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Conserved domains on  [gi|2169419209|ref|NP_001385693|]
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retinol dehydrogenase 5 [Rattus norvegicus]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 31-306 9.95e-139

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


The actual alignment was detected with superfamily member cd09805:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 281  Bit Score: 393.57  E-value: 9.95e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTP--SGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLFGL 108
Cdd:cd09805     3 VLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLWGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAAN-GGGYCVSKFGLEAFSD 187
Cdd:cd09805    83 VNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAFSD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 188 SLRRDMAPFGVQVSIVEPGFFRTPVTNLESLENTL-KACWARLPPATQAHYGEafltTYLQVQRRIMNLI---CDPDLTK 263
Cdd:cd09805   163 SLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQaKKLWERLPPEVKKDYGE----DYIDELKNKMLKYcsrASPDLSP 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2169419209 264 VTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVL 306
Cdd:cd09805   239 VIDSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 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; ...
 31-306 9.95e-139

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: 393.57  E-value: 9.95e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTP--SGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLFGL 108
Cdd:cd09805     3 VLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLWGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAAN-GGGYCVSKFGLEAFSD 187
Cdd:cd09805    83 VNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAFSD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 188 SLRRDMAPFGVQVSIVEPGFFRTPVTNLESLENTL-KACWARLPPATQAHYGEafltTYLQVQRRIMNLI---CDPDLTK 263
Cdd:cd09805   163 SLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQaKKLWERLPPEVKKDYGE----DYIDELKNKMLKYcsrASPDLSP 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2169419209 264 VTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVL 306
Cdd:cd09805   239 VIDSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
27-310 1.78e-46

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 157.34  E-value: 1.78e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  27 RDAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQ---MASSRLHTTLLDITDPQNVQQVAKWVKTRVGet 103
Cdd:COG0300     4 TGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAelrAAGARVEVVALDVTDPDAVAALAEAVLARFG-- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 104 GLFGLVNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPL-LQQARGRVVNITSVLGRIAANG-GGYCVSKFG 181
Cdd:COG0300    82 PIDVLVNNAGV-GGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLmRARGRGRIVNVSSVAGLRGLPGmAAYAASKAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNleslENTLKACWARLPPAtqahygeaflttylQVQRRIMNLIcdpdl 261
Cdd:COG0300   161 LEGFSESLRAELAPTGVRVTAVCPGPVDTPFTA----RAGAPAGRPLLSPE--------------EVARAILRAL----- 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2169419209 262 tkvtsclehaltaRHPRTRYSPGWDAKLLWLPASYLPaRVVDAVLAWVL 310
Cdd:COG0300   218 -------------ERGRAEVYVGWDARLLARLLRLLP-RLFDRLLRRAL 252
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 30-213 3.15e-40

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 139.29  E-value: 3.15e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDL---QQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLF 106
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVakeLGALGGKALFIQGDVTDRAQVKALVEQAVERLG--RLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 107 GLVNNAGVAGIiGPTPWLTQDDFQRVLNVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLEA 184
Cdd:pfam00106  80 ILVNNAGITGL-GPFSELSDEDWERVIDVNLTGVFNLTRAVLpAMIKGSGGRIVNISSVAGLVPyPGGSAYSASKAAVIG 158

                         170       180
                  ....*....|....*....|....*....
gi 2169419209 185 FSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:pfam00106 159 FTRSLALELAPHGIRVNAVAPGGVDTDMT 187
PRK06914 PRK06914
SDR family oxidoreductase;
30-300 4.36e-38

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 136.31  E-value: 4.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMA-----SSRLHTTLLDITDPQNVQQVAKWVKtRVGETG 104
Cdd:PRK06914    5 IAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQAtqlnlQQNIKVQQLDVTDQNSIHNFQLVLK-EIGRID 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LfgLVNNAGVA--GIIGPTPwltQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANG-GGYCVSKF 180
Cdd:PRK06914   84 L--LVNNAGYAngGFVEEIP---VEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGlSPYVSSKY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 181 GLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPV--TNLESLENtlkacwarlppatQAHYGEAFLTTYLQVQRRIMNLI-- 256
Cdd:PRK06914  159 ALEGFSESLRLELKPFGIDVALIEPGSYNTNIweVGKQLAEN-------------QSETTSPYKEYMKKIQKHINSGSdt 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2169419209 257 -CDPDltKVTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPAR 300
Cdd:PRK06914  226 fGNPI--DVANLIVEIAESKRPKLRYPIGKGVKLMILAKKILPWR 268
 
