYAASKHAVEGYS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  187 DSLRRDVAHFGIRVSIVEPGFFRTpvtnleSLEKTLQACWARLPP-ATQAhyggAFLTKYLKMQqriMNLICDPDLtkVS 265
Cdd:PRK06179 157 ESLDHEVRQFGIRVSLVEPAYTKT------NFDANAPEPDSPLAEyDRER----AVVSKAVAKA---VKKADAPEV--VA 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 50726952  266 RCLEHALTARHPRTRYSPGWDAKLLWLPASYLPASLVDAVL 306
Cdd:PRK06179 222 DTVVKAALGPWPKMRYTAGGQASLLSKLRRFMPAGAVDKSL 262
PRK06182 PRK06182
short chain dehydrogenase; Validated
 31-306 1.58e-35

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 129.31  E-value: 1.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLAscltpsGA---EDLQRVASSRLHTTLLDITDPQSVQQAAKwvEMHVKEAGLFG 107
Cdd:PRK06182   6 ALVTGASSGIGKATARRLAAQGYTVYG------AArrvDKMEDLASLGVHPLSLDVTDEASIKAAVD--TIIAEEGRIDV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 LVNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLAAN-GGGYCVSKFGLEAF 185
Cdd:PRK06182  78 LVNNAGY-GSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIYTPlGAWYHATKFALEGF 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  186 SDSLRRDVAHFGIRVSIVEPGFFRTPVTNL--ESLEKTLqacwARLPPATQAHYGGAFLTKYLKmqqriMNLICDPDLtk 263
Cdd:PRK06182 157 SDALRLEVAPFGIDVVVIEPGGIKTEWGDIaaDHLLKTS----GNGAYAEQAQAVAASMRSTYG-----SGRLSDPSV-- 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 50726952  264 VSRCLEHALTARHPRTRYSPGWDAKLLWLPASYLPASLVDAVL 306
Cdd:PRK06182 226 IADAISKAVTARRPKTRYAVGFGAKPLIFLRRILPDRAFDRLI 268
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 31-230 6.91e-35

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: 127.21  E-value: 6.91e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQ---RVASSRLHTTLLDITDPQSVQQAAKWVemhVKEAG-LF 106
Cdd:COG1028   9 ALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAaelRAAGGRALAVAADVTDEAAVEALVAAA---VAAFGrLD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 107 GLVNNAGVAGIiGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPL-LQQARGRVINITSVLGRLA-ANGGGYCVSKFGLEA 184
Cdd:COG1028  86 ILVNNAGITPP-GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHmRERGGGRIVNISSIAGLRGsPGQAAYAASKAAVVG 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 50726952 185 FSDSLRRDVAHFGIRVSIVEPGFFRTPVT-NLESLEKTLQACWARLP 230
Cdd:COG1028 165 LTRSLALELAPRGIRVNAVAPGPIDTPMTrALLGAEEVREALAARIP 211
PRK05993 PRK05993
SDR family oxidoreductase;
31-308 3.38e-30

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 115.51  E-value: 3.38e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPsgaEDLQRVASSRLHTTLLDITDPQSVQQAAKWVeMHVKEAGLFGLVN 110
Cdd:PRK05993   7 ILITGCSSGIGAYCARALQSDGWRVFATCRKE---EDVAALEAEGLEAFQLDYAEPESIAALVAQV-LELSGGRLDALFN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  111 NaGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLGRLAAN-GGGYCVSKFGLEAFSDS 188
Cdd:PRK05993  83 N-GAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIpVMRKQGQGRIVQCSSILGLVPMKyRGAYNASKFAIEGLSLT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  189 LRRDVAHFGIRVSIVEPGFFRTPVTN--LESLEKtlqacWARLppATQAHYggaflTKYLKMQQRIMN------LICDPD 260
Cdd:PRK05993 162 LRMELQGSGIHVSLIEPGPIETRFRAnaLAAFKR-----WIDI--ENSVHR-----AAYQQQMARLEGggsksrFKLGPE 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 50726952  261 ltKVSRCLEHALTARHPRTRYSPGWDAKLLWLPASYLPASLVDAVLTW 308
Cdd:PRK05993 230 --AVYAVLLHALTAPRPRPHYRVTTPAKQGALLKRLLPARWLYRLLRK 275
PRK05693 PRK05693
SDR family oxidoreductase;
31-206 2.81e-29

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 112.96  E-value: 2.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLAsclTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKwvEMHVKEAGLFGLVN 110
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWA---TARKAEDVEALAAAGFTAVQLDVNDGAALARLAE--ELEAEHGGLDVLIN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  111 NAGVaGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLAAN-GGGYCVSKFGLEAFSDSL 189
Cdd:PRK05693  79 NAGY-GAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTPfAGAYCASKAAVHALSDAL 157

                        170
                 ....*....|....*..
gi 50726952  190 RRDVAHFGIRVSIVEPG 206
Cdd:PRK05693 158 RLELAPFGVQVMEVQPG 174
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 31-210 2.87e-29

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: 112.00  E-value: 2.87e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRG-FRVLASCLTPSGAEDLQ--RVASSRLHTTLLDITDPqsVQQAAKWVEMHVKEAGLFG 107
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSAATELAalGASHSRLHILELDVTDE--IAESAEAVAERLGDAGLDV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 LVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVT-LALLPLLQQARGRVINITSVLGRLAANGGG----YCVSKFGL 182
Cdd:cd05325  79 LINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTqAFLPLLLKGARAKIINISSRVGSIGDNTSGgwysYRASKAAL 158

                       170       180
                ....*....|....*....|....*...
gi 50726952 183 EAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:cd05325 159 NMLTKSLAVELKRDGITVVSLHPGWVRT 186
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 31-213 5.97e-29

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 111.44  E-value: 5.97e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPS-GAEDL---QRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKeaGLF 106
Cdd:PRK05557   8 ALVTGASRGIGRAIAERLAAQGANVVINYASSEaGAEALvaeIGALGGKALAVQGDVSDAESVERAVDEAKAEFG--GVD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  107 GLVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRL-AANGGGYCVSKFGLEA 184
Cdd:PRK05557  86 ILVNNAGIT-RDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRsGRIINISSVVGLMgNPGQANYAASKAGVIG 164

                        170       180
                 ....*....|....*....|....*....
gi 50726952  185 FSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:PRK05557 165 FTKSLARELASRGITVNAVAPGFIETDMT 193
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 31-224 1.93e-28

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: 110.02  E-value: 1.93e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAE---DLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEAGLfg 107
Cdd:cd05339   2 VLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEetaNNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTI-- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 LVNNAGVAgiIGPTPW-LTRDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLGRLAANGGG-YCVSKFGLEA 184
Cdd:cd05339  80 LINNAGVV--SGKKLLeLPDEEIEKTFEVNTLAHFWTTKAFLpDMLERNHGHIVTIASVAGLISPAGLAdYCASKAAAVG 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 50726952 185 FSDSLRRDVAHF---GIRVSIVEPGF-----FRTPVTNLESLEKTLQA 224
Cdd:cd05339 158 FHESLRLELKAYgkpGIKTTLVCPYFintgmFQGVKTPRPLLAPILEP 205
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 28-210 7.65e-28

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: 108.44  E-value: 7.65e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  28 NAFVFITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQRVASSRL-------HTTLLDITDPQSVQQAAKWVEMHV 100
Cdd:cd05332   3 GKVVIITGASSGIGEELAYHLARLGARLV---LSARREERLEEVKSECLelgapspHVVPLDMSDLEDAEQVVEEALKLF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 101 KeaGLFGLVNNAGVAGiigPTPW--LTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLAANG-GGYC 176
Cdd:cd05332  80 G--GLDILINNAGISM---RSLFhdTSIDVDRKIMEVNYFGPVALTKAALPHLIERSqGSIVVVSSIAGKIGVPFrTAYA 154

                       170       180       190
                ....*....|....*....|....*....|....
gi 50726952 177 VSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:cd05332 155 ASKHALQGFFDSLRAELSEPNISVTVVCPGLIDT 188
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 32-210 1.05e-27

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 108.59  E-value: 1.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   32 FITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAakwVEMHVKEAG-LFGLVN 110
Cdd:PRK08263   7 FITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAA---VETAVEHFGrLDIVVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  111 NAGvAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLA-ANGGGYCVSKFGLEAFSDS 188
Cdd:PRK08263  84 NAG-YGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRsGHIIQISSIGGISAfPMSGIYHASKWALEGMSEA 162

                        170       180
                 ....*....|....*....|..
gi 50726952  189 LRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK08263 163 LAQEVAEFGIKVTLVEPGGYST 184
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
31-213 1.53e-27

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 107.55  E-value: 1.53e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQ---RVASSRLHTTLLDITDPQSVQQAakwVEMHVKEAG-LF 106
Cdd:PRK05653   8 ALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAaelRAAGGEARVLVFDVSDEAAVRAL---IEAAVEAFGaLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  107 GLVNNAGVAGIiGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRlAANGGG--YCVSKFGLE 183
Cdd:PRK05653  85 ILVNNAGITRD-ALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARyGRIVNISSVSGV-TGNPGQtnYSAAKAGVI 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 50726952  184 AFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:PRK05653 163 GFTKALALELASRGITVNAVAPGFIDTDMT 192
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 31-213 3.02e-27

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: 106.48  E-value: 3.02e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGA---EDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKeaGLFG 107
Cdd:cd05333   3 ALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAaetVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFG--PVDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 LVNNAGVagiigptpwlTRD---------DFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGrLAANGG--GY 175
Cdd:cd05333  81 LVNNAGI----------TRDnllmrmseeDWDAVINVNLTGVFNVTQAVIRAMIKRRsGRIINISSVVG-LIGNPGqaNY 149

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 50726952 176 CVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:cd05333 150 AASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMT 187
PRK12826 PRK12826
SDR family oxidoreductase;
31-211 4.15e-26

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 103.84  E-value: 4.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAE---DLQRVASSRLHTTLLDITDPQSVQQAAKWVEmhVKEAGLFG 107
Cdd:PRK12826   9 ALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAataELVEAAGGKARARQVDVRDRAALKAAVAAGV--EDFGRLDI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 LVNNAGVAGIiGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLAANGG--GYCVSKFGLEA 184
Cdd:PRK12826  87 LVANAGIFPL-TPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGgGRIVLTSSVAGPRVGYPGlaHYAASKAGLVG 165

                        170       180
                 ....*....|....*....|....*..
gi 50726952  185 FSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK12826 166 FTRALALELAARNITVNSVHPGGVDTP 192
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 32-229 6.97e-26

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: 103.00  E-value: 6.97e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  32 FITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQR---VASSRLHTTLLDITDPQSVQQAakwVEMHVKEAG-LFG 107
Cdd:cd08934   7 LVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADeleAEGGKALVLELDVTDEQQVDAA---VERTVEALGrLDI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 LVNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLGRLAA-NGGGYCVSKFGLEAF 185
Cdd:cd08934  84 LVNNAGI-MLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALpHHLLRNKGTIVNISSVAGRVAVrNSAVYNATKFGVNAF 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 50726952 186 SDSLRRDVAHFGIRVSIVEPGFFRTPVTNLESLEKTLQACWARL 229
Cdd:cd08934 163 SEGLRQEVTERGVRVVVIEPGTVDTELRDHITHTITKEAYEERI 206
PRK09291 PRK09291
SDR family oxidoreductase;
31-210 9.93e-26

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 103.15  E-value: 9.93e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSR---LHTTLLDITDPQSVQQAAKWvEMHVkeaglfg 107
Cdd:PRK09291   5 ILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRglaLRVEKLDLTDAIDRAQAAEW-DVDV------- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 LVNNAGV--AGIIGPTPW-LTRDDFQrvlnVNTMGPIGVTLALLPL-LQQARGRVINITSVLGRLA-ANGGGYCVSKFGL 182
Cdd:PRK09291  77 LLNNAGIgeAGAVVDIPVeLVRELFE----TNVFGPLELTQGFVRKmVARGKGKVVFTSSMAGLITgPFTGAYCASKHAL 152

                        170       180
                 ....*....|....*....|....*...
gi 50726952  183 EAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK09291 153 EAIAEAMHAELKPFGIQVATVNPGPYLT 180
PRK06482 PRK06482
SDR family oxidoreductase;
32-210 1.45e-25

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 102.89  E-value: 1.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   32 FITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAakwVEMHVKEAGLFG-LVN 110
Cdd:PRK06482   6 FITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARYGDRLWVLQLDVTDSAAVRAV---VDRAFAALGRIDvVVS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  111 NAGVaGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLAANGGG-YCVSKFGLEAFSDS 188
Cdd:PRK06482  83 NAGY-GLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGgGRIVQVSSEGGQIAYPGFSlYHATKWGIEGFVEA 161

                        170       180
                 ....*....|....*....|..
gi 50726952  189 LRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK06482 162 VAQEVAPFGIEFTIVEPGPART 183
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 30-206 3.21e-25

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: 101.04  E-value: 3.21e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  30 FVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAakwVEMHVKE-AGLFGL 108
Cdd:cd08929   2 AALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRA---VDAMEEAfGGLDAL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 109 VNNAGVaGIIGPTPWLTRDDFQR-VLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLAANGG-GYCVSKFGLEAFS 186
Cdd:cd08929  79 VNNAGV-GVMKPVEELTPEEWRLvLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGaAYNASKFGLLGLS 157

                       170       180
                ....*....|....*....|
gi 50726952 187 DSLRRDVAHFGIRVSIVEPG 206
Cdd:cd08929 158 EAAMLDLREANIRVVNVMPG 177
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 37-230 1.53e-24

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: 99.04  E-value: 1.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952    37 DSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASsRLHTTLL--DITDPQSVQQAAKWVemhVKEAG-LFGLVNNAG 113
Cdd:pfam13561   5 ESGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAE-ELGAAVLpcDVTDEEQVEALVAAA---VEKFGrLDILVNNAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   114 VAG-IIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQaRGRVINITSVLGRLA-ANGGGYCVSKFGLEAFSDSLRR 191
Cdd:pfam13561  81 FAPkLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKE-GGSIVNLSSIGAERVvPNYNAYGAAKAALEALTRYLAV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 50726952   192 DVAHFGIRVSIVEPGFFRTP-VTNLESLEKTLQACWARLP 230
Cdd:pfam13561 160 ELGPRGIRVNAISPGPIKTLaASGIPGFDELLAAAEARAP 199
PRK07326 PRK07326
SDR family oxidoreductase;
27-206 3.30e-24

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 98.54  E-value: 3.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   27 SNAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQR--VASSRLHTTLLDITDPQSVQQAakwVEMHVKE-A 103
Cdd:PRK07326   5 KGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAelNNKGNVLGLAADVRDEADVQRA---VDAIVAAfG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  104 GLFGLVNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLA-ANGGGYCVSKFGL 182
Cdd:PRK07326  82 GLDVLIANAGV-GHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGTNFfAGGAAYNASKFGL 160

                        170       180
                 ....*....|....*....|....
gi 50726952  183 EAFSDSLRRDVAHFGIRVSIVEPG 206
Cdd:PRK07326 161 VGFSEAAMLDLRQYGIKVSTIMPG 184
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 31-281 3.55e-24

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


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 98.69  E-value: 3.55e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQL---DQRGFRVLASCLTPSGAEDLQRVASSRLHTTL----LDITDPQSVQQAAKWV-EMHVKE 102
Cdd:cd09806   3 VLITGCSSGIGLHLAVRLasdPSKRFKVYATMRDLKKKGRLWEAAGALAGGTLetlqLDVCDSKSVAAAVERVtERHVDV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 103 aglfgLVNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGR--LAANGGgYCVSK 179
Cdd:cd09806  83 -----LVCNAGV-GLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGsGRILVTSSVGGLqgLPFNDV-YCASK 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 180 FGLEAFSDSLRRDVAHFGIRVSIVEPGffrtPVTNlESLEKTLQACWARLPPATQAHYGGAFLTKYLKMQQRIM-NLICD 258
Cdd:cd09806 156 FALEGLCESLAVQLLPFNVHLSLIECG----PVHT-AFMEKVLGSPEEVLDRTADDITTFHFFYQYLAHSKQVFrEAAQN 230

                       250       260
                ....*....|....*....|...
gi 50726952 259 PDltKVSRCLEHALTARHPRTRY 281
Cdd:cd09806 231 PE--EVAEVFLTAIRAPKPPLRY 251
PRK05650 PRK05650
SDR family oxidoreductase;
31-217 4.46e-24

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 98.96  E-value: 4.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRV-LASCLTPSGAEDLQRV--ASSRLHTTLLDITDPQSVQQAAKWVEmhVKEAGLFG 107
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLaLADVNEEGGEETLKLLreAGGDGFYQRCDVRDYSQLTALAQACE--EKWGGIDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 LVNNAGVA--GIIGPtpwLTRDDFQRVLNVNTMGPI-GVTLALLPLLQQARGRVINITSVLGRLAANG-GGYCVSKFGLE 183
Cdd:PRK05650  81 IVNNAGVAsgGFFEE---LSLEDWDWQIAINLMGVVkGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAmSSYNVAKAGVV 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 50726952  184 AFSDSLRRDVAHFGIRVSIVEPGFFRtpvTNLES 217
Cdd:PRK05650 158 ALSETLLVELADDEIGVHVVCPSFFQ---TNLLD 188
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 31-206 2.95e-23

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: 96.20  E-value: 2.95e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQRVAS-------SRLHTTLLDITDPQSVQQA-----AKWVEM 98
Cdd:cd05346   3 VLITGASSGIGEATARRFAKAGAKLI---LTGRRAERLQELADelgakfpVKVLPLQLDVSDRESIEAAlenlpEEFRDI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  99 HVkeaglfgLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLGRLA-ANGGGYC 176
Cdd:cd05346  80 DI-------LVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILpIMIARNQGHIINLGSIAGRYPyAGGNVYC 152

                       170       180       190
                ....*....|....*....|....*....|
gi 50726952 177 VSKFGLEAFSDSLRRDVAHFGIRVSIVEPG 206
Cdd:cd05346 153 ATKAAVRQFSLNLRKDLIGTGIRVTNIEPG 182
PRK07832 PRK07832
SDR family oxidoreductase;
29-214 7.67e-23

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 95.49  E-value: 7.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   29 AFVFITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQRVASS--------RLHTTLlDITDPQSVQQAAKwvEMHV 100
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELF---LTDRDADGLAQTVADaralggtvPEHRAL-DISDYDAVAAFAA--DIHA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  101 KEAGLFGLVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGV--TLALLPLLQQARGRVINITSVLGRLAAN-GGGYCV 177
Cdd:PRK07832  75 AHGSMDVVMNIAGIS-AWGTVDRLTHEQWRRMVDVNLMGPIHVieTFVPPMVAAGRGGHLVNVSSAAGLVALPwHAAYSA 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 50726952  178 SKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTN 214
Cdd:PRK07832 154 SKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVN 190
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 31-211 2.19e-22

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: 93.47  E-value: 2.19e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPS----GAEDLQRVA---SSRLHTTLLDITDPQSVQQAakWVEMHVKEA 103
Cdd:cd08939   4 VLITGGSSGIGKALAKELVKEGANVIIVARSESkleeAVEEIEAEAnasGQKVSYISADLSDYEEVEQA--FAQAVEKGG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 104 GLFGLVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLAANG-GGYCVSKFG 181
Cdd:cd08939  82 PPDLVVNCAGIS-IPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRpGHIVFVSSQAALVGIYGySAYCPSKFA 160

                       170       180       190
                ....*....|....*....|....*....|
gi 50726952 182 LEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:cd08939 161 LRGLAESLRQELKPYNIRVSVVYPPDTDTP 190
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 31-211 2.70e-22

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 93.39  E-value: 2.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCltPSGAEDLQRVASS------RLHTTLLDITDPQSVQQAakwVEMHVKEAG 104
Cdd:PRK12825   9 ALVTGAARGLGRAIALRLARAGADVVVHY--RSDEEAAEELVEAvealgrRAQAVQADVTDKAALEAA---VAAAVERFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  105 -LFGLVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGrLAANGG--GYCVSKF 180
Cdd:PRK12825  84 rIDILVNNAGIF-EDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRgGRIVNISSVAG-LPGWPGrsNYAAAKA 161

                        170       180       190
                 ....*....|....*....|....*....|.
gi 50726952  181 GLEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK12825 162 GLVGLTKALARELAEYGITVNMVAPGDIDTD 192
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 30-218 3.81e-22

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: 92.43  E-value: 3.81e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  30 FVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAeDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKeaGLFGLV 109
Cdd:cd08932   2 VALVTGASRGIGIEIARALARDGYRVSLGLRNPEDL-AALSASGGDVEAVPYDARDPEDARALVDALRDRFG--RIDVLV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 110 NNAGvagIIGPTPWL--TRDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLGRLAANG-GGYCVSKFGLEAF 185
Cdd:cd08932  79 HNAG---IGRPTTLRegSDAELEAHFSINVIAPAELTRALLpALREAGSGRVVFLNSLSGKRVLAGnAGYSASKFALRAL 155

                       170       180       190
                ....*....|....*....|....*....|...
gi 50726952 186 SDSLRRDVAHFGIRVSIVEPGFFRTPVTNLESL 218
Cdd:cd08932 156 AHALRQEGWDHGVRVSAVCPGFVDTPMAQGLTL 188
PRK08264 PRK08264
SDR family oxidoreductase;
28-213 8.83e-22

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 91.87  E-value: 8.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   28 NAFVFITGCDSGFGRLLALQLDQRGFR-VLASCLTPSGAEDLQrvasSRLHTTLLDITDPQSVQQAAKwvemHVKEAGLf 106
Cdd:PRK08264   6 GKVVLVTGANRGIGRAFVEQLLARGAAkVYAAARDPESVTDLG----PRVVPLQLDVTDPASVAAAAE----AASDVTI- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  107 gLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLA-LLPLLQQARGRVINITSVLGRLA-ANGGGYCVSKFGLEA 184
Cdd:PRK08264  77 -LVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAfAPVLAANGGGAIVNVLSVLSWVNfPNLGTYSASKAAAWS 155

                        170       180
                 ....*....|....*....|....*....
gi 50726952  185 FSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:PRK08264 156 LTQALRAELAPQGTRVLGVHPGPIDTDMA 184
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 21-308 1.20e-20

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 90.37  E-value: 1.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   21 RQSLPASNAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTL---LDITDPQSVQQAAKWVE 97
Cdd:PRK07109   1 MMLKPIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALavvADVADAEAVQAAADRAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   98 mhvKEAGLFGL-VNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPI-GVTLALLPLLQQARGRVINITSVLGR-----LAA 170
Cdd:PRK07109  81 ---EELGPIDTwVNNAMV-TVFGPFEDVTPEEFRRVTEVTYLGVVhGTLAALRHMRPRDRGAIIQVGSALAYrsiplQSA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  171 ngggYCVSKFGLEAFSDSLRRDVAHFG--IRVSIVEPGFFRTPvtnleslektlQACWARlppatqahyggafltKYLKM 248
Cdd:PRK07109 157 ----YCAAKHAIRGFTDSLRCELLHDGspVSVTMVQPPAVNTP-----------QFDWAR---------------SRLPV 206

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  249 QQRIMNLICDPDLtkVSRCLEHAltARHPRTRYSPGWDAKLLWLpASYLPASLVDAVLTW 308
Cdd:PRK07109 207 EPQPVPPIYQPEV--VADAILYA--AEHPRRELWVGGPAKAAIL-GNRLAPGLLDRYLAR 261
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 31-211 1.59e-20

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: 88.21  E-value: 1.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLL---DITDPQSVQQAAKWVEMHvkeaglFG 107
Cdd:cd05360   3 VVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAIAvvaDVADAAQVERAADTAVER------FG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 ----LVNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPI-GVTLALLPLLQQARGRVINITSVLG-RLAANGGGYCVSKFG 181
Cdd:cd05360  77 ridtWVNNAGV-AVFGRFEDVTPEEFRRVFDVNYLGHVyGTLAALPHLRRRGGGALINVGSLLGyRSAPLQAAYSASKHA 155

                       170       180       190
                ....*....|....*....|....*....|..
gi 50726952 182 LEAFSDSLRRDVAHFG--IRVSIVEPGFFRTP 211
Cdd:cd05360 156 VRGFTESLRAELAHDGapISVTLVQPTAMNTP 187
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 27-213 2.46e-20

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: 87.85  E-value: 2.46e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  27 SNAFVFITGCDSGFGRLLALQLDQRGF-RVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAA---KWVEMhvke 102
Cdd:cd05354   2 KDKTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAaqaKDVDV---- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 103 aglfgLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLGRLA-ANGGGYCVSKF 180
Cdd:cd05354  78 -----VINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFApVLKANGGGAIVNLNSVASLKNfPAMGTYSASKS 152

                       170       180       190
                ....*....|....*....|....*....|...
gi 50726952 181 GLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:cd05354 153 AAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMA 185
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 31-210 3.06e-20

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: 87.29  E-value: 3.06e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGF-RVLascLTpsgAEDLQRV-----------ASSRLHttLLDITDPQSVQQAAKWVEM 98
Cdd:cd05324   3 ALVTGANRGIGFEIVRQLAKSGPgTVI---LT---ARDVERGqaaveklraegLSVRFH--QLDVTDDASIEAAADFVEE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  99 hvKEAGLFGLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLGRLAAnggGYCV 177
Cdd:cd05324  75 --KYGGLDILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLpLLKKSPAGRIVNVSSGLGSLTS---AYGV 149

                       170       180       190
                ....*....|....*....|....*....|...
gi 50726952 178 SKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:cd05324 150 SKAALNALTRILAKELKETGIKVNACCPGWVKT 182
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 27-211 1.57e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 85.92  E-value: 1.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   27 SNAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTpsgAEDLQRVASSRLHTTL-LDITDPQSVQQAAKwvemhvkEAGL 105
Cdd:PRK07060   8 SGKSVLVTGASSGIGRACAVALAQRGARVVAAARN---AAALDRLAGETGCEPLrLDVGDDAAIRAALA-------AAGA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  106 F-GLVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQ--ARGRVINITSVLGRLA-ANGGGYCVSKFG 181
Cdd:PRK07060  78 FdGLVNCAGIA-SLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAagRGGSIVNVSSQAALVGlPDHLAYCASKAA 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 50726952  182 LEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK07060 157 LDAITRVLCVELGPHGIRVNSVNPTVTLTP 186
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 31-213 1.93e-19

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 85.79  E-value: 1.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRV-LASCLTPSGAEDLQRVASS--RLHTTLLDITDPQSVQQAAKWVEMHVkeAGLFG 107
Cdd:PRK12939  10 ALVTGAARGLGAAFAEALAEAGATVaFNDGLAAEARELAAALEAAggRAHAIAADLADPASVQRFFDAAAAAL--GGLDG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 LVNNAGVAGIIGPTPwLTRDDFQRVLNVNTMGPIGVTLALLPL-LQQARGRVINI-TSVLGRLAANGGGYCVSKFGLEAF 185
Cdd:PRK12939  88 LVNNAGITNSKSATE-LDIDTWDAVMNVNVRGTFLMLRAALPHlRDSGRGRIVNLaSDTALWGAPKLGAYVASKGAVIGM 166

                        170       180
                 ....*....|....*....|....*...
gi 50726952  186 SDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:PRK12939 167 TRSLARELGGRGITVNAIAPGLTATEAT 194
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 31-214 3.12e-19

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: 85.07  E-value: 3.12e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASC-----LTPSGAEDLQRVASSRLHTtlLDITDPQSVQqaaKWVEMHVKEAGL 105
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAArrtdrLDELKAELLNPNPSVEVEI--LDVTDEERNQ---LVIAELEAELGG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 106 FGL-VNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPI-GVTLALLPLLQQARGRVINITSVLG-RLAANGGGYCVSKFGL 182
Cdd:cd05350  76 LDLvIINAGV-GKGTSLGDLSFKAFRETIDTNLLGAAaILEAALPQFRAKGRGHLVLISSVAAlRGLPGAAAYSASKAAL 154

                       170       180       190
                ....*....|....*....|....*....|..
gi 50726952 183 EAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTN 214
Cdd:cd05350 155 SSLAESLRYDVKKRGIRVTVINPGFIDTPLTA 186
PRK07454 PRK07454
SDR family oxidoreductase;
30-217 7.33e-19

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 83.86  E-value: 7.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   30 FVFITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQRVAS------SRLHTTLLDITDPQSVQQAakwvemhVKE- 102
Cdd:PRK07454   8 RALITGASSGIGKATALAFAKAGWDLA---LVARSQDALEALAAelrstgVKAAAYSIDLSNPEAIAPG-------IAEl 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  103 AGLFG----LVNNAGVA--GIIGPTPWltrDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLA-ANGGG 174
Cdd:PRK07454  78 LEQFGcpdvLINNAGMAytGPLLEMPL---SDWQWVIQLNLTSVFQCCSAVLPGMRARGgGLIINVSSIAARNAfPQWGA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 50726952  175 YCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTNLES 217
Cdd:PRK07454 155 YCVSKAALAAFTKCLAEEERSHGIRVCTITLGAVNTPLWDTET 197
PRK06484 PRK06484
short chain dehydrogenase; Validated
 31-214 1.82e-18

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 85.67  E-value: 1.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAakwveMHvKEAGLFG--- 107
Cdd:PRK06484 272 VAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESA-----FA-QIQARWGrld 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 -LVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIgVTLALLPLLQQARGRVINITSVLGRLAANG-GGYCVSKFGLEAF 185
Cdd:PRK06484 346 vLVNNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAF-ACARAAARLMSQGGVIVNLGSIASLLALPPrNAYCASKAAVTML 424

                        170       180
                 ....*....|....*....|....*....
gi 50726952  186 SDSLRRDVAHFGIRVSIVEPGFFRTPVTN 214
Cdd:PRK06484 425 SRSLACEWAPAGIRVNTVAPGYIETPAVL 453
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 31-211 2.54e-18

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


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 82.81  E-value: 2.54e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRV-LASCLTPSGAEDLQRVASS---RLHTTLLDITDPQSVQQAakwVEMHVKEAGLF 106
Cdd:cd05366   5 AIITGAAQGIGRAIAERLAADGFNIvLADLNLEEAAKSTIQEISEagyNAVAVGADVTDKDDVEAL---IDQAVEKFGSF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 107 G-LVNNAGVAGIigpTPWL--TRDDFQRVLNVNTMGPI-GVTLALLPLLQQAR-GRVINITSVLGRLA-ANGGGYCVSKF 180
Cdd:cd05366  82 DvMVNNAGIAPI---TPLLtiTEEDLKKVYAVNVFGVLfGIQAAARQFKKLGHgGKIINASSIAGVQGfPNLGAYSASKF 158

                       170       180       190
                ....*....|....*....|....*....|.
gi 50726952 181 GLEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:cd05366 159 AVRGLTQTAAQELAPKGITVNAYAPGIVKTE 189
PRK09072 PRK09072
SDR family oxidoreductase;
27-205 4.29e-18

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 82.30  E-value: 4.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   27 SNAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQR--VASSRLHTTLLDITDPQSVQQAAKWVEMHvkeAG 104
Cdd:PRK09072   4 KDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAArlPYPGRHRWVVADLTSEAGREAVLARAREM---GG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  105 LFGLVNNAGVAGIIgptpWLTR---DDFQRVLNVNTMGPIGVTLAL-LPLLQQARGRVINITSVLGRLAANG-GGYCVSK 179
Cdd:PRK09072  81 INVLINNAGVNHFA----LLEDqdpEAIERLLALNLTAPMQLTRALlPLLRAQPSAMVVNVGSTFGSIGYPGyASYCASK 156

                        170       180
                 ....*....|....*....|....*.
gi 50726952  180 FGLEAFSDSLRRDVAHFGIRVSIVEP 205
Cdd:PRK09072 157 FALRGFSEALRRELADTGVRVLYLAP 182
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 31-210 4.65e-18

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 82.30  E-value: 4.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRV----LASCLTPSGAEDLQRVASSRLhttllDITDPQSVQQAAKWVEMHvkeaglF 106
Cdd:PRK07825   8 VAITGGARGIGLATARALAALGARVaigdLDEALAKETAAELGLVVGGPL-----DVTDPASFAAFLDAVEAD------L 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  107 G----LVNNAGVAGIigpTPWLTRDD--FQRVLNVNTMGPI-GVTLALLPLLQQARGRVINITSVLGRLAANGGG-YCVS 178
Cdd:PRK07825  77 GpidvLVNNAGVMPV---GPFLDEPDavTRRILDVNVYGVIlGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMAtYCAS 153

                        170       180       190
                 ....*....|....*....|....*....|..
gi 50726952  179 KFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK07825 154 KHAVVGFTDAARLELRGTGVHVSVVLPSFVNT 185
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 31-235 6.27e-18

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: 80.96  E-value: 6.27e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQ-RVASSRLHTTLLDITDPQSVQQAAKwvEMHVKEAG-LFGL 108
Cdd:cd08931   3 IFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAaELGAENVVAGALDVTDRAAWAAALA--DFAAATGGrLDAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 109 VNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPI-GVTLALLPLLQQARGRVINITSVLG-----RLAAngggYCVSKFGL 182
Cdd:cd08931  81 FNNAGV-GRGGPFEDVPLAAHDRMVDINVKGVLnGAYAALPYLKATPGARVINTASSSAiygqpDLAV----YSATKFAV 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 50726952 183 EAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTNLESLEKTLQACWARLPPATQA 235
Cdd:cd08931 156 RGLTEALDVEWARHGIRVADVWPWFVDTPILTKGETGAAPKKGLGRVLPVSDV 208
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 31-211 6.34e-18

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 81.64  E-value: 6.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQ-RVASSRLHTTLLDITDPQSVQQAAKWVEMHVkeAGLFGLV 109
Cdd:PRK12829  14 VLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAaRLPGAKVTATVADVADPAQVERVFDTAVERF--GGLDVLV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  110 NNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPI-GVTLALLPLLQQARGRVI-NITSVLGRLAANGG-GYCVSKFGLEAFS 186
Cdd:PRK12829  92 NNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFyFARAAVPLLKASGHGGVIiALSSVAGRLGYPGRtPYAASKWAVVGLV 171

                        170       180
                 ....*....|....*....|....*
gi 50726952  187 DSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK12829 172 KSLAIELGPLGIRVNAILPGIVRGP 196
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 27-214 8.08e-18

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


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 81.30  E-value: 8.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  27 SNAFVFITGCDSGFGRLLALQLDQRGFRVlasCLTPSGAEDLQRVASSRLHTTLL---------DITDPQSVQQAAKWVE 97
Cdd:cd05364   2 SGKVAIITGSSSGIGAGTAILFARLGARL---ALTGRDAERLEETRQSCLQAGVSekkillvvaDLTEEEGQDRIISTTL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  98 MHvkeaglFG----LVNNAGVAGIIGPTPwLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLAANGG 173
Cdd:cd05364  79 AK------FGrldiLVNNAGILAKGGGED-QDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGRSFPGV 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 50726952 174 -GYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTN 214
Cdd:cd05364 152 lYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHR 193
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
33-211 1.23e-17

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 80.58  E-value: 1.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLASCLTPSGA----EDLQRVASSRLHTTLLDITDPQSVQQAAKwvEMHVKEAGLFGL 108
Cdd:PRK12824   7 VTGAKRGIGSAIARELLNDGYRVIATYFSGNDCakdwFEEYGFTEDQVRLKELDVTDTEECAEALA--EIEEEEGPVDIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  109 VNNAGVagiigptpwlTRD---------DFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLAANGG-GYCV 177
Cdd:PRK12824  85 VNNAGI----------TRDsvfkrmshqEWNDVINTNLNSVFNVTQPLFAAMCEQGyGRIINISSVNGLKGQFGQtNYSA 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 50726952  178 SKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK12824 155 AKAGMIGFTKALASEGARYGITVNCIAPGYIATP 188
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 22-205 1.65e-17

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 80.12  E-value: 1.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   22 QSLPASNAFvfITGCDSGFGRLLALQLDQRGFRVlasCLTPSGAEDLQRVASS------RLHTTLLDITDPQSVQQAAKW 95
Cdd:PRK07666   3 QSLQGKNAL--ITGAGRGIGRAVAIALAKEGVNV---GLLARTEENLKAVAEEveaygvKVVIATADVSDYEEVTAAIEQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   96 VEMHVKEAGLfgLVNNAGVAGIiGPTPWLTRDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLG-RLAANGG 173
Cdd:PRK07666  78 LKNELGSIDI--LINNAGISKF-GKFLELDPAEWEKIIQVNLMGVYYATRAVLpSMIERQSGDIINISSTAGqKGAAVTS 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 50726952  174 GYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEP 205
Cdd:PRK07666 155 AYSASKFGVLGLTESLMQEVRKHNIRVTALTP 186
PRK05855 PRK05855
SDR family oxidoreductase;
31-214 2.08e-17

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 82.72  E-value: 2.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAE---DLQRVASSRLHTTLLDITDPQSVQQAAKWVemhVKEAGLFG 107
Cdd:PRK05855 318 VVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAErtaELIRAAGAVAHAYRVDVSDADAMEAFAEWV---RAEHGVPD 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 -LVNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPI-------------GVTlallpllqqarGRVINITSVLGRLAANG- 172
Cdd:PRK05855 395 iVVNNAGI-GMAGGFLDTSAEDWDRVLDVNLWGVIhgcrlfgrqmverGTG-----------GHIVNVASAAAYAPSRSl 462

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 50726952  173 GGYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTN 214
Cdd:PRK05855 463 PAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVA 504
PRK08267 PRK08267
SDR family oxidoreductase;
31-253 3.56e-17

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 79.60  E-value: 3.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQR-VASSRLHTTLLDITDPQSVQQAAKwvEMHVKEAG-LFGL 108
Cdd:PRK08267   4 IFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAeLGAGNAWTGALDVTDRAAWDAALA--DFAAATGGrLDVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  109 VNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPI-GVTLALLPLLQQARGRVINITSVLG-----RLAAngggYCVSKFGL 182
Cdd:PRK08267  82 FNNAGI-LRGGPFEDIPLEAHDRVIDINVKGVLnGAHAALPYLKATPGARVINTSSASAiygqpGLAV----YSATKFAV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  183 EAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTNLESLE------KTL----------QACWARLPPATQAHYGGAFLTKYL 246
Cdd:PRK08267 157 RGLTEALDLEWRRHGIRVADVMPLFVDTAMLDGTSNEvdagstKRLgvrltpedvaEAVWAAVQHPTRLHWPVGKQAKLL 236


                 ....*..
gi 50726952  247 KMQQRIM 253
Cdd:PRK08267 237 AFLARLS 243
PRK06484 PRK06484
short chain dehydrogenase; Validated
 31-216 3.83e-17

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 81.82  E-value: 3.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHvkeaglFG--- 107
Cdd:PRK06484   8 VLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHRE------FGrid 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 -LVNNAGvagIIGPTPWLTRD----DFQRVLNVNTMGPIGVTLALLPLLQQAR--GRVINITSVLGrLAANGG--GYCVS 178
Cdd:PRK06484  82 vLVNNAG---VTDPTMTATLDttleEFARLQAINLTGAYLVAREALRLMIEQGhgAAIVNVASGAG-LVALPKrtAYSAS 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 50726952  179 KFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTP-VTNLE 216
Cdd:PRK06484 158 KAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQmVAELE 196
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 31-200 4.44e-17

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: 79.05  E-value: 4.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLAScltpsG--AEDLQRVASSR--LHTTLLDITDPQSVQQAAKWVemhvKEA--G 104
Cdd:COG3967   8 ILITGGTSGIGLALAKRLHARGNTVIIT-----GrrEEKLEEAAAANpgLHTIVLDVADPASIAALAEQV----TAEfpD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 105 LFGLVNNAGVAGII----GPTPWltrDDFQRVLNVNTMGPIGVTLALLPL-LQQARGRVINITSVLGRL-AANGGGYCVS 178
Cdd:COG3967  79 LNVLINNAGIMRAEdlldEAEDL---ADAEREITTNLLGPIRLTAAFLPHlKAQPEAAIVNVSSGLAFVpLAVTPTYSAT 155