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; ...
 31-306 9.95e-139

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: 393.57  E-value: 9.95e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTP--SGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLFGL 108
Cdd:cd09805     3 VLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLWGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAAN-GGGYCVSKFGLEAFSD 187
Cdd:cd09805    83 VNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAFSD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 188 SLRRDMAPFGVQVSIVEPGFFRTPVTNLESLENTL-KACWARLPPATQAHYGEafltTYLQVQRRIMNLI---CDPDLTK 263
Cdd:cd09805   163 SLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQaKKLWERLPPEVKKDYGE----DYIDELKNKMLKYcsrASPDLSP 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2169419209 264 VTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVL 306
Cdd:cd09805   239 VIDSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 30-288 3.61e-60

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: 192.45  E-value: 3.61e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLV 109
Cdd:cd05374     2 VVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFG--RIDVLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 110 NNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIA-ANGGGYCVSKFGLEAFSD 187
Cdd:cd05374    80 NNAGY-GLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGsGRIVNVSSVAGLVPtPFLGPYCASKAALEALSE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 188 SLRRDMAPFGVQVSIVEPGFFRTpvtnlesleNTLKACWARLPPATQAHYGEAFLTTYLQVQRRIMNLICDPDltKVTSC 267
Cdd:cd05374   159 SLRLELAPFGIKVTIIEPGPVRT---------GFADNAAGSALEDPEISPYAPERKEIKENAAGVGSNPGDPE--KVADV 227

                         250       260
                  ....*....|....*....|.
gi 2169419209 268 LEHALTARHPRTRYSPGWDAK 288
Cdd:cd05374   228 IVKALTSESPPLRYFLGSDAL 248
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
27-310 1.78e-46

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 157.34  E-value: 1.78e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  27 RDAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQ---MASSRLHTTLLDITDPQNVQQVAKWVKTRVGet 103
Cdd:COG0300     4 TGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAelrAAGARVEVVALDVTDPDAVAALAEAVLARFG-- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 104 GLFGLVNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPL-LQQARGRVVNITSVLGRIAANG-GGYCVSKFG 181
Cdd:COG0300    82 PIDVLVNNAGV-GGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLmRARGRGRIVNVSSVAGLRGLPGmAAYAASKAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNleslENTLKACWARLPPAtqahygeaflttylQVQRRIMNLIcdpdl 261
Cdd:COG0300   161 LEGFSESLRAELAPTGVRVTAVCPGPVDTPFTA----RAGAPAGRPLLSPE--------------EVARAILRAL----- 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2169419209 262 tkvtsclehaltaRHPRTRYSPGWDAKLLWLPASYLPaRVVDAVLAWVL 310
Cdd:COG0300   218 -------------ERGRAEVYVGWDARLLARLLRLLP-RLFDRLLRRAL 252
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 25-211 3.21e-42

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: 146.10  E-value: 3.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  25 PARDAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetG 104
Cdd:COG4221     2 SDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFG--R 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LFGLVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPL-LQQARGRVVNITSVLGRIA-ANGGGYCVSKFGL 182
Cdd:COG4221    80 LDVLVNNAGVA-LLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAmRARGSGHIVNISSIAGLRPyPGGAVYAATKAAV 158

                         170       180
                  ....*....|....*....|....*....
gi 2169419209 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:COG4221   159 RGLSESLRAELRPTGIRVTVIEPGAVDTE 187
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 30-213 3.15e-40

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 139.29  E-value: 3.15e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDL---QQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLF 106
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVakeLGALGGKALFIQGDVTDRAQVKALVEQAVERLG--RLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 107 GLVNNAGVAGIiGPTPWLTQDDFQRVLNVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLEA 184
Cdd:pfam00106  80 ILVNNAGITGL-GPFSELSDEDWERVIDVNLTGVFNLTRAVLpAMIKGSGGRIVNISSVAGLVPyPGGSAYSASKAAVIG 158

                         170       180
                  ....*....|....*....|....*....
gi 2169419209 185 FSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:pfam00106 159 FTRSLALELAPHGIRVNAVAPGGVDTDMT 187
PRK06914 PRK06914
SDR family oxidoreductase;
30-300 4.36e-38

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 136.31  E-value: 4.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMA-----SSRLHTTLLDITDPQNVQQVAKWVKtRVGETG 104
Cdd:PRK06914    5 IAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQAtqlnlQQNIKVQQLDVTDQNSIHNFQLVLK-EIGRID 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LfgLVNNAGVA--GIIGPTPwltQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANG-GGYCVSKF 180
Cdd:PRK06914   84 L--LVNNAGYAngGFVEEIP---VEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGlSPYVSSKY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 181 GLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPV--TNLESLENtlkacwarlppatQAHYGEAFLTTYLQVQRRIMNLI-- 256
Cdd:PRK06914  159 ALEGFSESLRLELKPFGIDVALIEPGSYNTNIweVGKQLAEN-------------QSETTSPYKEYMKKIQKHINSGSdt 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2169419209 257 -CDPDltKVTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPAR 300
Cdd:PRK06914  226 fGNPI--DVANLIVEIAESKRPKLRYPIGKGVKLMILAKKILPWR 268
PRK06182 PRK06182
short chain dehydrogenase; Validated
 29-306 7.63e-38