                       170       180
                ....*....|....*....|..
gi 50726952 179 KFGLEAFSDSLRRDVAHFGIRV 200
Cdd:COG3967 156 KAALHSYTQSLRHQLKDTSVKV 177
PRK08219 PRK08219
SDR family oxidoreductase;
33-211 4.66e-17

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 78.44  E-value: 4.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLdQRGFRVLASClTPSGAEDLQRVASSRLHTTLLDITDPQSVQQA-AKWVEMHVkeaglfgLVNN 111
Cdd:PRK08219   8 ITGASRGIGAAIAREL-APTHTLLLGG-RPAERLDELAAELPGATPFPVDLTDPEAIAAAvEQLGRLDV-------LVHN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  112 AGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLA-ANGGGYCVSKFGLEAFSDSLR 190
Cdd:PRK08219  79 AGVA-DLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRAnPGWGSYAASKFALRALADALR 157

                        170       180
                 ....*....|....*....|.
gi 50726952  191 RDvAHFGIRVSIVEPGFFRTP 211
Cdd:PRK08219 158 EE-EPGNVRVTSVHPGRTDTD 177
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 31-231 5.24e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 79.63  E-value: 5.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRV--ASSRLHTTLLDITDPQSVQQAAKwvemHVKEAglFG- 107
Cdd:PRK05872  12 VVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAElgGDDRVLTVVADVTDLAAMQAAAE----EAVER--FGg 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 ---LVNNAGVAGiigPTPWLTRD--DFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSvLGRLAANGGG--YCVSKF 180
Cdd:PRK05872  86 idvVVANAGIAS---GGSVAQVDpdAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSS-LAAFAAAPGMaaYCASKA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 50726952  181 GLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT-----NLESLEKTLqacwARLPP 231
Cdd:PRK05872 162 GVEAFANALRLEVAHHGVTVGSAYLSWIDTDLVrdadaDLPAFRELR----ARLPW 213
FabG-like PRK07231
SDR family oxidoreductase;
33-211 6.75e-17

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 78.72  E-value: 6.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVlasCLTPSGAEDLQRVAS-----SRLHTTLLDITDPQSVQQAakwVEMHVKEaglFG 107
Cdd:PRK07231  10 VTGASSGIGEGIARRFAAEGARV---VVTDRNEEAAERVAAeilagGRAIAVAADVSDEADVEAA---VAAALER---FG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 ----LVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLG-RLAANGGGYCVSKFG 181
Cdd:PRK07231  81 svdiLVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGgGAIVNVASTAGlRPRPGLGWYNASKGA 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 50726952  182 LEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK07231 161 VITLTKALAAELGPDKIRVNAVAPVVVETG 190
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 31-211 9.51e-17

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: 78.28  E-value: 9.51e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVassrLHTTLLDITDPQSV-QQAAKWVEMHvkeAGLFGLV 109
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYGDP----LRLTPLDVADAAAVrEVCSRLLAEH---GPIDALV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 110 NNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITS-VLGRLAANGGGYCVSKFGLEAFSD 187
Cdd:cd05331  74 NCAGVL-RPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRtGAIVTVASnAAHVPRISMAAYGASKAALASLSK 152

                       170       180
                ....*....|....*....|....
gi 50726952 188 SLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:cd05331 153 CLGLELAPYGVRCNVVSPGSTDTA 176
PRK12743 PRK12743
SDR family oxidoreductase;
33-216 1.51e-16

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 77.77  E-value: 1.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVlaSCLTPSGAEDLQRVAS------SRLHTTLLDITDPqsvQQAAKWVEMHVKE-AGL 105
Cdd:PRK12743   7 VTASDSGIGKACALLLAQQGFDI--GITWHSDEEGAKETAEevrshgVRAEIRQLDLSDL---PEGAQALDKLIQRlGRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  106 FGLVNNAGvAGIIGPTPWLTRDDFQRVLNVNTMGPI--GVTLALLPLLQQARGRVINITSVLGRLAANGGG-YCVSKFGL 182
Cdd:PRK12743  82 DVLVNNAG-AMTKAPFLDMDFDEWRKIFTVDVDGAFlcSQIAARHMVKQGQGGRIINITSVHEHTPLPGASaYTAAKHAL 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 50726952  183 EAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTNLE 216
Cdd:PRK12743 161 GGLTKAMALELVEHGILVNAVAPGAIATPMNGMD 194
PRK06181 PRK06181
SDR family oxidoreductase;
31-210 2.07e-16

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 77.33  E-value: 2.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTL---LDITDPQSVQQAakwVEMHVKEaglFG 107
Cdd:PRK06181   4 VIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALvvpTDVSDAEACERL---IEAAVAR---FG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 ----LVNNAGVagiigpTPWLTRDD------FQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLAANG-GGYC 176
Cdd:PRK06181  78 gidiLVNNAGI------TMWSRFDEltdlsvFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTrSGYA 151

                        170       180       190
                 ....*....|....*....|....*....|....
gi 50726952  177 VSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK06181 152 ASKHALHGFFDSLRIELADDGVAVTVVCPGFVAT 185
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 33-211 2.30e-16

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 77.33  E-value: 2.30e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  33 ITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRvASSRLHTTLLDITDPQSVQQAAKWVEmhVKEAGLFGLVNNA 112
Cdd:cd05371   7 VTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAK-LGDNCRFVPVDVTSEKDVKAALALAK--AKFGRLDIVVNCA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 113 GVA------GIIGPTPwLTRDDFQRVLNVNTMGPIGVTLALLPLLQQA-------RGRVINITSVlgrlAANGG-----G 174
Cdd:cd05371  84 GIAvaaktyNKKGQQP-HSLELFQRVINVNLIGTFNVIRLAAGAMGKNepdqggeRGVIINTASV----AAFEGqigqaA 158

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 50726952 175 YCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:cd05371 159 YSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTP 195
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 31-206 2.34e-16

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: 76.58  E-value: 2.34e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSrLHTTLLDITDPQSVQQAAKWVEMHVKEagLFGLVN 110
Cdd:cd05370   8 VLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN-IHTIVLDVGDAESVEALAEALLSEYPN--LDILIN 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 111 NAGVA---GIIGPTPWLtrDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLGRLA-ANGGGYCVSKFGLEAF 185
Cdd:cd05370  85 NAGIQrpiDLRDPASDL--DKADTEIDTNLIGPIRLIKAFLpHLKKQPEATIVNVSSGLAFVPmAANPVYCATKAALHSY 162

                       170       180
                ....*....|....*....|..
gi 50726952 186 SDSLRRDVAHFGIRV-SIVEPG 206
Cdd:cd05370 163 TLALRHQLKDTGVEVvEIVPPA 184
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 23-213 2.46e-16

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: 77.01  E-value: 2.46e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  23 SLPASNAFVfiTGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASS---RLHTTLLDITDPQSVQQAakwVEMH 99
Cdd:cd05347   2 SLKGKVALV--TGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKegvEATAFTCDVSDEEAIKAA---VEAI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 100 VKEAGLFG-LVNNAGvagIIGPTPWL--TRDDFQRVLNVNTMGPIGVTLALLPLLQ-QARGRVINITSVLGRLAANG-GG 174
Cdd:cd05347  77 EEDFGKIDiLVNNAG---IIRRHPAEefPEAEWRDVIDVNLNGVFFVSQAVARHMIkQGHGKIINICSLLSELGGPPvPA 153

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 50726952 175 YCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:cd05347 154 YAASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMT 192
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 31-211 3.46e-16

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 76.68  E-value: 3.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCL-TPSGAEDLQRVAS------SRLHTTLLDITDPQSVQQAakwVEMHVKEA 103
Cdd:PRK12827   9 VLITGGSGGLGRAIAVRLAADGADVIVLDIhPMRGRAEADAVAAgieaagGKALGLAFDVRDFAATRAA---LDAGVEEF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  104 G-LFGLVNNAGVAGIiGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR--GRVINITSVLGrLAANGG--GYCVS 178
Cdd:PRK12827  86 GrLDILVNNAGIATD-AAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARrgGRIVNIASVAG-VRGNRGqvNYAAS 163

                        170       180       190
                 ....*....|....*....|....*....|...
gi 50726952  179 KFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK12827 164 KAGLIGLTKTLANELAPRGITVNAVAPGAINTP 196
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 33-222 5.29e-16

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


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 76.27  E-value: 5.29e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  33 ITGCDSGFGRLLALQLDQRGFRVLASCLT-PSGAEDLQRVASSRLHTTLL---DITDPQSVQqaaKWVEMHVKEaglFG- 107
Cdd:cd05358   8 VTGASSGIGKAIAIRLATAGANVVVNYRSkEDAAEEVVEEIKAVGGKAIAvqaDVSKEEDVV---ALFQSAIKE---FGt 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 ---LVNNAGVAGIIgPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR--GRVINITSVLGRLAANG-GGYCVSKFG 181
Cdd:cd05358  82 ldiLVNNAGLQGDA-SSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKikGKIINMSSVHEKIPWPGhVNYAASKGG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 50726952 182 LEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT-----NLESLEKTL 222
Cdd:cd05358 161 VKMMTKTLAQEYAPKGIRVNAIAPGAINTPINaeawdDPEQRADLL 206
PRK07024 PRK07024
SDR family oxidoreductase;
31-213 7.26e-16

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 75.74  E-value: 7.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQRVASS-----RLHTTLLDITDPQSVQQAAkwvEMHVKEAGL 105
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLG---LVARRTDALQAFAARlpkaaRVSVYAADVRDADALAAAA---ADFIAAHGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  106 FGLV-NNAGVA-GIigptpwLT--RDD---FQRVLNVNTMGPIGV-TLALLPLLQQARGRVINITSVLG-RLAANGGGYC 176
Cdd:PRK07024  79 PDVViANAGISvGT------LTeeREDlavFREVMDTNYFGMVATfQPFIAPMRAARRGTLVGIASVAGvRGLPGAGAYS 152

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 50726952  177 VSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:PRK07024 153 ASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPMT 189
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 31-213 8.74e-16

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: 75.50  E-value: 8.74e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQRVASS---RLHTTLLDITDPQSVQQAakwVEMHVKEAG-LF 106
Cdd:cd05341   8 AIVTGGARGLGLAHARLLVAEGAKVV---LSDILDEEGQAAAAElgdAARFFHLDVTDEDGWTAV---VDTAREAFGrLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 107 GLVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGP-IGVTLALLPLLQQARGRVINITSVLGRL-AANGGGYCVSKFGLEA 184
Cdd:cd05341  82 VLVNNAGIL-TGGTVETTTLEEWRRLLDINLTGVfLGTRAVIPPMKEAGGGSIINMSSIEGLVgDPALAAYNASKGAVRG 160

                       170       180       190
                ....*....|....*....|....*....|.
gi 50726952 185 FSDSLRRDVA--HFGIRVSIVEPGFFRTPVT 213
Cdd:cd05341 161 LTKSAALECAtqGYGIRVNSVHPGYIYTPMT 191
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 31-235 2.27e-15

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: 74.26  E-value: 2.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRV--LASCLTPSGAEDLQRVASS---RLHTTllDITDPQsvQQAAKWVEMHVKEAGL 105
Cdd:cd05323   3 AIITGGASGIGLATAKLLLKKGAKVaiLDRNENPGAAAELQAINPKvkaTFVQC--DVTSWE--QLAAAFKKAIEKFGRV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 106 FGLVNNagvAGIIGPTPWLTRDDFQ----RVLNVNTMGPI-GVTLALLPLLQQAR---GRVINITSVLG----RLAANgg 173
Cdd:cd05323  79 DILINN---AGILDEKSYLFAGKLPppweKTIDVNLTGVInTTYLALHYMDKNKGgkgGVIVNIGSVAGlypaPQFPV-- 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50726952 174 gYCVSKFGLEAFSDSLR-RDVAHFGIRVSIVEPGFFRTP-VTNLESLEKTLQACWARLPPATQA 235
Cdd:cd05323 154 -YSASKHGVVGFTRSLAdLLEYKTGVRVNAICPGFTNTPlLPDLVAKEAEMLPSAPTQSPEVVA 216
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 31-206 2.78e-15

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 74.02  E-value: 2.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQA-----AKWVEMHVkeagl 105
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMlaslpAEWRNIDV----- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  106 fgLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLGRLAANGGG-YCVSKFGLE 183
Cdd:PRK10538  78 --LVNNAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLpGMVERNHGHIINIGSTAGSWPYAGGNvYGATKAFVR 155

                        170       180
                 ....*....|....*....|...
gi 50726952  184 AFSDSLRRDVAHFGIRVSIVEPG 206
Cdd:PRK10538 156 QFSLNLRTDLHGTAVRVTDIEPG 178
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 31-265 4.03e-15

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: 73.80  E-value: 4.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAED-----LQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEagL 105
Cdd:cd05327   4 VVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEaaaeiKKETGNAKVEVIQLDLSSLASVRQFAEEFLARFPR--L 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 106 FGLVNNAGVAGiigPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLA---------ANGGG- 174
Cdd:cd05327  82 DILINNAGIMA---PPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASApSRIVNVSSIAHRAGpidfndldlENNKEy 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 175 -----YCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTNLESLEKTLQACWARLPPATQAHygGAfltkylkmq 249
Cdd:cd05327 159 spykaYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNGSFFLLYKLLRPFLKKSPEQ--GA--------- 227

                       250
                ....*....|....*.
gi 50726952 250 QRIMNLICDPDLTKVS 265
Cdd:cd05327 228 QTALYAATSPELEGVS 243
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 25-206 4.47e-15

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 73.24  E-value: 4.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   25 PASNAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPS-GAEDLQR---VASSRLHTTLLDITDPQSVQQAAKWVEmhv 100
Cdd:PRK12937   2 TLSNKVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAaAADELVAeieAAGGRAIAVQADVADAAAVTRLFDAAE--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  101 keaGLFG----LVNNAGVAGIiGPTPWLTRDDFQRVLNVNTMGPIgVTLALLPLLQQARGRVINI-TSVLGRLAANGGGY 175
Cdd:PRK12937  79 ---TAFGridvLVNNAGVMPL-GTIADFDLEDFDRTIATNLRGAF-VVLREAARHLGQGGRIINLsTSVIALPLPGYGPY 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 50726952  176 CVSKFGLEAFSDSLRRDVAHFGIRVSIVEPG 206
Cdd:PRK12937 154 AASKAAVEGLVHVLANELRGRGITVNAVAPG 184
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 31-211 5.46e-15

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 73.38  E-value: 5.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQrvassrLHTTLLDITDPQSVQQAAKWVEmhvKEAGLFG-LV 109
Cdd:PRK08220  11 VWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDYP------FATFVLDVSDAAAVAQVCQRLL---AETGPLDvLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  110 NnagVAGII--GPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVlgrlAANG-----GGYCVSKFG 181
Cdd:PRK08220  82 N---AAGILrmGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRsGAIVTVGSN----AAHVprigmAAYGASKAA 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 50726952  182 LEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK08220 155 LTSLAKCVGLELAPYGVRCNVVSPGSTDTD 184
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 30-185 5.63e-15

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: 73.09  E-value: 5.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  30 FVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSgAEDLQR-----VASSRLHTTLLDITDPQSVQQ---AAKWVEMHvk 101
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARS-EEPLQElkeelRPGLRVTTVKADLSDAAGVEQlleAIRKLDGE-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 102 eagLFGLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLAL--LPLLQQARGRVINITSVLGRLAANG-GGYCVS 178
Cdd:cd05367  78 ---RDLLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLlrAFKKRGLKKTVVNVSSGAAVNPFKGwGLYCSS 154


                ....*..
gi 50726952 179 KFGLEAF 185
Cdd:cd05367 155 KAARDMF 161
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 31-211 5.88e-15

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: 73.08  E-value: 5.88e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQRVASsRLHTTLL-------DITDPQSVQQAAKWVEMHVkeA 103
Cdd:cd05344   4 ALVTAASSGIGLAIARALAREGARVA---ICARNRENLERAAS-ELRAGGAgvlavvaDLTDPEDIDRLVEKAGDAF--G 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 104 GLFGLVNNAGvAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGR-----LAANGggycV 177
Cdd:cd05344  78 RVDILVNNAG-GPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLTVKepepnLVLSN----V 152

                       170       180       190
                ....*....|....*....|....*....|....
gi 50726952 178 SKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:cd05344 153 ARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTE 186
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 31-211 7.16e-15

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 72.91  E-value: 7.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQR----VASSRLHTTLLDITDPQSVQQAAKwvEMHVKEAGLF 106
Cdd:PRK12828  10 VAITGGFGGLGRATAAWLAARGARVA---LIGRGAAPLSQtlpgVPADALRIGGIDLVDPQAARRAVD--EVNRQFGRLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  107 GLVNNAGVagiigpTPW-----LTRDDFQRVLNVNTMGPI-GVTLALLPLLQQARGRVINITSVLGRLAANG-GGYCVSK 179
Cdd:PRK12828  85 ALVNIAGA------FVWgtiadGDADTWDRMYGVNVKTTLnASKAALPALTASGGGRIVNIGAGAALKAGPGmGAYAAAK 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 50726952  180 FGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK12828 159 AGVARLTEALAAELLDRGITVNAVLPSIIDTP 190
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 31-212 2.23e-14

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: 71.78  E-value: 2.23e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAED-----LQRVASSRLHTTLLDITDpqsVQQAAKWVEMHVKEAG- 104
Cdd:cd05330   6 VLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAakaalLEIAPDAEVLLIKADVSD---EAQVEAYVDATVEQFGr 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 105 LFGLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGP-IGVTLALLPLLQQARGRVINITSVLG-RLAANGGGYCVSKFGL 182
Cdd:cd05330  83 IDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVfYGLEKVLKVMREQGSGMIVNTASVGGiRGVGNQSGYAAAKHGV 162

                       170       180       190
                ....*....|....*....|....*....|
gi 50726952 183 EAFSDSLRRDVAHFGIRVSIVEPGFFRTPV 212
Cdd:cd05330 163 VGLTRNSAVEYGQYGIRINAIAPGAILTPM 192
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 24-205 5.06e-14

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 70.46  E-value: 5.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   24 LPASNAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVemhvkeA 103
Cdd:PRK06841  11 FDLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAV------I 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  104 GLFG----LVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQA-RGRVINITSVLGRLAANGG-GYCV 177
Cdd:PRK06841  85 SAFGridiLVNSAGVA-LLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAgGGKIVNLASQAGVVALERHvAYCA 163

                        170       180
                 ....*....|....*....|....*...
gi 50726952  178 SKFGLEAFSDSLRRDVAHFGIRVSIVEP 205
Cdd:PRK06841 164 SKAGVVGMTKVLALEWGPYGITVNAISP 191
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 31-213 1.16e-13

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: 69.44  E-value: 1.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVqqaAKWVEMHVKE-AGLFGLV 109
Cdd:cd08944   6 AIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQV---AALFERAVEEfGGLDLLV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 110 NNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIgVTLALLPLLQQARG--RVINITSVLGRLAANG-GGYCVSKFGLEAFS 186
Cdd:cd08944  83 NNAGAMHLTPAIIDTDLAVWDQTMAINLRGTF-LCCRHAAPRMIARGggSIVNLSSIAGQSGDPGyGAYGASKAAIRNLT 161

                       170       180
                ....*....|....*....|....*..
gi 50726952 187 DSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:cd08944 162 RTLAAELRHAGIRCNALAPGLIDTPLL 188
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
32-212 3.01e-13

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 68.67  E-value: 3.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   32 FITGCDSGFGRLLALQLDQRGFRVLASCLTPSgAEDLQRVASSRLH---TTLLDITDPQSVQQAAKWVEMhvKEAGLFGL 108
Cdd:PRK08226  10 LITGALQGIGEGIARVFARHGANLILLDISPE-IEKLADELCGRGHrctAVVADVRDPASVAAAIKRAKE--KEGRIDIL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  109 VNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLGRLAANGG--GYCVSKFGLEAF 185
Cdd:PRK08226  87 VNNAGVC-RLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLpEMIARKDGRIVMMSSVTGDMVADPGetAYALTKAAIVGL 165

                        170       180
                 ....*....|....*....|....*..
gi 50726952  186 SDSLRRDVAHFGIRVSIVEPGFFRTPV 212
Cdd:PRK08226 166 TKSLAVEYAQSGIRVNAICPGYVRTPM 192
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
32-210 3.08e-13

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 68.12  E-value: 3.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   32 FITGCDSGFGRLLALQLDQRGFRVLASC--LTPSGAE--DLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEAGLfg 107
Cdd:PRK12938   7 YVTGGMGGIGTSICQRLHKDGFKVVAGCgpNSPRRVKwlEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVGEIDV-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 LVNNAGVAGIIGPTPwLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLAANG-GGYCVSKFGLEAF 185
Cdd:PRK12938  85 LVNNAGITRDVVFRK-MTREDWTAVIDTNLTSLFNVTKQVIDGMVERGwGRIINISSVNGQKGQFGqTNYSTAKAGIHGF 163

                        170       180
                 ....*....|....*....|....*
gi 50726952  186 SDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK12938 164 TMSLAQEVATKGVTVNTVSPGYIGT 188
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 28-224 3.15e-13

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 68.45  E-value: 3.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   28 NAFVFITGCDSGFGRLLALQLDQRGFRvLAscLTPSGAEDLQ------RVASSRLHTTLLDITDPQSVQQAAKWVEMHVK 101
Cdd:PRK08217   5 DKVIVITGGAQGLGRAMAEYLAQKGAK-LA--LIDLNQEKLEeavaecGALGTEVRGYAANVTDEEDVEATFAQIAEDFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  102 eaGLFGLVNNAGVagiigptpwlTRD------------------DFQRVLNVNTMGPI--GVTLALLPLLQQARGRVINI 161
Cdd:PRK08217  82 --QLNGLINNAGI----------LRDgllvkakdgkvtskmsleQFQSVIDVNLTGVFlcGREAAAKMIESGSKGVIINI 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50726952  162 TSVlGRlAANGG--GYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT---NLESLEKTLQA 224
Cdd:PRK08217 150 SSI-AR-AGNMGqtNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTaamKPEALERLEKM 215
PRK06124 PRK06124
SDR family oxidoreductase;
19-228 4.90e-13

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 67.82  E-value: 4.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   19 RDRQSLPASNAFVfiTGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQ------RVASSRLHTTLLDITDPQSVQQA 92
Cdd:PRK06124   4 LQRFSLAGQVALV--TGSARGLGFEIARALAGAGAHVL---VNGRNAATLEaavaalRAAGGAAEALAFDIADEEAVAAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   93 AKWVEmhvKEAG-LFGLVNNAGvAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLA- 169
Cdd:PRK06124  79 FARID---AEHGrLDILVNNVG-ARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGyGRIIAITSIAGQVAr 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 50726952  170 ANGGGYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPvTNLESLEKTLQACWAR 228
Cdd:PRK06124 155 AGDAVYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATE-TNAAMAADPAVGPWLA 212
PRK06949 PRK06949
SDR family oxidoreductase;
32-210 8.55e-13

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 67.09  E-value: 8.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   32 FITGCDSGFGRLLALQLDQRGFRV-LASCLTPSGAEDLQRVASS--RLHTTLLDITDPQSVQQAAKWVEmhvKEAGLFG- 107
Cdd:PRK06949  13 LVTGASSGLGARFAQVLAQAGAKVvLASRRVERLKELRAEIEAEggAAHVVSLDVTDYQSIKAAVAHAE---TEAGTIDi 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 LVNNAGVAG---IIGPTPwltrDDFQRVLNVNTMGPIGVTL---------ALLPLLQQARGRVINITSVLG-RLAANGGG 174
Cdd:PRK06949  90 LVNNSGVSTtqkLVDVTP----ADFDFVFDTNTRGAFFVAQevakrmiarAKGAGNTKPGGRIINIASVAGlRVLPQIGL 165

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 50726952  175 YCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK06949 166 YCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDT 201
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 27-213 9.94e-13

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 66.70  E-value: 9.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   27 SNAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQ---RVASSRLHTTLLDITDPQSVQQAAKWVEMHVkeA 103
Cdd:PRK08085   8 AGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVaklRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDI--G 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  104 GLFGLVNNAGVAGiIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQ-ARGRVINITSV---LGRLAANggGYCVSK 179
Cdd:PRK08085  86 PIDVLINNAGIQR-RHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKrQAGKIINICSMqseLGRDTIT--PYAASK 162

                        170       180       190
                 ....*....|....*....|....*....|....
gi 50726952  180 FGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:PRK08085 163 GAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMT 196
PRK08589 PRK08589
SDR family oxidoreductase;
28-212 9.94e-13

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 67.11  E-value: 9.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   28 NAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRV--ASSRLHTTLLDITDPQSVQQAAKwvemHVKEAgl 105
Cdd:PRK08589   6 NKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDKIksNGGKAKAYHVDISDEQQVKDFAS----EIKEQ-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  106 FG----LVNNAGV---AGIIGPTPwltRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLA-ANGGGYCV 177
Cdd:PRK08589  80 FGrvdvLFNNAGVdnaAGRIHEYP---VDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAAdLYRSGYNA 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 50726952  178 SKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPV 212
Cdd:PRK08589 157 AKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPL 191
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 31-207 1.32e-12

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 66.52  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTL---LDITDPQSVQQAakwVEMHVKEAG-LF 106
Cdd:PRK07890   8 VVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALavpTDITDEDQCANL---VALALERFGrVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  107 GLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITS-VLGRLAANGGGYCVSKFGLEAF 185
Cdd:PRK07890  85 ALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMINSmVLRHSQPKYGAYKMAKGALLAA 164

                        170       180
                 ....*....|....*....|..
gi 50726952  186 SDSLRRDVAHFGIRVSIVEPGF 207
Cdd:PRK07890 165 SQSLATELGPQGIRVNSVAPGY 186
PRK07023 PRK07023
SDR family oxidoreductase;
33-206 1.37e-12

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 66.19  E-value: 1.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLasCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQ--AAKWVEMHVKEAGLFGLVN 110
Cdd:PRK07023   6 VTGHSRGLGAALAEQLLQPGIAVL--GVARSRHPSLAAAAGERLAEVELDLSDAAAAAAwlAGDLLAAFVDGASRVLLIN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  111 NAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLA-LLPLLQQARGRVINITSVLGRLAANG-GGYCVSKFGLEAFSDS 188
Cdd:PRK07023  84 NAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAAlAQAASDAAERRILHISSGAARNAYAGwSVYCATKAALDHHARA 163

                        170
                 ....*....|....*...
gi 50726952  189 LRRDvAHFGIRVSIVEPG 206
Cdd:PRK07023 164 VALD-ANRALRIVSLAPG 180
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 33-211 1.51e-12

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: 66.14  E-value: 1.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  33 ITGCDSGFGRLLALQLDQRGFRVLASCLTPS-GAEDLQ---RVASSRLHTTLLDITDPQSVQQAAKWVEMHvkEAGLFGL 108
Cdd:cd05362   8 VTGASRGIGRAIAKRLARDGASVVVNYASSKaAAEEVVaeiEAAGGKAIAVQADVSDPSQVARLFDAAEKA--FGGVDIL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 109 VNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQArGRVINITSVLGRLAA-NGGGYCVSKFGLEAFSD 187
Cdd:cd05362  86 VNNAGV-MLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDG-GRIINISSSLTAAYTpNYGAYAGSKAAVEAFTR 163

                       170       180
                ....*....|....*....|....
gi 50726952 188 SLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:cd05362 164 VLAKELGGRGITVNAVAPGPVDTD 187
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 31-211 1.98e-12

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 66.06  E-value: 1.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLtpsGAEDLQRVASSRLHTTL------LDITDPQSVQQAAKWVEMHvkeag 104
Cdd:PRK12429   7 ALVTGAASGIGLEIALALAKEGAKVVIADL---NDEAAAAAAEALQKAGGkaigvaMDVTDEEAINAGIDYAVET----- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  105 lFG----LVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLAANG-GGYCVS 178
Cdd:PRK12429  79 -FGgvdiLVNNAGIQ-HVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGgGRIINMASVHGLVGSAGkAAYVSA 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 50726952  179 KFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK12429 157 KHGLIGLTKVVALEGATHGVTVNAICPGYVDTP 189
PRK07069 PRK07069
short chain dehydrogenase; Validated
 32-212 2.53e-12

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 65.50  E-value: 2.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   32 FITGCDSGFGRLLALQLDQRGFRVLascLTPSGAED-LQRVASS--RLHTTLLDITDPQSVQQAAKWV----EMHVKEAG 104
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVF---LTDINDAAgLDAFAAEinAAHGEGVAFAAVQDVTDEAQWQallaQAADAMGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  105 LFGLVNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPI-GVTLALLPLLQQARGRVINITSVLG-RLAANGGGYCVSKFGL 182
Cdd:PRK07069  80 LSVLVNNAGV-GSFGAIEQIELDEWRRVMAINVESIFlGCKHALPYLRASQPASIVNISSVAAfKAEPDYTAYNASKAAV 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 50726952  183 EAFSDSLRRDVAHFG--IRVSIVEPGFFRTPV 212
Cdd:PRK07069 159 ASLTKSIALDCARRGldVRCNSIHPTFIRTGI 190
PRK06172 PRK06172
SDR family oxidoreductase;
27-210 2.88e-12

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 65.54  E-value: 2.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   27 SNAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAED---LQRVASSRLHTTLLDITDPQSVQQaakwveMHVKEA 103
Cdd:PRK06172   6 SGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEEtvaLIREAGGEALFVACDVTRDAEVKA------LVEQTI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  104 GLFGLV----NNAGVAGIIGPTPWLTRDDFQRVLNVNTMGP-IGVTLALLPLLQQARGRVINITSVLGRLAANG-GGYCV 177
Cdd:PRK06172  80 AAYGRLdyafNNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVwLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKmSIYAA 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 50726952  178 SKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK06172 160 SKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDT 192
PRK07774 PRK07774
SDR family oxidoreductase;
33-230 3.29e-12

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 65.15  E-value: 3.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEdlqRVASSRLHT------TLLDITDPQSVQQ-AAKWVEmhvKEAGL 105
Cdd:PRK07774  11 VTGAAGGIGQAYAEALAREGASVVVADINAEGAE---RVAKQIVADggtaiaVQVDVSDPDSAKAmADATVS---AFGGI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  106 FGLVNNAGVAGIIGPTPWLTR--DDFQRVLNVNTMGPIGVTLALLPLLQQARG-RVINITSVLGRLAanGGGYCVSKFGL 182
Cdd:PRK07774  85 DYLVNNAAIYGGMKLDLLITVpwDYYKKFMSVNLDGALVCTRAVYKHMAKRGGgAIVNQSSTAAWLY--SNFYGLAKVGL 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 50726952  183 EAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTNLESLEKTLQACWARLP 230
Cdd:PRK07774 163 NGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVTPKEFVADMVKGIP 210
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 33-210 3.73e-12

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 65.25  E-value: 3.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLASCLT--PSGAEDLQRVASSRLHTTLL--DITDPQSVQQAAKWVEmhVKEAGLFGL 108
Cdd:PRK05565  10 VTGASGGIGRAIAELLAKEGAKVVIAYDIneEAAQELLEEIKEEGGDAIAVkaDVSSEEDVENLVEQIV--EKFGKIDIL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  109 VNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVI-NITSVLGRL-AANGGGYCVSKFGLEAFS 186
Cdd:PRK05565  88 VNNAGI-SNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIvNISSIWGLIgASCEVLYSASKGAVNAFT 166

                        170       180
                 ....*....|....*....|....
gi 50726952  187 DSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK05565 167 KALAKELAPSGIRVNAVAPGAIDT 190
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 33-213 4.06e-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: 65.18  E-value: 4.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  33 ITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTL----LDITDPQSVQQ--AAKWVEMHvkeaGLF 106
Cdd:cd05337   6 VTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAGRRAiyfqADIGELSDHEAllDQAWEDFG----RLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 107 GLVNNAGVAGII-GPTPWLTRDDFQRVLNVNTMGPIGVTLALL-------PLLQQARGRVINITSV-LGRLAANGGGYCV 177
Cdd:cd05337  82 CLVNNAGIAVRPrGDLLDLTEDSFDRLIAINLRGPFFLTQAVArrmveqpDRFDGPHRSIIFVTSInAYLVSPNRGEYCI 161

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 50726952 178 SKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:cd05337 162 SKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMT 197
PRK09242 PRK09242
SDR family oxidoreductase;
33-230 4.18e-12

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 65.15  E-value: 4.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQRV--------ASSRLHTTLLDITDPQSVQQAAKWVEMHVkeAG 104
Cdd:PRK09242  14 ITGASKGIGLAIAREFLGLGADVL---IVARDADALAQArdelaeefPEREVHGLAADVSDDEDRRAILDWVEDHW--DG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  105 LFGLVNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLGrLAANGGG--YCVSKFG 181
Cdd:PRK09242  89 LHILVNNAGG-NIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHpLLKQHASSAIVNIGSVSG-LTHVRSGapYGMTKAA 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 50726952  182 LEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTN-LESLEKTLQACWARLP 230
Cdd:PRK09242 167 LLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSgPLSDPDYYEQVIERTP 216
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 32-214 4.71e-12

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 64.94  E-value: 4.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   32 FITGCDSGFGRLLALQLDQRGFRVlasCLTPSGAEDLQRVASS---RLHTTLLDITDPQSVQQAAKWVEMHVKeaGLFGL 108
Cdd:PRK12936  10 LVTGASGGIGEEIARLLHAQGAIV---GLHGTRVEKLEALAAElgeRVKIFPANLSDRDEVKALGQKAEADLE--GVDIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  109 VNNAGVAGIiGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGrLAANGG--GYCVSKFGLEAF 185
Cdd:PRK12936  85 VNNAGITKD-GLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRyGRIINITSVVG-VTGNPGqaNYCASKAGMIGF 162

                        170       180
                 ....*....|....*....|....*....
gi 50726952  186 SDSLRRDVAHFGIRVSIVEPGFFRTPVTN 214
Cdd:PRK12936 163 SKSLAQEIATRNVTVNCVAPGFIESAMTG 191
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 31-205 6.31e-12

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


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 64.41  E-value: 6.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSrLHTTLLDITDPQSVQQAakwvemhVKEAGLF-GLV 109
Cdd:cd05351  10 ALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPG-IEPVCVDLSDWDATEEA-------LGSVGPVdLLV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 110 NNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPL--LQQARGRVINITSVLGRLA-ANGGGYCVSKFGLEAFS 186
Cdd:cd05351  82 NNAAVA-ILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGmiARGVPGSIVNVSSQASQRAlTNHTVYCSTKAALDMLT 160

                       170
                ....*....|....*....
gi 50726952 187 DSLRRDVAHFGIRVSIVEP 205
Cdd:cd05351 161 KVMALELGPHKIRVNSVNP 179
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 33-254 6.45e-12

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 64.26  E-value: 6.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLASC-LTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEAGLFG-LVN 110
Cdd:PRK12935  11 VTGGAKGIGKAITVALAQEGAKVVINYnSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFGKVDiLVN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  111 NAGVAGIIGPTPwLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLAANG-GGYCVSKFGLEAFSDS 188
Cdd:PRK12935  91 NAGITRDRTFKK-LNREDWERVIDVNLSSVFNTTSAVLPYITEAEeGRIISISSIIGQAGGFGqTNYSAAKAGMLGFTKS 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50726952  189 LRRDVAHFGIRVSIVEPGFFRTPVTnLESLEKTLQACWARLPP-----ATQAHYGGAFLTK---YLKMQQRIMN 254
Cdd:PRK12935 170 LALELAKTNVTVNAICPGFIDTEMV-AEVPEEVRQKIVAKIPKkrfgqADEIAKGVVYLCRdgaYITGQQLNIN 242
PRK07074 PRK07074
SDR family oxidoreductase;
31-211 8.65e-12

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 64.02  E-value: 8.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQR-VASSRLHTTLLDITDPQSVQQAakwVEMHVKEAGLFG-L 108
Cdd:PRK07074   5 ALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADaLGDARFVPVACDLTDAASLAAA---LANAAAERGPVDvL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  109 VNNAGVAGIIG--PTpwlTRDDFQRVLNVNTMGP-IGVTLALLPLLQQARGRVINITSVLGRLAANGGGYCVSKFGLEAF 185
Cdd:PRK07074  82 VANAGAARAASlhDT---TPASWRADNALNLEAAyLCVEAVLEGMLKRSRGAVVNIGSVNGMAALGHPAYSAAKAGLIHY 158

                        170       180
                 ....*....|....*....|....*.
gi 50726952  186 SDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK07074 159 TKLLAVEYGRFGIRANAVAPGTVKTQ 184
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 33-212 9.37e-12

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 64.15  E-value: 9.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAE---DLQRVASSRLHTTLLDITDPQSVQQaakwveMHVKEAGLFG-- 107
Cdd:PRK13394  12 VTGAASGIGKEIALELARAGAAVAIADLNQDGANavaDEINKAGGKAIGVAMDVTNEDAVNA------GIDKVAERFGsv 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 --LVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR--GRVINITSVLGRLAANG-GGYCVSKFGL 182
Cdd:PRK13394  86 diLVSNAGIQ-IVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHSHEASPLkSAYVTAKHGL 164

                        170       180       190
                 ....*....|....*....|....*....|
gi 50726952  183 EAFSDSLRRDVAHFGIRVSIVEPGFFRTPV 212
Cdd:PRK13394 165 LGLARVLAKEGAKHNVRSHVVCPGFVRTPL 194
PRK06194 PRK06194
hypothetical protein; Provisional
 33-210 9.90e-12

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 64.27  E-value: 9.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFR-VLA-----------SCLTPSGAEDLQRVassrlhttlLDITDPQSVQQAAKWVEMHV 100
Cdd:PRK06194  11 ITGAASGFGLAFARIGAALGMKlVLAdvqqdaldravAELRAQGAEVLGVR---------TDVSDAAQVEALADAALERF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  101 KEAGLfgLVNNAGVAGiiGPTPWL-TRDDFQRVLNVNTMGPI-GVTL------ALLPLLQQARGRVINITSVLGRLAA-N 171
Cdd:PRK06194  82 GAVHL--LFNNAGVGA--GGLVWEnSLADWEWVLGVNLWGVIhGVRAftplmlAAAEKDPAYEGHIVNTASMAGLLAPpA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 50726952  172 GGGYCVSKFGLEAFSDSLRRDVAHFG--IRVSIVEPGFFRT 210
Cdd:PRK06194 158 MGIYNVSKHAVVSLTETLYQDLSLVTdqVGASVLCPYFVPT 198
PRK06114 PRK06114
SDR family oxidoreductase;
32-211 1.46e-11

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 63.65  E-value: 1.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   32 FITGCDSGFGRLLALQLDQRGFRVLASCLTPSG--AEDLQRVASSRLHTTLL--DITDPQSVQQAAKWVEMHVkeAGLFG 107
Cdd:PRK06114  12 FVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDglAETAEHIEAAGRRAIQIaaDVTSKADLRAAVARTEAEL--GALTL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 LVNNAGVAGIIgPTPWLTRDDFQRVLNVNTMGP-IGVTLALLPLLQQARGRVINITSVLGRLAANG---GGYCVSKFGLE 183
Cdd:PRK06114  90 AVNAAGIANAN-PAEEMEEEQWQTVMDINLTGVfLSCQAEARAMLENGGGSIVNIASMSGIIVNRGllqAHYNASKAGVI 168

                        170       180
                 ....*....|....*....|....*...
gi 50726952  184 AFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK06114 169 HLSKSLAMEWVGRGIRVNSISPGYTATP 196
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
33-211 1.64e-11

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 63.51  E-value: 1.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAakwVEMHVKEAG-LFGLVNN 111
Cdd:PRK07067  11 LTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRI---VAAAVERFGgIDILFNN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  112 AGVAGiIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR--GRVINITSVLGR----LAANgggYCVSKFGLEAF 185
Cdd:PRK07067  88 AALFD-MAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGrgGKIINMASQAGRrgeaLVSH---YCATKAAVISY 163

                        170       180
                 ....*....|....*....|....*.
gi 50726952  186 SDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK07067 164 TQSAALALIRHGINVNAIAPGVVDTP 189
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
30-210 2.05e-11

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 63.16  E-value: 2.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   30 FVFITGCDSGFGRLLALQLDQRGFRVLasCLTPSGAEDLQRVAS---SRLHTTLLDITDpqsVQQAAKWVE-----MHVK 101
Cdd:PRK06924   3 YVIITGTSQGLGEAIANQLLEKGTHVI--SISRTENKELTKLAEqynSNLTFHSLDLQD---VHELETNFNeilssIQED 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  102 EAGLFGLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARG--RVINITSVLGRLAANG-GGYCVS 178
Cdd:PRK06924  78 NVSSIHLINNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKVdkRVINISSGAAKNPYFGwSAYCSS 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 50726952  179 KFGLEAFSDS--LRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK06924 158 KAGLDMFTQTvaTEQEEEEYPVKIVAFSPGVMDT 191
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
32-211 2.26e-11

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 62.82  E-value: 2.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   32 FITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEAGLFG-LVN 110
Cdd:PRK08643   6 LVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDLNvVVN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  111 NAGVAGIIgPTPWLTRDDFQRVLNVNTMGPI-GVTLALLPLLQQARG-RVINITSVLGRLA-ANGGGYCVSKFGLEAFSD 187
Cdd:PRK08643  86 NAGVAPTT-PIETITEEQFDKVYNINVGGVIwGIQAAQEAFKKLGHGgKIINATSQAGVVGnPELAVYSSTKFAVRGLTQ 164

                        170       180
                 ....*....|....*....|....
gi 50726952  188 SLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK08643 165 TAARDLASEGITVNAYAPGIVKTP 188
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 77-213 2.76e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 62.77  E-value: 2.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   77 HTTLLDITDPQSVQQAAKWVEmhvKEAGLFG-LVNNagvAGIIGPTPWL--TRDDFQRVLNVNTMGPIGVTLALLPLLQQ 153
Cdd:PRK07097  62 HGYVCDVTDEDGVQAMVSQIE---KEVGVIDiLVNN---AGIIKRIPMLemSAEDFRQVIDIDLNAPFIVSKAVIPSMIK 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50726952  154 AR-GRVINI---TSVLGRlaANGGGYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:PRK07097 136 KGhGKIINIcsmMSELGR--ETVSAYAAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIATPQT 197
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 32-212 3.29e-11

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: 62.56  E-value: 3.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  32 FITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQ------RVASSRLHTTLLDITDPQSVQQAakwVEMHVKEAGL 105
Cdd:cd08945   7 LVTGATSGIGLAIARRLGKEGLRVF---VCARGEEGLAttvkelREAGVEADGRTCDVRSVPEIEAL---VAAAVARYGP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 106 FG-LVNNAGVAGIiGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPL---LQQARGRVINITSVLGRLAA-NGGGYCVSKF 180
Cdd:cd08945  81 IDvLVNNAGRSGG-GATAELADELWLDVVETNLTGVFRVTKEVLKAggmLERGTGRIINIASTGGKQGVvHAAPYSASKH 159

                       170       180       190
                ....*....|....*....|....*....|..
gi 50726952 181 GLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPV 212
Cdd:cd08945 160 GVVGFTKALGLELARTGITVNAVCPGFVETPM 191
PRK09730 PRK09730
SDR family oxidoreductase;
29-210 3.81e-11

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 62.17  E-value: 3.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   29 AFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGA--EDLQRVASSRLHTTLL--DITDPQSVQqaAKWVEMHVKEAG 104
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAaqEVVNLITQAGGKAFVLqaDISDENQVV--AMFTAIDQHDEP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  105 LFGLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARG----RVINITSVLGRLAANGG--GYCVS 178
Cdd:PRK09730  80 LAALVNNAGILFTQCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALKHGgsggAIVNVSSAASRLGAPGEyvDYAAS 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 50726952  179 KFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK09730 160 KGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYT 191
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 32-213 3.81e-11

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 62.29  E-value: 3.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   32 FITGCDSGFGRLLALQLDQRGFRVLASCLTPSG--AEDLQRVAS--SRLHTTLLDITD----PQSVQQAAKWVemhvkeA 103
Cdd:PRK12745   6 LVTGGRRGIGLGIARALAAAGFDLAINDRPDDEelAATQQELRAlgVEVIFFPADVADlsahEAMLDAAQAAW------G 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  104 GLFGLVNNAGVAGII-GPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGR-------VINITSVLGRLAA-NGGG 174
Cdd:PRK12745  80 RIDCLVNNAGVGVKVrGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPeelphrsIVFVSSVNAIMVSpNRGE 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 50726952  175 YCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:PRK12745 160 YCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMT 198
PRK06101 PRK06101
SDR family oxidoreductase;
28-219 4.28e-11

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 61.81  E-value: 4.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   28 NAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRvASSRLHTTLLDITDPQSVQQAAKWVEMhVKEAGLFg 107
Cdd:PRK06101   1 MTAVLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDELHT-QSANIFTLAFDVTDHPGTKAALSQLPF-IPELWIF- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 lvnNAGVAGIIgptpwltrDD-------FQRVLNVNTMGPIGVTLALLPLLQqaRG-RVINITSVLGRLA-ANGGGYCVS 178
Cdd:PRK06101  78 ---NAGDCEYM--------DDgkvdatlMARVFNVNVLGVANCIEGIQPHLS--CGhRVVIVGSIASELAlPRAEAYGAS 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 50726952  179 KFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTNLESLE 219
Cdd:PRK06101 145 KAAVAYFARTLQLDLRPKGIEVVTVFPGFVATPLTDKNTFA 185
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 31-210 5.62e-11

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 61.70  E-value: 5.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCL-TPSGAEDLQRVASSRLHTTLLDITDPQSVQQaakwveMHVKEAGLFG-- 107
Cdd:cd05349   3 VLVTGASRGLGAAIARSFAREGARVVVNYYrSTESAEAVAAEAGERAIAIQADVRDRDQVQA------MIEEAKNHFGpv 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 --LVNNAGVAGIIGPTPWLTRD-----DFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSvlgRLAANG----GGY 175
Cdd:cd05349  77 dtIVNNALIDFPFDPDQRKTFDtidweDYQQQLEGAVKGALNLLQAVLPDFKERGsGRVINIGT---NLFQNPvvpyHDY 153

                       170       180       190
                ....*....|....*....|....*....|....*
gi 50726952 176 CVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:cd05349 154 TTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKV 188
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 31-213 1.07e-10

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 60.95  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVlaSCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEAGLfgLVN 110
Cdd:PRK06463  10 ALITGGTRGIGRAIAEAFLREGAKV--AVLYNSAENEAKELREKGVFTIKCDVGNRDQVKKSKEVVEKEFGRVDV--LVN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  111 NAGVAGIIgptPWLTRDD--FQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSV--LGRLAANGGGYCVSKFGLEAF 185
Cdd:PRK06463  86 NAGIMYLM---PFEEFDEekYNKMIKINLNGAIYTTYEFLPLLKLSKnGAIVNIASNagIGTAAEGTTFYAITKAGIIIL 162

                        170       180
                 ....*....|....*....|....*...
gi 50726952  186 SDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:PRK06463 163 TRRLAFELGKYGIRVNAVAPGWVETDMT 190
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 31-230 1.31e-10

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: 60.68  E-value: 1.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTP----SGAEDLQRVASSRLHTTLLDITDPQSVQQAakwVEMHVKEAGLF 106
Cdd:cd05369   6 AFITGGGTGIGKAIAKAFAELGASVAIAGRKPevleAAAEEISSATGGRAHPIQCDVRDPEAVEAA---VDETLKEFGKI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 107 -GLVNNAGvAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR--GRVINITSVLgrlAANGGGYCV----SK 179
Cdd:cd05369  83 dILINNAA-GNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKhgGSILNISATY---AYTGSPFQVhsaaAK 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 50726952 180 FGLEAFSDSLRRDVAHFGIRVSIVEPG-FFRTP-VTNLESLEKTLQACWARLP 230
Cdd:cd05369 159 AGVDALTRSLAVEWGPYGIRVNAIAPGpIPTTEgMERLAPSGKSEKKMIERVP 211
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-213 1.75e-10

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 59.98  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   27 SNAFVFITGCDSGFGRLLALQLDQRGFRVLAScltpsgaeDLQR--VASSRLHTTLLDITDPqsVQQAAKWV-EMHVkea 103
Cdd:PRK06550   4 MTKTVLITGAASGIGLAQARAFLAQGAQVYGV--------DKQDkpDLSGNFHFLQLDLSDD--LEPLFDWVpSVDI--- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  104 glfgLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLAL-LPLLQQARGRVINITSVLGrLAANGGG--YCVSKF 180
Cdd:PRK06550  71 ----LCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYlPQMLERKSGIIINMCSIAS-FVAGGGGaaYTASKH 145

                        170       180       190
                 ....*....|....*....|....*....|...
gi 50726952  181 GLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:PRK06550 146 ALAGFTKQLALDYAKDGIQVFGIAPGAVKTPMT 178
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 31-224 1.92e-10

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: 60.18  E-value: 1.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRvaSSRLHTTLLDITDPQSVQQAAKwvemhvkEAGLFG-LV 109
Cdd:cd05368   5 ALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELER--GPGITTRVLDVTDKEQVAALAK-------EEGRIDvLF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 110 NNAGVAGIiGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLAA--NGGGYCVSKFGLEAFS 186
Cdd:cd05368  76 NCAGFVHH-GSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKdGSIINMSSVASSIKGvpNRFVYSTTKAAVIGLT 154

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 50726952 187 DSLRRDVAHFGIRVSIVEPGFFRTPvtnleSLEKTLQA 224
Cdd:cd05368 155 KSVAADFAQQGIRCNAICPGTVDTP-----SLEERIQA 187
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 28-211 1.96e-10

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: 59.90  E-value: 1.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  28 NAFVFITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQRVA---------SSRLHTTLLDITDPQSVQQAAKWVEM 98
Cdd:cd05340   4 DRIILVTGASDGIGREAALTYARYGATVI---LLGRNEEKLRQVAdhineeggrQPQWFILDLLTCTSENCQQLAQRIAV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  99 HVKEagLFGLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRL-AANGGGYC 176
Cdd:cd05340  81 NYPR--LDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQgRANWGAYA 158

                       170       180       190
                ....*....|....*....|....*....|....*
gi 50726952 177 VSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:cd05340 159 VSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTA 193
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 31-210 2.30e-10

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: 60.17  E-value: 2.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQR--VASSRLHTTL---LDITDPQSVQQAAKwvEMHVKEAGL 105
Cdd:cd09807   4 VIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAeiRRDTLNHEVIvrhLDLASLKSIRAFAA--EFLAEEDRL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 106 FGLVNNAGVagIIGPTpWLTRDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVL-------------GRLAAN 171
Cdd:cd09807  82 DVLINNAGV--MRCPY-SKTEDGFEMQFGVNHLGHFLLTNLLLdLLKKSAPSRIVNVSSLAhkagkinfddlnsEKSYNT 158

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 50726952 172 GGGYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:cd09807 159 GFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRT 197
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 33-206 2.42e-10

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 60.05  E-value: 2.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLASCLTpsgAEDLQRVAS--------SRLHTTLLDITDPQSVQQAAKWVEMHVKEAG 104
Cdd:PRK12384   7 VIGGGQTLGAFLCHGLAEEGYRVAVADIN---SEKAANVAQeinaeygeGMAYGFGADATSEQSVLALSRGVDEIFGRVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  105 LfgLVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPI--GVTLALLPLLQQARGRVINITSVLGRLAA-NGGGYCVSKFG 181
Cdd:PRK12384  84 L--LVYNAGIA-KAAFITDFQLGDFDRSLQVNLVGYFlcAREFSRLMIRDGIQGRIIQINSKSGKVGSkHNSGYSAAKFG 160

                        170       180
                 ....*....|....*....|....*
gi 50726952  182 LEAFSDSLRRDVAHFGIRVSIVEPG 206
Cdd:PRK12384 161 GVGLTQSLALDLAEYGITVHSLMLG 185
PRK07814 PRK07814
SDR family oxidoreductase;
33-206 2.82e-10

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 59.79  E-value: 2.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQ---RVASSRLHTTLLDITDPQSVQQ-AAKWVEMhvkeaglFG- 107
Cdd:PRK07814  15 VTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAeqiRAAGRRAHVVAADLAHPEATAGlAGQAVEA-------FGr 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 ---LVNNAGVAGiigPTPWLT------RDDFQrvLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLAANG-GGYCV 177
Cdd:PRK07814  88 ldiVVNNVGGTM---PNPLLStstkdlADAFT--FNVATAHALTVAAVPLMLEHSGGGSVINISSTMGRLAGRGfAAYGT 162

                        170       180
                 ....*....|....*....|....*....
gi 50726952  178 SKFGLEAFSDSLRRDVAHfGIRVSIVEPG 206
Cdd:PRK07814 163 AKAALAHYTRLAALDLCP-RIRVNAIAPG 190
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 33-224 6.52e-10

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 58.80  E-value: 6.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQRVASS------RLHTTLLDITDPQSVQQAAKWVEMHvkeaglF 106
Cdd:PRK08213  17 VTGGSRGLGLQIAEALGEAGARVV---LSARKAEELEEAAAHlealgiDALWIAADVADEADIERLAEETLER------F 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  107 G----LVNNAGVA-GiiGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR--GRVINITSVLGrLAANGG------ 173
Cdd:PRK08213  88 GhvdiLVNNAGATwG--APAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRSMIPRgyGRIINVASVAG-LGGNPPevmdti 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 50726952  174 GYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTN--LESLEKTLQA 224
Cdd:PRK08213 165 AYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRgtLERLGEDLLA 217
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 33-213 8.57e-10

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 59.46  E-value: 8.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLasCL-TPSGAEDLQRVASsRLH-TTL-LDITDPQSVQQAAKwvemHVKE--AGLFG 107
Cdd:PRK08261 215 VTGAARGIGAAIAEVLARDGAHVV--CLdVPAAGEALAAVAN-RVGgTALaLDITAPDAPARIAE----HLAErhGGLDI 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 LVNNAGVagiigptpwlTRD------DFQR---VLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGrLAANGG--GY 175
Cdd:PRK08261 288 VVHNAGI----------TRDktlanmDEARwdsVLAVNLLAPLRITEALLAAGALGDgGRIVGVSSISG-IAGNRGqtNY 356

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 50726952  176 CVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:PRK08261 357 AASKAGVIGLVQALAPLLAERGITINAVAPGFIETQMT 394
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 31-224 8.85e-10

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


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 58.13  E-value: 8.85e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPS--GAEDLQRVASSRLHTTLL--DITDPQSVQQAAKWVEMHVKeaGLF 106
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSKdaAAEVAAEIEELGGKAVVVraDVSQPQDVEEMFAAVKERFG--RLD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 107 GLVNNAGvAGIIGPTPWLTRDDFQRVLNVNTMGPI-GVTLALLPLLQQARGRVINITSVL-GRLAANGGGYCVSKFGLEA 184
Cdd:cd05359  79 VLVSNAA-AGAFRPLSELTPAHWDAKMNTNLKALVhCAQQAAKLMRERGGGRIVAISSLGsIRALPNYLAVGTAKAALEA 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 50726952 185 FSDSLRRDVAHFGIRVSIVEPGFFRTPVT----NLESLEKTLQA 224
Cdd:cd05359 158 LVRYLAVELGPRGIRVNAVSPGVIDTDALahfpNREDLLEAAAA 201
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 33-212 9.52e-10

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: 58.24  E-value: 9.52e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  33 ITGCDSGFGRLLALQLDQRGFRV-LASCLTPSGAE---DLQRVASSRLHTtllDITDPQSVQQAAKWVemhVKEAG-LFG 107
Cdd:cd05326   9 ITGGASGIGEATARLFAKHGARVvIADIDDDAGQAvaaELGDPDISFVHC---DVTVEADVRAAVDTA---VARFGrLDI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 LVNNAGVAGiiGPTPWL---TRDDFQRVLNVNTMGP-IGVTLALLPLLQQARGRVINITSVLGRLAanGGG---YCVSKF 180
Cdd:cd05326  83 MFNNAGVLG--APCYSIletSLEEFERVLDVNVYGAfLGTKHAARVMIPAKKGSIVSVASVAGVVG--GLGphaYTASKH 158

                       170       180       190
                ....*....|....*....|....*....|..
gi 50726952 181 GLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPV 212
Cdd:cd05326 159 AVLGLTRSAATELGEHGIRVNCVSPYGVATPL 190
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 33-205 9.59e-10

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: 58.17  E-value: 9.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  33 ITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDpqsvqqAAKWVEMHVKEAGLFG----L 108
Cdd:cd05345  10 VTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTK------RADVEAMVEAALSKFGrldiL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 109 VNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGpIGVTLALLPLLQQAR--GRVINITSVLG-RLAANGGGYCVSKFGLEAF 185
Cdd:cd05345  84 VNNAGITHRNKPMLEVDEEEFDRVFAVNVKS-IYLSAQALVPHMEEQggGVIINIASTAGlRPRPGLTWYNASKGWVVTA 162

                       170       180
                ....*....|....*....|
gi 50726952 186 SDSLRRDVAHFGIRVSIVEP 205
Cdd:cd05345 163 TKAMAVELAPRNIRVNCLCP 182
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 21-213 1.56e-09

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


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 57.46  E-value: 1.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  21 RQSLPASNAFvfITGCDSGFGRLLALQLDQRGFRV---------LASCLTPSGAEDLQRVASsrlhttLLDITDPQSVQQ 91
Cdd:cd05329   1 RWNLEGKTAL--VTGGTKGIGYAIVEELAGLGAEVytcarnqkeLDECLTEWREKGFKVEGS------VCDVSSRSERQE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  92 AAKWVEMHVKEAgLFGLVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLAL-LPLLQQARGRVINITSVLGRLAA 170
Cdd:cd05329  73 LMDTVASHFGGK-LNILVNNAGTN-IRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAhPLLKASGNGNIVFISSVAGVIAV 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 50726952 171 NGGG-YCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:cd05329 151 PSGApYGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLV 194
PRK06139 PRK06139
SDR family oxidoreductase;
25-211 1.87e-09

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 57.81  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   25 PASNAFVFITGCDSGFGRLLALQLDQRGFR-VLAScltpSGAEDLQRVASS--RLHTTLL----DITDPQSVQQAAKwve 97
Cdd:PRK06139   4 PLHGAVVVITGASSGIGQATAEAFARRGARlVLAA----RDEEALQAVAEEcrALGAEVLvvptDVTDADQVKALAT--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   98 mhvKEAGLFG----LVNNAGVaGIIG---PTPWltrDDFQRVLNVNTMG---------PIGVTLAllpllqqaRGRVINI 161
Cdd:PRK06139  77 ---QAASFGGridvWVNNVGV-GAVGrfeETPI---EAHEQVIQTNLIGymrdahaalPIFKKQG--------HGIFINM 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 50726952  162 TSvLGRLAAN--GGGYCVSKFGLEAFSDSLRRDVAHF-GIRVSIVEPGFFRTP 211
Cdd:PRK06139 142 IS-LGGFAAQpyAAAYSASKFGLRGFSEALRGELADHpDIHVCDVYPAFMDTP 193
PRK07201 PRK07201
SDR family oxidoreductase;
31-211 2.07e-09

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 58.42  E-value: 2.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQRVASS------RLHTTLLDITDPQSVQQAAKWVemhvkeAG 104
Cdd:PRK07201 374 VLITGASSGIGRATAIKVAEAGATVF---LVARNGEALDELVAEirakggTAHAYTCDLTDSAAVDHTVKDI------LA 444

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  105 LFG----LVNNAGVAgiIGPTPWLTRD---DFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITS--VLG---RLAAn 171
Cdd:PRK07201 445 EHGhvdyLVNNAGRS--IRRSVENSTDrfhDYERTMAVNYFGAVRLILGLLPHMRERRfGHVVNVSSigVQTnapRFSA- 521

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 50726952  172 gggYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK07201 522 ---YVASKAALDAFSDVAASETLSDGITFTTIHMPLVRTP 558
PRK06128 PRK06128
SDR family oxidoreductase;
33-212 2.26e-09

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 57.56  E-value: 2.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLASCLtPSGAEDLQRV-----ASSRLHTTLL-DITDPQSVQQAakwVEMHVKE-AGL 105
Cdd:PRK06128  60 ITGADSGIGRATAIAFAREGADIALNYL-PEEEQDAAEVvqliqAEGRKAVALPgDLKDEAFCRQL---VERAVKElGGL 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  106 FGLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMG------------PIGVTlallpllqqargrVINITSVLG-RLAANG 172
Cdd:PRK06128 136 DILVNIAGKQTAVKDIADITTEQFDATFKTNVYAmfwlckaaiphlPPGAS-------------IINTGSIQSyQPSPTL 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 50726952  173 GGYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPV 212
Cdd:PRK06128 203 LDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPL 242
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
31-205 2.26e-09

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 58.32  E-value: 2.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLH--TTLLDITDPQSVQQAAKWVEMHvkeaglFG- 107
Cdd:PRK08324 425 ALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPDRalGVACDVTDEAAVQAAFEEAALA------FGg 498

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 ---LVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMG---------------PIGvtlallpllqqarGRVINITSVLGrLA 169
Cdd:PRK08324 499 vdiVVSNAGIA-ISGPIEETSDEDWRRSFDVNATGhflvareavrimkaqGLG-------------GSIVFIASKNA-VN 563

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 50726952  170 A--NGGGYCVSKfgleAFSDSLRR----DVAHFGIRVSIVEP 205
Cdd:PRK08324 564 PgpNFGAYGAAK----AAELHLVRqlalELGPDGIRVNGVNP 601
PRK06953 PRK06953
SDR family oxidoreductase;
31-210 4.06e-09

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 55.85  E-value: 4.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLAsclTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEAGLFglvn 110
Cdd:PRK06953   4 VLIVGASRGIGREFVRQYRADGWRVIA---TARDAAALAALQALGAEALALDVADPASVAGLAWKLDGEALDAAVY---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  111 nagVAGIIGP----TPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLAANGGG----YCVSKFGL 182
Cdd:PRK06953  77 ---VAGVYGPrtegVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSRMGSIGDATGTtgwlYRASKAAL 153

                        170       180
                 ....*....|....*....|....*...
gi 50726952  183 EAFSDSLRRDVAHfGIRVSIvEPGFFRT 210
Cdd:PRK06953 154 NDALRAASLQARH-ATCIAL-HPGWVRT 179
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 33-211 4.47e-09

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: 56.30  E-value: 4.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  33 ITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLH--TTLLDITDPQSVQQAAKWVEMHVKE-AGLFGLV 109
Cdd:cd08940   7 VTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGLAAKHgvKVLYHGADLSKPAAIEDMVAYAQRQfGGVDILV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 110 NNAGVAGIiGPTPWLTRDDFQRVLNVNTMGP-IGVTLALLPLLQQARGRVINITSVLGRLA-ANGGGYCVSKFGLEAFSD 187
Cdd:cd08940  87 NNAGIQHV-APIEDFPTEKWDAIIALNLSAVfHTTRLALPHMKKQGWGRIINIASVHGLVAsANKSAYVAAKHGVVGLTK 165

                       170       180
                ....*....|....*....|....
gi 50726952 188 SLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:cd08940 166 VVALETAGTGVTCNAICPGWVLTP 189
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 33-211 4.99e-09

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 56.09  E-value: 4.99e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  33 ITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKwvEMHVKEAGLFGLVNNA 112
Cdd:cd05363   8 ITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVA--ALVDRWGSIDILVNNA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 113 GVAGiIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQA--RGRVINITSVLGRLA-ANGGGYCVSKFGLEAFSDSL 189
Cdd:cd05363  86 ALFD-LAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgrGGKIINMASQAGRRGeALVGVYCATKAAVISLTQSA 164

                       170       180
                ....*....|....*....|..
gi 50726952 190 RRDVAHFGIRVSIVEPGFFRTP 211
Cdd:cd05363 165 GLNLIRHGINVNAIAPGVVDGE 186
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 108-211 7.24e-09

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 54.44  E-value: 7.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 LVNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRL-AANGGGYCVSKFGLEAF 185
Cdd:cd02266  35 VVHNAAI-LDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRlGRFILISSVAGLFgAPGLGGYAASKAALDGL 113

                        90       100
                ....*....|....*....|....*.
gi 50726952 186 SDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:cd02266 114 AQQWASEGWGNGLPATAVACGTWAGS 139
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 33-210 1.37e-08

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: 54.71  E-value: 1.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  33 ITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLL--DITDPQSVQQAakwVEMHVKE-AGLFGLV 109
Cdd:cd08943   6 VTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQGGPRALGVqcDVTSEAQVQSA---FEQAVLEfGGLDIVV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 110 NNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR--GRVINITSVLGRLAA-NGGGYCVSKfgleAFS 186
Cdd:cd08943  83 SNAGIA-TSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGigGNIVFNASKNAVAPGpNAAAYSAAK----AAE 157

                       170       180
                ....*....|....*....|....*....
gi 50726952 187 DSLRRDVA----HFGIRVSIVEP-GFFRT 210
Cdd:cd08943 158 AHLARCLAleggEDGIRVNTVNPdAVFRG 186
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 33-212 1.59e-08

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 54.39  E-value: 1.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLASCLTPS---GAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEAGLfgLV 109
Cdd:PRK07523  15 VTGSSQGIGYALAEGLAQAGAEVILNGRDPAklaAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGPIDI--LV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  110 NNAGVAgIIGPTPWLTRDDFQRVL--NVNTMGPIGvTLALLPLLQQARGRVINITSVLGRLAANG-GGYCVSKFGLEAFS 186
Cdd:PRK07523  93 NNAGMQ-FRTPLEDFPADAFERLLrtNISSVFYVG-QAVARHMIARGAGKIINIASVQSALARPGiAPYTATKGAVGNLT 170

                        170       180
                 ....*....|....*....|....*.
gi 50726952  187 DSLRRDVAHFGIRVSIVEPGFFRTPV 212
Cdd:PRK07523 171 KGMATDWAKHGLQCNAIAPGYFDTPL 196
PRK05867 PRK05867
SDR family oxidoreductase;
32-210 1.74e-08

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 54.27  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   32 FITGCDSGFGRLLALQLDQRGFRVlasCLTPSGAEDLQRVASS------RLHTTLLDITDPQSVQQAAKwvEMHVKEAGL 105
Cdd:PRK05867  13 LITGASTGIGKRVALAYVEAGAQV---AIAARHLDALEKLADEigtsggKVVPVCCDVSQHQQVTSMLD--QVTAELGGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  106 FGLVNNAGVAGIiGPTPWLTRDDFQRVLNVNTMGpIGVTLALLPLLQQARGR---VINITSVLGRL---AANGGGYCVSK 179
Cdd:PRK05867  88 DIAVCNAGIITV-TPMLDMPLEEFQRLQNTNVTG-VFLTAQAAAKAMVKQGQggvIINTASMSGHIinvPQQVSHYCASK 165

                        170       180       190
                 ....*....|....*....|....*....|.
gi 50726952  180 FGLEAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK05867 166 AAVIHLTKAMAVELAPHKIRVNSVSPGYILT 196
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 64-213 1.76e-08

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: 54.26  E-value: 1.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  64 GAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEagLFGLVNNAGVA---GIIGPTPwltrDDFQRVLNVNTMGP 140
Cdd:cd05352  48 KAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFGK--IDILIANAGITvhkPALDYTY----EQWNKVIDVNLNGV 121

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50726952 141 IGV-TLALLPLLQQARGRVINITSVLGRLA---ANGGGYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:cd05352 122 FNCaQAAAKIFKKQGKGSLIITASMSGTIVnrpQPQAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLT 198
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 28-212 2.00e-08

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: 54.46  E-value: 2.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  28 NAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTT----LLDITDPQSVQQAakwVEMHVKEA 103
Cdd:cd08933   9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGSckfvPCDVTKEEDIKTL---ISVTVERF 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 104 G-LFGLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLA-ANGGGYCVSKFG 181
Cdd:cd08933  86 GrIDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIGqKQAAPYVATKGA 165

                       170       180       190
                ....*....|....*....|....*....|.
gi 50726952 182 LEAFSDSLRRDVAHFGIRVSIVEPGFFRTPV 212
Cdd:cd08933 166 ITAMTKALAVDESRYGVRVNCISPGNIWTPL 196
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 31-216 2.28e-08

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 54.25  E-value: 2.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDlqrvasSRLHTTLLDITDPQSVQQAAKWVEMhvKEAGLFGLVN 110
Cdd:PRK06171  12 IIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQH------ENYQFVPTDVSSAEEVNHTVAEIIE--KFGRIDGLVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  111 NAGVAGiigptPWLTRD-------------DFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLAANGGG-Y 175
Cdd:PRK06171  84 NAGINI-----PRLLVDekdpagkyelneaAFDKMFNINQKGVFLMSQAVARQMVKQHdGVIVNMSSEAGLEGSEGQScY 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 50726952  176 CVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFR-TPVTNLE 216
Cdd:PRK06171 159 AATKAALNSFTRSWAKELGKHNIRVVGVAPGILEaTGLRTPE 200
PRK06947 PRK06947
SDR family oxidoreductase;
31-212 3.27e-08

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 53.66  E-value: 3.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQ----RVASSRLHTTLLDITDPQSVqqaakwVEMHVKEAGLF 106
Cdd:PRK06947   5 VLITGASRGIGRATAVLAAARGWSVGINYARDAAAAEETadavRAAGGRACVVAGDVANEADV------IAMFDAVQSAF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  107 G----LVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR----GRVINITSVLGRLAANGG--GYC 176
Cdd:PRK06947  79 GrldaLVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRggrgGAIVNVSSIASRLGSPNEyvDYA 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 50726952  177 VSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPV 212
Cdd:PRK06947 159 GSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEI 194
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 31-212 3.57e-08

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 53.58  E-value: 3.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLT-PSGAEDLQ---RVASSRLHTTLLDITDPQSVQqaaKWVEMHVKEAG-L 105
Cdd:PRK08936  10 VVITGGSTGLGRAMAVRFGKEKAKVVINYRSdEEEANDVAeeiKKAGGEAIAVKGDVTVESDVV---NLIQTAVKEFGtL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  106 FGLVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGP-IGV-TLALLPLLQQARGRVINITSVLGRLA-ANGGGYCVSKFGL 182
Cdd:PRK08936  87 DVMINNAGIE-NAVPSHEMSLEDWNKVINTNLTGAfLGSrEAIKYFVEHDIKGNIINMSSVHEQIPwPLFVHYAASKGGV 165

                        170       180       190
                 ....*....|....*....|....*....|
gi 50726952  183 EAFSDSLRRDVAHFGIRVSIVEPGFFRTPV 212
Cdd:PRK08936 166 KLMTETLAMEYAPKGIRVNNIGPGAINTPI 195
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 33-218 4.20e-08

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


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 53.24  E-value: 4.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  33 ITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLL----DITDPQSVQQAAKWVEMHVKEAGLfgL 108
Cdd:cd05322   7 VIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYGEKAYgfgaDATNEQSVIALSKGVDEIFKRVDL--L 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 109 VNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPI--GVTLALLPLLQQARGRVINITSVLGRLAA-NGGGYCVSKFGLEAF 185
Cdd:cd05322  85 VYSAGIA-KSAKITDFELGDFDRSLQVNLVGYFlcAREFSKLMIRDGIQGRIIQINSKSGKVGSkHNSGYSAAKFGGVGL 163

                       170       180       190
                ....*....|....*....|....*....|....
gi 50726952 186 SDSLRRDVAHFGIRVSIVEPG-FFRTPVtnLESL 218
Cdd:cd05322 164 TQSLALDLAEHGITVNSLMLGnLLKSPM--FQSL 195
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 31-211 5.72e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 52.98  E-value: 5.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSG--AEDLQRVASsrlhttllDITDPQSVQQAAKwvemHVKEA--GLF 106
Cdd:PRK06523  12 ALVTGGTKGIGAATVARLLEAGARVVTTARSRPDdlPEGVEFVAA--------DLTTAEGCAAVAR----AVLERlgGVD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  107 GLVNNAGvaGIIGPT---PWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLAANGG--GYCVSKF 180
Cdd:PRK06523  80 ILVHVLG--GSSAPAggfAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGsGVIIHVTSIQRRLPLPESttAYAAAKA 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 50726952  181 GLEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK06523 158 ALSTYSKSLSKEVAPKGVRVNTVSPGWIETE 188
PRK08628 PRK08628
SDR family oxidoreductase;
31-230 6.84e-08

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 52.65  E-value: 6.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRG-FRVLASCLTPSG--AEDLQRvASSRLHTTLLDITDPQSVQQAakwVEMHVKEAG-LF 106
Cdd:PRK08628  10 VIVTGGASGIGAAISLRLAEEGaIPVIFGRSAPDDefAEELRA-LQPRAEFVQVDLTDDAQCRDA---VEQTVAKFGrID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  107 GLVNNAGVAGIIGptpwL--TRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGrLAANGG--GYCVSKFGL 182
Cdd:PRK08628  86 GLVNNAGVNDGVG----LeaGREAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISSKTA-LTGQGGtsGYAAAKGAQ 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 50726952  183 EAFSDSLRRDVAHFGIRVSIVEPGFFRTP-----VTNLESLEKTLQACWARLP 230
Cdd:PRK08628 161 LALTREWAVALAKDGVRVNAVIPAEVMTPlyenwIATFDDPEAKLAAITAKIP 213
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 33-221 6.85e-08

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: 52.61  E-value: 6.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  33 ITGCDSGFGRLLALQLDQRGFRVlasCLTPSGAEDLQRVASS-------RLHTTLLDITDPQSVQQAAKwVEMHVKEAGL 105
Cdd:cd05356   6 VTGATDGIGKAYAEELAKRGFNV---ILISRTQEKLDAVAKEieekygvETKTIAADFSAGDDIYERIE-KELEGLDIGI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 106 fgLVNNAGVAGIIgPTPWL--TRDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLG-----RLAAngggYCV 177
Cdd:cd05356  82 --LVNNVGISHSI-PEYFLetPEDELQDIINVNVMATLKMTRLILpGMVKRKKGAIVNISSFAGliptpLLAT----YSA 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 50726952 178 SKFGLEAFSDSLRRDVAHFGIRVSIVEPGFfrtPVTNLESLEKT 221
Cdd:cd05356 155 SKAFLDFFSRALYEEYKSQGIDVQSLLPYL---VATKMSKIRKS 195
PRK12746 PRK12746
SDR family oxidoreductase;
32-212 7.32e-08

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 52.73  E-value: 7.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   32 FITGCDSGFGRLLALQLDQRGFRV-LASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVE-------MHVKEA 103
Cdd:PRK12746  10 LVTGASRGIGRAIAMRLANDGALVaIHYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEqlknelqIRVGTS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  104 GLFGLVNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQaRGRVINITSVLGRLAANGG-GYCVSKFGL 182
Cdd:PRK12746  90 EIDILVNNAGI-GTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRA-EGRVINISSAEVRLGFTGSiAYGLSKGAL 167

                        170       180       190
                 ....*....|....*....|....*....|
gi 50726952  183 EAFSDSLRRDVAHFGIRVSIVEPGFFRTPV 212
Cdd:PRK12746 168 NTMTLPLAKHLGERGITVNTIMPGYTKTDI 197
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 31-206 7.53e-08

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: 52.34  E-value: 7.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRV-LASCLTPSG---AEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEAGlf 106
Cdd:cd08930   5 ILITGAAGLIGKAFCKALLSAGARLiLADINAPALeqlKEELTNLYKNRVIALELDITSKESIKELIESYLEKFGRID-- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 107 GLVNNAGvagiIGPTPWLTR------DDFQRVLNVNTMGPIGVTLALLPL-LQQARGRVINITSVLGRLAAN-----GGG 174
Cdd:cd08930  83 ILINNAY----PSPKVWGSRfeefpyEQWNEVLNVNLGGAFLCSQAFIKLfKKQGKGSIINIASIYGVIAPDfriyeNTQ 158

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 50726952 175 ------YCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPG 206
Cdd:cd08930 159 myspveYSVIKAGIIHLTKYLAKYYADTGIRVNAISPG 196
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 33-212 8.66e-08

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 52.32  E-value: 8.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQRVASS---RLHTTLLDITDPQSVQQAAKWVemHVKEAGLFGLV 109
Cdd:PRK08265  11 VTGGATLIGAAVARALVAAGARVA---IVDIDADNGAAVAASlgeRARFIATDITDDAAIERAVATV--VARFGRVDILV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  110 NNA------GVAGiigptpwlTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLAANGGG-YCVSKFGL 182
Cdd:PRK08265  86 NLActylddGLAS--------SRADWLAALDVNLVSAAMLAQAAHPHLARGGGAIVNFTSISAKFAQTGRWlYPASKAAI 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 50726952  183 EAFSDSLRRDVAHFGIRVSIVEPGFFRTPV 212
Cdd:PRK08265 158 RQLTRSMAMDLAPDGIRVNSVSPGWTWSRV 187
PRK06138 PRK06138
SDR family oxidoreductase;
31-211 1.21e-07

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 51.69  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAED-LQRVASSRLHTTLL-DITDPQSVQQAAKWVEmhVKEAGLFGL 108
Cdd:PRK06138   8 AIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERvAAAIAAGGRAFARQgDVGSAEAVEALVDFVA--ARWGRLDVL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  109 VNNAGVaGIIGPTPWLTRDDFQRVLNVNTMGP-IGVTLALLPLLQQARGRVINITSVLGRLAANG-GGYCVSKFGLEAFS 186
Cdd:PRK06138  86 VNNAGF-GCGGTVVTTDEADWDAVMRVNVGGVfLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGrAAYVASKGAIASLT 164

                        170       180
                 ....*....|....*....|....*
gi 50726952  187 DSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK06138 165 RAMALDHATDGIRVNAVAPGTIDTP 189
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 27-210 1.62e-07

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: 51.36  E-value: 1.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  27 SNAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLL----DITDPQSVQQAAKWVEMHvkE 102
Cdd:cd05343   5 RGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLFpyqcDLSNEEQILSMFSAIRTQ--H 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 103 AGLFGLVNNAGVAgiiGPTPWLT--RDDFQRVLNVNTMGPIGVTLALL---PLLQQARGRVINITSVLGR---LAANGGG 174
Cdd:cd05343  83 QGVDVCINNAGLA---RPEPLLSgkTEGWKEMFDVNVLALSICTREAYqsmKERNVDDGHIININSMSGHrvpPVSVFHF 159

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 50726952 175 YCVSKFGLEAFSDSLRRDV--AHFGIRVSIVEPGFFRT 210
Cdd:cd05343 160 YAATKHAVTALTEGLRQELreAKTHIRATSISPGLVET 197
PRK07063 PRK07063
SDR family oxidoreductase;
31-213 1.75e-07

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 51.59  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVL-----ASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVkeAGL 105
Cdd:PRK07063  10 ALVTGAAQGIGAAIARAFAREGAAVAladldAALAERAAAAIARDVAGARVLAVPADVTDAASVAAAVAAAEEAF--GPL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  106 FGLVNNAGVAGIIGPTPwLTRDDFQRVLNVNTMGPI-GVTLALLPLLQQARGRVINITSVLG-RLAANGGGYCVSKFGLE 183
Cdd:PRK07063  88 DVLVNNAGINVFADPLA-MTDEDWRRCFAVDLDGAWnGCRAVLPGMVERGRGSIVNIASTHAfKIIPGCFPYPVAKHGLL 166

                        170       180       190
                 ....*....|....*....|....*....|
gi 50726952  184 AFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:PRK07063 167 GLTRALGIEYAARNVRVNAIAPGYIETQLT 196
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 28-211 2.12e-07

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: 51.30  E-value: 2.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  28 NAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDpqsVQQAAKWVEMHVKEAGLFG 107
Cdd:cd08935   5 NKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAAD---VLDRASLERAREEIVAQFG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 ----LVNNAGV---AGIIGPTPW----------LTRDDFQRVLNVNTMG---PIGVtlALLPLLQQARGRVINITSV--- 164
Cdd:cd08935  82 tvdiLINGAGGnhpDATTDPEHYepeteqnffdLDEEGWEFVFDLNLNGsflPSQV--FGKDMLEQKGGSIINISSMnaf 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 50726952 165 --LGRLAAngggYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:cd08935 160 spLTKVPA----YSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTP 204
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 33-214 4.39e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 50.31  E-value: 4.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQRVASS------RLHTTLLDITDPQSvqqAAKWVEMHVKE-AGL 105
Cdd:PRK07478  11 ITGASSGIGRAAAKLFAREGAKVV---VGARRQAELDQLVAEiraeggEAVALAGDVRDEAY---AKALVALAVERfGGL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  106 FGLVNNAGVAGIIGPTPWLTRDDFQRVLNVN-TMGPIGVTLALLPLLQQARGRVINITSVLGRLAANGG--GYCVSKFGL 182
Cdd:PRK07478  85 DIAFNNAGTLGEMGPVAEMSLEGWRETLATNlTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHTAGFPGmaAYAASKAGL 164

                        170       180       190
                 ....*....|....*....|....*....|..
gi 50726952  183 EAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTN 214
Cdd:PRK07478 165 IGLTQVLAAEYGAQGIRVNALLPGGTDTPMGR 196
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 31-210 4.54e-07

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


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 50.26  E-value: 4.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAE---DLQRVASSRLHTTLLDITDPQSVQQAAKwvEMHVKEAGLFG 107
Cdd:cd05365   2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEavaAAIQQAGGQAIGLECNVTSEQDLEAVVK--ATVSQFGGITI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 LVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVI-NITSVLGRLAA-NGGGYCVSKFGLEAF 185
Cdd:cd05365  80 LVNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAIlNISSMSSENKNvRIAAYGSSKAAVNHM 159

                       170       180
                ....*....|....*....|....*
gi 50726952 186 SDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:cd05365 160 TRNLAFDLGPKGIRVNAVAPGAVKT 184
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 31-211 5.02e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 50.42  E-value: 5.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSG-AEDLQRVASSRLHTTLL---DITDPQSVQQAakwVEMHVKEAG-L 105
Cdd:PRK06701  49 ALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEdANETKQRVEKEGVKCLLipgDVSDEAFCKDA---VEETVRELGrL 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  106 FGLVNNAG----VAGIigptPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQArGRVINITSVLGrLAANGG--GYCVSK 179
Cdd:PRK06701 126 DILVNNAAfqypQQSL----EDITAEQLDKTFKTNIYSYFHMTKAALPHLKQG-SAIINTGSITG-YEGNETliDYSATK 199

                        170       180       190
                 ....*....|....*....|....*....|..
gi 50726952  180 FGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK06701 200 GAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTP 231
PRK08177 PRK08177
SDR family oxidoreductase;
31-210 5.12e-07

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 49.64  E-value: 5.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTtlLDITDPQSVQQAAKwvemHVKEAGLFGLVN 110
Cdd:PRK08177   4 ALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIEK--LDMNDPASLDQLLQ----RLQGQRFDLLFV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  111 NAGVAgiiGPTPW----LTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLAANGGG----YCVSKFGL 182
Cdd:PRK08177  78 NAGIS---GPAHQsaadATAAEIGQLFLTNAIAPIRLARRLLGQVRPGQGVLAFMSSQLGSVELPDGGemplYKASKAAL 154

                        170       180
                 ....*....|....*....|....*...
gi 50726952  183 EAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK08177 155 NSMTRSFVAELGEPTLTVLSMHPGWVKT 182
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 85-210 6.58e-07

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 49.49  E-value: 6.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   85 DPQSVQQAAKWVEMHVKEagLFGLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPL-LQQARGRVINITS 163
Cdd:PRK08945  75 TPQNYQQLADTIEEQFGR--LDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLlLKSPAASLVFTSS 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 50726952  164 VLGRLA-ANGGGYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK08945 153 SVGRQGrANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRT 200
PRK07577 PRK07577
SDR family oxidoreductase;
26-206 6.85e-07

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 49.34  E-value: 6.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   26 ASNAFVFITGCDSGFGRLLALQLDQRGFRVLAscLTPSGAEDLqrvaSSRLHTTllDITDPQsvQQAAKWVEMhVKEAGL 105
Cdd:PRK07577   1 MSSRTVLVTGATKGIGLALSLRLANLGHQVIG--IARSAIDDF----PGELFAC--DLADIE--QTAATLAQI-NEIHPV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  106 FGLVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGRLAANGGGYCVSKFGLEA 184
Cdd:PRK07577  70 DAIVNNVGIA-LPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREqGRIVNICSRAIFGALDRTSYSAAKSALVG 148

                        170       180
                 ....*....|....*....|..
gi 50726952  185 FSDSLRRDVAHFGIRVSIVEPG 206
Cdd:PRK07577 149 CTRTWALELAEYGITVNAVAPG 170
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
31-139 7.33e-07

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 49.98  E-value: 7.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCdSGF-GRLLALQLDQRGFRVLASCLTPSGAEDLQRVAssRLHTTLLDITDPQSVQQAAKWVEmhvkeaglfGLV 109
Cdd:COG0451   2 ILVTGG-AGFiGSHLARRLLARGHEVVGLDRSPPGAANLAALP--GVEFVRGDLRDPEALAAALAGVD---------AVV 69

                        90       100       110
                ....*....|....*....|....*....|
gi 50726952 110 NNAGVAGIigptpwlTRDDFQRVLNVNTMG 139
Cdd:COG0451  70 HLAAPAGV-------GEEDPDETLEVNVEG 92
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 31-207 1.25e-06

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


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 48.81  E-value: 1.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAED--LQRVASSRLHTTLL--DITDPQSVQQAAKWVEMHVKEAGLf 106
Cdd:cd05357   3 ALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQrlKDELNALRNSAVLVqaDLSDFAACADLVAAAFRAFGRCDV- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 107 gLVNNAGV--AGIIGPTPWltrDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINIT-SVLGRLAANGGGYCVSKFGL 182
Cdd:cd05357  82 -LVNNASAfyPTPLGQGSE---DAWAELFGINLKAPYLLIQAFArRLAGSRNGSIINIIdAMTDRPLTGYFAYCMSKAAL 157

                       170       180
                ....*....|....*....|....*
gi 50726952 183 EAFSDSLRRDVAHFgIRVSIVEPGF 207
Cdd:cd05357 158 EGLTRSAALELAPN-IRVNGIAPGL 181
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 33-218 1.29e-06

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 48.80  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEdlQRVASSR-----LHTTLLDITDPQSVQQAAkwvEMHVKEAGLFG 107
Cdd:PRK05876  11 ITGGASGIGLATGTEFARRGARVVLGDVDKPGLR--QAVNHLRaegfdVHGVMCDVRHREEVTHLA---DEAFRLLGHVD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 LV-NNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPI-GVTLALLPLLQQARGRVINITSVLGRLAANGG--GYCVSKFGLE 183
Cdd:PRK05876  86 VVfSNAGIV-VGGPIVEMTHDDWRWVIDVDLWGSIhTVEAFLPRLLEQGTGGHVVFTASFAGLVPNAGlgAYGVAKYGVV 164

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 50726952  184 AFSDSLRRDVAHFGIRVSIVEPGFFRTP-VTNLESL 218
Cdd:PRK05876 165 GLAETLAREVTADGIGVSVLCPMVVETNlVANSERI 200
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 25-210 1.52e-06

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 48.64  E-value: 1.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  25 PASNAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKwvemHVKEAG 104
Cdd:cd08951   4 PPPMKRIFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSSLAETRKLAD----QVNAIG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 105 LF-GLVNNAGVagIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLqqargRVINITSVL--------------GRLA 169
Cdd:cd08951  80 RFdAVIHNAGI--LSGPNRKTPDTGIPAMVAVNVLAPYVLTALIRRPK-----RLIYLSSGMhrggnaslddidwfNRGE 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 50726952 170 ANGGGYCVSKFGLEAFSDSLRR---DVahfgiRVSIVEPGFFRT 210
Cdd:cd08951 153 NDSPAYSDSKLHVLTLAAAVARrwkDV-----SSNAVHPGWVPT 191
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 31-211 1.80e-06

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: 47.90  E-value: 1.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTllDITDPQSVQQAAkwvemhvKEAGLFGLVN 110
Cdd:cd11730   1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALARPA--DVAAELEVWALA-------QELGPLDLLV 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 111 NAgvAGIIGPTPWL--TRDDFQRVLNVNTMGPIGVTLALLPLLQQArGRVINITSVLGRLAANG-GGYCVSKFGLEAFSD 187
Cdd:cd11730  72 YA--AGAILGKPLArtKPAAWRRILDANLTGAALVLKHALALLAAG-ARLVFLGAYPELVMLPGlSAYAAAKAALEAYVE 148

                       170       180
                ....*....|....*....|....
gi 50726952 188 SLRRDVAhfGIRVSIVEPGFFRTP 211
Cdd:cd11730 149 VARKEVR--GLRLTLVRPPAVDTG 170
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 33-210 2.04e-06

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 48.30  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQ---RVASSRLHTTLLDITDPQSVQQAAKwvemhvKEAGLFG-- 107
Cdd:PRK06113  16 ITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVdeiQQLGGQAFACRCDITSEQELSALAD------FALSKLGkv 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 --LVNNAGVAgiiGPTPW-LTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVI-NITSVLG-----RLAAngggYCVS 178
Cdd:PRK06113  90 diLVNNAGGG---GPKPFdMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVIlTITSMAAenkniNMTS----YASS 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 50726952  179 KFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK06113 163 KAAASHLVRNMAFDLGEKNIRVNGIAPGAILT 194
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 31-206 2.08e-06

(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: 48.09  E-value: 2.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLtpsGAEDLQRVASSRLHTTLLD---------ITDPQSVQQAAKWVEMHVK 101
Cdd:cd05353   8 VLVTGAGGGLGRAYALAFAERGAKVVVNDL---GGDRKGSGKSSSAADKVVDeikaaggkaVANYDSVEDGEKIVKTAID 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 102 EaglFG----LVNNAGVagiigptpwlTRD---------DFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITSVLGr 167
Cdd:cd05353  85 A---FGrvdiLVNNAGI----------LRDrsfakmseeDWDLVMRVHLKGSFKVTRAAWPYMRKQKfGRIINTSSAAG- 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 50726952 168 LAANGG--GYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPG 206
Cdd:cd05353 151 LYGNFGqaNYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA 191
PRK05866 PRK05866
SDR family oxidoreductase;
31-211 4.08e-06

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 47.43  E-value: 4.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLAsclTPSGAEDLQRVAS------SRLHTTLLDITDPQSVQQAAKWVEMHVkeAG 104
Cdd:PRK05866  43 ILLTGASSGIGEAAAEQFARRGATVVA---VARREDLLDAVADritragGDAMAVPCDLSDLDAVDALVADVEKRI--GG 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  105 LFGLVNNAGVAgIIGPT-PWLTR-DDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINITS--VLGRLAANGGGYCVSK 179
Cdd:PRK05866 118 VDILINNAGRS-IRRPLaESLDRwHDVERTMVLNYYAPLRLIRGLAPGMLERGdGHIINVATwgVLSEASPLFSVYNASK 196

                        170       180       190
                 ....*....|....*....|....*....|..
gi 50726952  180 FGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK05866 197 AALSAVSRVIETEWGDRGVHSTTLYYPLVATP 228
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 28-210 4.53e-06

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


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 47.19  E-value: 4.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  28 NAFVFITGCDSGFGRLLALQLDQRGFRVlasCLTPSGAEDLQRVASS-RLHTTLL--DITDPQSVQQAAKwvEMHVKEAG 104
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKV---VFADIDEERGADFAEAeGPNLFFVhgDVADETLVKFVVY--AMLEKLGR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 105 LFGLVNNAGVA--GIIGPTPWltrDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLG-RLAANGGGYCVSKFG 181
Cdd:cd09761  76 IDVLVNNAARGskGILSSLLL---EEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAfQSEPDSEAYAASKGG 152

                       170       180
                ....*....|....*....|....*....
gi 50726952 182 LEAFSDSLRRDVAHFgIRVSIVEPGFFRT 210
Cdd:cd09761 153 LVALTHALAMSLGPD-IRVNCISPGWINT 180
PRK06123 PRK06123
SDR family oxidoreductase;
27-210 5.08e-06

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 47.08  E-value: 5.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   27 SNAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLL----DITDPQSVQQAAKWVEmhvKE 102
Cdd:PRK06123   1 MRKVMIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVVQAIRRQGGEALavaaDVADEADVLRLFEAVD---RE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  103 AG-LFGLVNNAGvagIIGPTPWLTRDD---FQRVLNVNTMGPIgVTLALLPLLQQAR-----GRVINITSVLGRLAANGG 173
Cdd:PRK06123  78 LGrLDALVNNAG---ILEAQMRLEQMDaarLTRIFATNVVGSF-LCAREAVKRMSTRhggrgGAIVNVSSMAARLGSPGE 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 50726952  174 --GYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK06123 154 yiDYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYT 192
PRK07831 PRK07831
SDR family oxidoreductase;
75-220 5.93e-06

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 46.95  E-value: 5.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   75 RLHTTLLDITDPQSVQqaAKWVEMHVKEAGLFGLVNNAGVAGIiGPTPWLTRDDFQRVLNVNTMGPIGVT--LALLPLLQ 152
Cdd:PRK07831  70 RVEAVVCDVTSEAQVD--ALIDAAVERLGRLDVLVNNAGLGGQ-TPVVDMTDDEWSRVLDVTLTGTFRATraALRYMRAR 146

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50726952  153 QARGRVINITSVLG-RLAANGGGYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTP----VTNLESLEK 220
Cdd:PRK07831 147 GHGGVIVNNASVLGwRAQHGQAHYAAAKAGVMALTRCSALEAAEYGVRINAVAPSIAMHPflakVTSAELLDE 219
PRK07985 PRK07985
SDR family oxidoreductase;
19-212 8.58e-06

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 46.53  E-value: 8.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   19 RDRQSLpasnafvfITGCDSGFGRLLALQLDQRGFRVLASCLtPSGAEDLQRVAS----SRLHTTLL--DITDPQSvqqA 92
Cdd:PRK07985  48 KDRKAL--------VTGGDSGIGRAAAIAYAREGADVAISYL-PVEEEDAQDVKKiieeCGRKAVLLpgDLSDEKF---A 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   93 AKWVEMHVKEAGlfGLVNNAGVAG---IIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQqaRGRVINITSVLG--R 167
Cdd:PRK07985 116 RSLVHEAHKALG--GLDIMALVAGkqvAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLP--KGASIITTSSIQayQ 191

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 50726952  168 LAANGGGYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPV 212
Cdd:PRK07985 192 PSPHLLDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTAL 236
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
33-230 1.08e-05

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 46.05  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLASCL-----TPSGAEDLQRvassRLHTTLLDITDPQSVQQAakwVEMHVKEAGLFG 107
Cdd:PRK12481  13 ITGCNTGLGQGMAIGLAKAGADIVGVGVaeapeTQAQVEALGR----KFHFITADLIQQKDIDSI---VSQAVEVMGHID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 -LVNNagvAGIIGPTPWL--TRDDFQRVLNVN--TMGPIGVTLALLPLLQQARGRVINITSVlgrLAANGG----GYCVS 178
Cdd:PRK12481  86 iLINN---AGIIRRQDLLefGNKDWDDVININqkTVFFLSQAVAKQFVKQGNGGKIINIASM---LSFQGGirvpSYTAS 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 50726952  179 KFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTN-LESLEKTLQACWARLP 230
Cdd:PRK12481 160 KSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAaLRADTARNEAILERIP 212
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 33-211 1.19e-05

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


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 46.13  E-value: 1.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  33 ITGCDSGFGRLLALQLDQRGFRVLASCLtPSGAEDLQRV------ASSRLHTTLLDITDPQSVQQAakwVEMHVKEAG-L 105
Cdd:cd05355  31 ITGGDSGIGRAVAIAFAREGADVAINYL-PEEEDDAEETkklieeEGRKCLLIPGDLGDESFCRDL---VKEVVKEFGkL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 106 FGLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQArGRVINITSVLGRlaaNGGG----YCVSKFG 181
Cdd:cd05355 107 DILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKKG-SSIINTTSVTAY---KGSPhlldYAATKGA 182

                       170       180       190
                ....*....|....*....|....*....|
gi 50726952 182 LEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:cd05355 183 IVAFTRGLSLQLAEKGIRVNAVAPGPIWTP 212
PRK08251 PRK08251
SDR family oxidoreductase;
31-213 1.81e-05

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 45.31  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGfRVLASC------LTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKwvEMHVKEAG 104
Cdd:PRK08251   5 ILITGASSGLGAGMAREFAAKG-RDLALCarrtdrLEELKAELLARYPGIKVAVAALDVNDHDQVFEVFA--EFRDELGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  105 LFGLVNNAGV---AGIIGPTPWLTRddfqRVLNVNTMGPIG-VTLALLPLLQQARGRVINITSVL------GRLAAnggg 174
Cdd:PRK08251  82 LDRVIVNAGIgkgARLGTGKFWANK----ATAETNFVAALAqCEAAMEIFREQGSGHLVLISSVSavrglpGVKAA---- 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 50726952  175 YCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:PRK08251 154 YAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMN 192
PRK07775 PRK07775
SDR family oxidoreductase;
31-228 1.86e-05

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 45.52  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRV------------LASCLTPSGAEdlqRVAssrLHttlLDITDPQSV-------QQ 91
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPValgarrvekceeLVDKIRADGGE---AVA---FP---LDVTDPDSVksfvaqaEE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   92 AAKWVEMHVKEAG--LFGLVNNagvagiigptpwLTRDDFQRVLNVNTMGPIGV-TLALLPLLQQARGRVINITS-VLGR 167
Cdd:PRK07775  84 ALGEIEVLVSGAGdtYFGKLHE------------ISTEQFESQVQIHLVGANRLaTAVLPGMIERRRGDLIFVGSdVALR 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50726952  168 LAANGGGYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPV---TNLESLEKTLQAcWAR 228
Cdd:PRK07775 152 QRPHMGAYGAAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGMgwsLPAEVIGPMLED-WAK 214
PRK06500 PRK06500
SDR family oxidoreductase;
28-211 2.32e-05

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 44.95  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   28 NAFVFITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQRVASSRLHTTLLDITDPQSVQqAAKWVEMHVKEAG--L 105
Cdd:PRK06500   6 GKTALITGGTSGIGLETARQFLAEGARVA---ITGRDPASLEAARAELGESALVIRADAGDVA-AQKALAQALAEAFgrL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  106 FGLVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINiTSVLGRL-AANGGGYCVSKFGLEA 184
Cdd:PRK06500  82 DAVFINAGVA-KFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPASIVLN-GSINAHIgMPNSSVYAASKAALLS 159

                        170       180
                 ....*....|....*....|....*..
gi 50726952  185 FSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK06500 160 LAKTLSGELLPRGIRVNAVSPGPVQTP 186
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
33-230 2.69e-05

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 44.86  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLA-SCLTPSgaEDLQRVASsrLHTTLLDIT-DPQSVQQAAKWVEMHVKEAGLFG-LV 109
Cdd:PRK08993  15 VTGCDTGLGQGMALGLAEAGCDIVGiNIVEPT--ETIEQVTA--LGRRFLSLTaDLRKIDGIPALLERAVAEFGHIDiLV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  110 NNagvAGIIGPTPWL--TRDDFQRVLNVNTMGPIGVTLALLPL--LQQARGRVINITSVlgrLAANGG----GYCVSKFG 181
Cdd:PRK08993  91 NN---AGLIRREDAIefSEKDWDDVMNLNIKSVFFMSQAAAKHfiAQGNGGKIINIASM---LSFQGGirvpSYTASKSG 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 50726952  182 LEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTN-LESLEKTLQACWARLP 230
Cdd:PRK08993 165 VMGVTRLMANEWAKHNINVNAIAPGYMATNNTQqLRADEQRSAEILDRIP 214
PLN02253 PLN02253
xanthoxin dehydrogenase
 33-205 2.81e-05

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 44.81  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVlasCLTpsgaeDLQRVASSRLHTTL----------LDITDPQSVQQAakwVEMHVKE 102
Cdd:PLN02253  23 VTGGATGIGESIVRLFHKHGAKV---CIV-----DLQDDLGQNVCDSLggepnvcffhCDVTVEDDVSRA---VDFTVDK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  103 AG-LFGLVNNAGVAGiiGPTPWLTR---DDFQRVLNVNTMGP-IGVTLALLPLLQQARGRVINITSVLGRLAANG-GGYC 176
Cdd:PLN02253  92 FGtLDIMVNNAGLTG--PPCPDIRNvelSEFEKVFDVNVKGVfLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGpHAYT 169

                        170       180
                 ....*....|....*....|....*....
gi 50726952  177 VSKFGLEAFSDSLRRDVAHFGIRVSIVEP 205
Cdd:PLN02253 170 GSKHAVLGLTRSVAAELGKHGIRVNCVSP 198
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 33-211 2.84e-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: 44.89  E-value: 2.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  33 ITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQR--VASS---RLHTTLLDITDPQSVQQAAKWVEMHVKEagLFG 107
Cdd:cd09808   6 ITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKeiETESgnqNIFLHIVDMSDPKQVWEFVEEFKEEGKK--LHV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 LVNNAGVagiIGPTPWLTRDDFQRVLNVNTMGP-IGVTLALLPLLQQARGRVINITSvlgrlaangGGYCVSKF------ 180
Cdd:cd09808  84 LINNAGC---MVNKRELTEDGLEKNFATNTLGTyILTTHLIPVLEKEEDPRVITVSS---------GGMLVQKLntnnlq 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 50726952 181 -------GLEAFSDSLRRDV--------AHFGIRVSIVEPGFFRTP 211
Cdd:cd09808 152 sertafdGTMVYAQNKRQQVimteqwakKHPEIHFSVMHPGWADTP 197
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 31-212 3.34e-05

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: 44.44  E-value: 3.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQ--RVASSRLHTTLLDITDPQSVQQAakwvemHVKEAGLFG- 107
Cdd:cd08937   7 VVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAeiLAAGDAAHVHTADLETYAGAQGV------VRAAVERFGr 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 ---LVNNAGvaGIIGPTPWLTRDDFQRVLNVN-TMGPIGVTLALLPLLQQAR--GRVINITSVLGRlAANGGGYCVSKFG 181
Cdd:cd08937  81 vdvLINNVG--GTIWAKPYEHYEEEQIEAEIRrSLFPTLWCCRAVLPHMLERqqGVIVNVSSIATR-GIYRIPYSAAKGG 157

                       170       180       190
                ....*....|....*....|....*....|.
gi 50726952 182 LEAFSDSLRRDVAHFGIRVSIVEPGFFRTPV 212
Cdd:cd08937 158 VNALTASLAFEHARDGIRVNAVAPGGTEAPP 188
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 31-214 4.78e-05

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: 43.92  E-value: 4.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVL-----ASCLTPSGAEDLQ----------RVASSRLHTTLLDITDPQSVQQAakw 95
Cdd:cd05338   6 AFVTGASRGIGRAIALRLAKAGATVVvaaktASEGDNGSAKSLPgtieetaeeiEAAGGQALPIVVDVRDEDQVRAL--- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  96 VEMHVKEAG-LFGLVNNAGVA--GIIGPTPwLTRddFQRVLNVNTMGP-IGVTLALLPLLQQARGRVINITSVLGRLAAN 171
Cdd:cd05338  83 VEATVDQFGrLDILVNNAGAIwlSLVEDTP-AKR--FDLMQRVNLRGTyLLSQAALPHMVKAGQGHILNISPPLSLRPAR 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 50726952 172 GG-GYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPG-FFRTPVTN 214
Cdd:cd05338 160 GDvAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPStAIETPAAT 204
PRK09135 PRK09135
pteridine reductase; Provisional
 31-206 6.34e-05

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 43.76  E-value: 6.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTpSGAEDLQRVA---SSRLHTTLLDITDPQSVQQAAKWVEMHVKEAG-LF 106
Cdd:PRK09135   9 ALITGGARRIGAAIARTLHAAGYRVAIHYHR-SAAEADALAAelnALRPGSAAALQADLLDPDALPELVAACVAAFGrLD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  107 GLVNNAGVagiIGPTPW--LTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLG-RLAANGGGYCVSKFGLE 183
Cdd:PRK09135  88 ALVNNASS---FYPTPLgsITEAQWDDLFASNLKAPFFLSQAAAPQLRKQRGAIVNITDIHAeRPLKGYPVYCAAKAALE 164

                        170       180
                 ....*....|....*....|...
gi 50726952  184 AFSDSLRRDVAHfGIRVSIVEPG 206
Cdd:PRK09135 165 MLTRSLALELAP-EVRVNAVAPG 186
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 24-210 6.46e-05

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 43.54  E-value: 6.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   24 LPASNAFVFITGCDSGFGRLLALQLDQRGFRVLASCL-TPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHvke 102
Cdd:PRK08642   1 MQISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHqSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEH--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  103 aglFG-----LVNNAGVAGIIGPT-----PWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-GRVINI-TSVLGRLAA 170
Cdd:PRK08642  78 ---FGkpittVVNNALADFSFDGDarkkaDDITWEDFQQQLEGSVKGALNTIQAALPGMREQGfGRIINIgTNLFQNPVV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 50726952  171 NGGGYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK08642 155 PYHDYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRT 194
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 75-206 6.73e-05

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 43.62  E-value: 6.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   75 RLHTTLLDITDPQSVQQAAKWVEMHVKEAGLfgLVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQA 154
Cdd:PRK12859  69 KVSSMELDLTQNDAPKELLNKVTEQLGYPHI--LVNNAAYS-TNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKK 145

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 50726952  155 RG-RVINITS------VLGRLAangggYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPG 206
Cdd:PRK12859 146 SGgRIINMTSgqfqgpMVGELA-----YAATKGAIDALTSSLAAEVAHLGITVNAINPG 199
PRK12742 PRK12742
SDR family oxidoreductase;
100-206 7.91e-05

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 43.21  E-value: 7.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  100 VKEAG-LFGLVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQArGRVINITSVLG-RLAANGG-GYC 176
Cdd:PRK12742  70 VRKSGaLDILVVNAGIA-VFGDALELDADDIDRLFKINIHAPYHASVEAARQMPEG-GRIIIIGSVNGdRMPVAGMaAYA 147

                         90       100       110
                 ....*....|....*....|....*....|
gi 50726952  177 VSKFGLEAFSDSLRRDVAHFGIRVSIVEPG 206
Cdd:PRK12742 148 ASKSALQGMARGLARDFGPRGITINVVQPG 177
PRK07102 PRK07102
SDR family oxidoreductase;
30-213 1.51e-04

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 42.60  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   30 FVFITGCDSGFGRLLALQLDQRGFRVlasCLTPSGAEDLQRVAS-------SRLHTTLLDITD----PQSVQQAAKWVEM 98
Cdd:PRK07102   3 KILIIGATSDIARACARRYAAAGARL---YLAARDVERLERLADdlrargaVAVSTHELDILDtashAAFLDSLPALPDI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   99 HVKEAGLFG----LVNNAGVAgiigptpwltrddfQRVLNVNTMGPIGV-TLALLPLLQQARGRVINITSVLG-RLAANG 172
Cdd:PRK07102  80 VLIAVGTLGdqaaCEADPALA--------------LREFRTNFEGPIALlTLLANRFEARGSGTIVGISSVAGdRGRASN 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 50726952  173 GGYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:PRK07102 146 YVYGSAKAALTAFLSGLRNRLFKSGVHVLTVKPGFVRTPMT 186
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 31-222 2.10e-04

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 42.02  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASclTPSGAEDLQ---RVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEAGLFG 107
Cdd:PRK06077   9 VVVTGSGRGIGRAIAVRLAKEGSLVVVN--AKKRAEEMNetlKMVKENGGEGIGVLADVSTREGCETLAKATIDRYGVAD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  108 -LVNNAGVaGIIgpTPWLTRDD--FQRVLNVNTMGPIGVTLALLPLLQQArGRVINITSVLGRLAANG-GGYCVSKFGLE 183
Cdd:PRK06077  87 iLVNNAGL-GLF--SPFLNVDDklIDKHISTDFKSVIYCSQELAKEMREG-GAIVNIASVAGIRPAYGlSIYGAMKAAVI 162

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 50726952  184 AFSDSLRRDVAHfGIRVSIVEPGFFRTPVTnlESLEKTL 222
Cdd:PRK06077 163 NLTKYLALELAP-KIRVNAIAPGFVKTKLG--ESLFKVL 198
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 31-139 2.22e-04

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 42.20  E-value: 2.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAED-LQRV----ASSRLHTTLLDITDPQSVQQAAKwvEMHVKEAGL 105
Cdd:cd09809   4 IIITGANSGIGFETARSFALHGAHVILACRNMSRASAaVSRIleewHKARVEAMTLDLASLRSVQRFAE--AFKAKNSPL 81

                        90       100       110
                ....*....|....*....|....*....|....*
gi 50726952 106 FGLVNNAGVAGIigptPW-LTRDDFQRVLNVNTMG 139
Cdd:cd09809  82 HVLVCNAAVFAL----PWtLTEDGLETTFQVNHLG 112
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 25-133 3.09e-04

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 41.99  E-value: 3.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  25 PASNAFVFITGCDSGFGRLLALQLDQRGFRVLAscLT--------PSGAEDLQRVASSRLHTTLLDITDPQSVQQAAkwv 96
Cdd:cd05274 147 GGLDGTYLITGGLGGLGLLVARWLAARGARHLV--LLsrrgpaprAAARAALLRAGGARVSVVRCDVTDPAALAALL--- 221

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 50726952  97 EMHVKEAGLFGLVNNAGVAgIIGPTPWLTRDDFQRVL 133
Cdd:cd05274 222 AELAAGGPLAGVIHAAGVL-RDALLAELTPAAFAAVL 257
PRK05717 PRK05717
SDR family oxidoreductase;
25-207 3.35e-04

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 41.41  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   25 PASNAFV-FITGCDSGFGRLLALQLDQRGFRVLAScltpsgaeDLQRVASSRLHTTL--------LDITDpqSVQQAAKW 95
Cdd:PRK05717   6 PGHNGRVaLVTGAARGIGLGIAAWLIAEGWQVVLA--------DLDRERGSKVAKALgenawfiaMDVAD--EAQVAAGV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   96 VEMHVKEAGLFGLVNNAGVAGIIGPT-PWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLA-ANGG 173
Cdd:PRK05717  76 AEVLGQFGRLDALVCNAAIADPHNTTlESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHNGAIVNLASTRARQSePDTE 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 50726952  174 GYCVSKFGLEAFSDSLrrdVAHFG--IRVSIVEPGF 207
Cdd:PRK05717 156 AYAASKGGLLALTHAL---AISLGpeIRVNAVSPGW 188
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 25-223 6.13e-04

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: 40.60  E-value: 6.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  25 PASNAFVFITGCDSGFGRLLALQLDQRGFRVLAScltpsgAEDLQRV--ASSRLHTTLLDITDPQ-SVQQAAKW---VEM 98
Cdd:cd08936   7 PLANKVALVTASTDGIGLAIARRLAQDGAHVVVS------SRKQQNVdrAVATLQGEGLSVTGTVcHVGKAEDRerlVAT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  99 HVKEAGLFG-LVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLGRLAANG-GGY 175
Cdd:cd08936  81 AVNLHGGVDiLVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVpEMEKRGGGSVVIVSSVAAFHPFPGlGPY 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 50726952 176 CVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTN--------LESLEKTLQ 223
Cdd:cd08936 161 NVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSalwmdkavEESMKETLR 216
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 31-211 8.37e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 40.37  E-value: 8.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLASC-LTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEAG-LFGL 108
Cdd:PRK06198   9 ALVTGGTQGLGAAIARAFAERGAAGLVICgRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADEAFGrLDAL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  109 VNNAGV---AGIIGPTPwltrDDFQRVLNVNTMGPIGVTLALLPLLQQAR--GRVINITSvlgrLAANGG-----GYCVS 178
Cdd:PRK06198  89 VNAAGLtdrGTILDTSP----ELFDRHFAVNVRAPFFLMQEAIKLMRRRKaeGTIVNIGS----MSAHGGqpflaAYCAS 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 50726952  179 KFGLEAfsdsLRRDVAHF----GIRVSIVEPGFFRTP 211
Cdd:PRK06198 161 KGALAT----LTRNAAYAllrnRIRVNGLNIGWMATE 193
PRK07035 PRK07035
SDR family oxidoreductase;
32-210 1.37e-03

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 39.61  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   32 FITGCDSGFGRLLALQLDQRGFRVLAScltPSGAEDLQRVASS------RLHTTLLDITDPQSVQQAAKwvemHVKEAgl 105
Cdd:PRK07035  12 LVTGASRGIGEAIAKLLAQQGAHVIVS---SRKLDGCQAVADAivaaggKAEALACHIGEMEQIDALFA----HIRER-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  106 FG----LVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGV-TLALLPLLQQARGRVINITSVLGRLAANGGG-YCVSK 179
Cdd:PRK07035  83 HGrldiLVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMsVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGiYSITK 162

                        170       180       190
                 ....*....|....*....|....*....|.
gi 50726952  180 FGLEAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK07035 163 AAVISMTKAFAKECAPFGIRVNALLPGLTDT 193
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 156-206 1.85e-03

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 39.29  E-value: 1.85e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 50726952  156 GRVINITS------VLGRLAangggYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPG 206
Cdd:PRK12748 147 GRIINLTSgqslgpMPDELA-----YAATKGAIEAFTKSLAPELAEKGITVNAVNPG 198
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 31-206 1.89e-03

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 39.28  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   31 VFITGCDSGFGRLLALQLDQRGFRVLascLTPSGAEDLQRVAS------SRLHTTLLDITDPQSVQQAakwVEMHVKEAG 104
Cdd:PRK07677   4 VIITGGSSGMGKAMAKRFAEEGANVV---ITGRTKEKLEEAKLeieqfpGQVLTVQMDVRNPEDVQKM---VEQIDEKFG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  105 -LFGLVNNAgvAG-IIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPL--LQQARGRVINITSVlgrLAANGGGYCVSKF 180
Cdd:PRK07677  78 rIDALINNA--AGnFICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKYwiEKGIKGNIINMVAT---YAWDAGPGVIHSA 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 50726952  181 GLEAFSDSLRRDVA-----HFGIRVSIVEPG 206
Cdd:PRK07677 153 AAKAGVLAMTRTLAvewgrKYGIRVNAIAPG 183
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 31-139 2.03e-03

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 39.42  E-value: 2.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRG-FRVLASCLTPSGAEDLQR---VASSRLHTTLLDITDPQSVQQAAKwvEMHVKEAGLF 106
Cdd:cd09810   4 VVITGASSGLGLAAAKALARRGeWHVVMACRDFLKAEQAAQevgMPKDSYSVLHCDLASLDSVRQFVD--NFRRTGRPLD 81

                        90       100       110
                ....*....|....*....|....*....|...
gi 50726952 107 GLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMG 139
Cdd:cd09810  82 ALVCNAAVYLPTAKEPRFTADGFELTVGVNHLG 114
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 31-213 2.08e-03

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: 39.00  E-value: 2.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASS--RLHTTLLDITDPQSVQQ-AAKWVEmhvKEAGLFG 107
Cdd:cd08942   9 VLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAygECIAIPADLSSEEGIEAlVARVAE---RSDRLDV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 LVNNAGvAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQAR-----GRVINITSVLGrLAANGG---GYCVSK 179
Cdd:cd08942  86 LVNNAG-ATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAAtaenpARVINIGSIAG-IVVSGLenySYGASK 163

                       170       180       190
                ....*....|....*....|....*....|....
gi 50726952 180 FGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVT 213
Cdd:cd08942 164 AAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMT 197
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 33-211 2.11e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 38.94  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   33 ITGCDSGFGRLLALQLDQRGFRVLASCLTP-SGAEDLQRVASSRLHTtllDITDPQSVQqaakwvEMHVKEAGLFGLV-- 109
Cdd:PRK06057  12 ITGGGSGIGLATARRLAAEGATVVVGDIDPeAGKAAADEVGGLFVPT---DVTDEDAVN------ALFDTAAETYGSVdi 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  110 --NNAGVA----GIIGPTpwlTRDDFQRVLNVN-TMGPIGVTLALLPLLQQARGRVINITSVLGRLAANGG--GYCVSKF 180
Cdd:PRK06057  83 afNNAGISppedDSILNT---GLDAWQRVQDVNlTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSATSqiSYTASKG 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 50726952  181 GLEAFSDSLRRDVAHFGIRVSIVEPGFFRTP 211
Cdd:PRK06057 160 GVLAMSRELGVQFARQGIRVNALCPGPVNTP 190
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
27-230 2.50e-03

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 38.93  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   27 SNAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGA-----EDLQRVAsSRLHTTLLDITDPQSVQQAAKWVEMHVK 101
Cdd:PRK08063   3 SGKVALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAaeetaEEIEALG-RKALAVKANVGDVEKIKEMFAQIDEEFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  102 eaGLFGLVNNAGvAGIIGPTPWLTRDDFQRVLNVNTMG-PIGVTLALLPLLQQARGRVINITSvLG--RLAANGGGYCVS 178
Cdd:PRK08063  82 --RLDVFVNNAA-SGVLRPAMELEESHWDWTMNINAKAlLFCAQEAAKLMEKVGGGKIISLSS-LGsiRYLENYTTVGVS 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 50726952  179 KFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRT-PVTNLESLEKTLQACWARLP 230
Cdd:PRK08063 158 KAALEALTRYLAVELAPKGIAVNAVSGGAVDTdALKHFPNREELLEDARAKTP 210
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 31-213 3.13e-03

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: 38.63  E-value: 3.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEdlqrvassrlhttlLDITDPQSVQQA-AKWVEMHVKeaGLFGLV 109
Cdd:cd05328   2 IVITGAASGIGAATAELLEDAGHTVIGIDLREADVI--------------ADLSTPEGRAAAiADVLARCSG--VLDGLV 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 110 NNAGVAgiiGPTPwltrddFQRVLNVNTMGPIGVTLALL-PLLQQARGRVINITSVLG---------------------- 166
Cdd:cd05328  66 NCAGVG---GTTV------AGLVLKVNYFGLRALMEALLpRLRKGHGPAAVVVSSIAGagwaqdklelakalaagteara 136

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 50726952 167 -RLAANGG-----GYCVSKfglEAFSDSLRRDV----AHFGIRVSIVEPGFFRTPVT 213
Cdd:cd05328 137 vALAEHAGqpgylAYAGSK---EALTVWTRRRAatwlYGAGVRVNTVAPGPVETPIL 190
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 80-211 3.56e-03

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: 37.95  E-value: 3.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  80 LLDITDPQSVQQAAKwvemhvkEAGLF-GLVNNAGVAgIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQarGRV 158
Cdd:cd11731  36 QVDITDEASIKALFE-------KVGHFdAIVSTAGDA-EFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYLND--GGS 105

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50726952 159 INITS-VLGR---------LAANGggycvskfGLEAFSDSLRRDVAHfGIRVSIVEPGFFRTP 211
Cdd:cd11731 106 ITLTSgILAQrpipggaaaATVNG--------ALEGFVRAAAIELPR-GIRINAVSPGVVEES 159
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 31-206 4.53e-03

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: 38.10  E-value: 4.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952  31 VFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQA-AKWVEMhvkeaglFG-- 107
Cdd:cd05348   7 ALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAvARCVER-------FGkl 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952 108 --LVNNAGV----AGIIGpTPWLTRDD-FQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGrLAANGGG--YCVS 178
Cdd:cd05348  80 dcFIGNAGIwdysTSLVD-IPEEKLDEaFDELFHINVKGYILGAKAALPALYATEGSVIFTVSNAG-FYPGGGGplYTAS 157

                       170       180
                ....*....|....*....|....*...
gi 50726952 179 KFGLEAFSDSLRRDVAHFgIRVSIVEPG 206
Cdd:cd05348 158 KHAVVGLVKQLAYELAPH-IRVNGVAPG 184
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 82-210 4.60e-03

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 37.96  E-value: 4.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50726952   82 DITDPQSVQQAAKWVEmhvkeaGLFG----LVNNAG-----------VAGIIGPTPW---LTRDDFQRVLNVN---TMGP 140
Cdd:PRK08277  67 DVLDKESLEQARQQIL------EDFGpcdiLINGAGgnhpkattdneFHELIEPTKTffdLDEEGFEFVFDLNllgTLLP 140

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50726952  141 IGVtlALLPLLQQARGRVINITSV-----LGRLAAngggYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRT 210
Cdd:PRK08277 141 TQV--FAKDMVGRKGGNIINISSMnaftpLTKVPA----YSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLT 209
 
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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