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 135.47  E-value: 7.63e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  29 AVIFITGCDSGFGRLLALQLDQKGFQVLAGCltpSGAEDLQQMASSRLHTTLLDITDPQNVQQVakwVKTRVGETGLFG- 107
Cdd:PRK06182    4 KVALVTGASSGIGKATARRLAAQGYTVYGAA---RRVDKMEDLASLGVHPLSLDVTDEASIKAA---VDTIIAEEGRIDv 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAAN-GGGYCVSKFGLEAF 185
Cdd:PRK06182   78 LVNNAGY-GSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIYTPlGAWYHATKFALEGF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 186 SDSLRRDMAPFGVQVSIVEPGFFRTPVTNL--ESLENTLkacwARLPPATQAH-YGEAFLTTYLQvqrrimNLICDPDLt 262
Cdd:PRK06182  157 SDALRLEVAPFGIDVVVIEPGGIKTEWGDIaaDHLLKTS----GNGAYAEQAQaVAASMRSTYGS------GRLSDPSV- 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2169419209 263 kVTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVL 306
Cdd:PRK06182  226 -IADAISKAVTARRPKTRYAVGFGAKPLIFLRRILPDRAFDRLI 268
PRK08017 PRK08017
SDR family oxidoreductase;
31-308 1.63e-37

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 134.06  E-value: 1.63e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPsgaEDLQQMASSRLHTTLLDITDPQNVQQVAKWVkTRVGETGLFGLVN 110
Cdd:PRK08017    5 VLITGCSSGIGLEAALELKRRGYRVLAACRKP---DDVARMNSLGFTGILLDLDDPESVERAADEV-IALTDNRLYGLFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 111 NAGVaGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIAANG-GGYCVSKFGLEAFSDS 188
Cdd:PRK08017   81 NAGF-GVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLpAMLPHGEGRIVMTSSVMGLISTPGrGAYAASKYALEAWSDA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 189 LRRDMAPFGVQVSIVEPGFFRTPVTN-------LESLENTLKACWARLPPatqahygEAFLTTylqvqrrimnlicdpdl 261
Cdd:PRK08017  160 LRMELRHSGIKVSLIEPGPIRTRFTDnvnqtqsDKPVENPGIAARFTLGP-------EAVVPK----------------- 215

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2169419209 262 tkvtscLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVLAW 308
Cdd:PRK08017  216 ------LRHALESPKPKLRYPVTLVTHAVMVLKRLLPGRMMDKILRG 256
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 30-210 1.70e-36

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 131.96  E-value: 1.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgLV 109
Cdd:PRK06180    6 TWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFGPIDV--LV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 110 NNAGVA--GIIGPTPwltQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANG-GGYCVSKFGLEAF 185
Cdd:PRK06180   84 NNAGYGheGAIEESP---LAEMRRQFEVNVFGAVAMTKAVLPGMRARRrGHIVNITSMGGLITMPGiGYYCGSKFALEGI 160

                         170       180
                  ....*....|....*....|....*
gi 2169419209 186 SDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK06180  161 SESLAKEVAPFGIHVTAVEPGSFRT 185
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 31-211 2.89e-34

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: 125.09  E-value: 2.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASS--RLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGL 108
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEALggNAVAVQADVSDEEDVEALVEEALEEFG--RLDIL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VNNAGVAGIiGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIA-ANGGGYCVSKFGLEAFS 186
Cdd:cd05233    79 VNNAGIARP-GPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGgGRIVNISSVAGLRPlPGQAAYAASKAALEGLT 157

                         170       180
                  ....*....|....*....|....*
gi 2169419209 187 DSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd05233   158 RSLALELAPYGIRVNAVAPGLVDTP 182
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 30-213 1.15e-33

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: 123.74  E-value: 1.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQM---ASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLF 106
Cdd:COG1028     8 VALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAElraAGGRALAVAADVTDEAAVEALVAAAVAAFG--RLD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 107 GLVNNAGVAGIiGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPL-LQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLEA 184
Cdd:COG1028    86 ILVNNAGITPP-GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHmRERGGGRIVNISSIAGLRGsPGQAAYAASKAAVVG 164

                         170       180
                  ....*....|....*....|....*....
gi 2169419209 185 FSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:COG1028   165 LTRSLALELAPRGIRVNAVAPGPIDTPMT 193
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 30-306 3.15e-33

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 123.47  E-value: 3.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMassrlhTTL-LDITDPQNVQQVAKWVKTRVGETGLfgL 108
Cdd:PRK06179    6 VALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIPGV------ELLeLDVTDDASVQAAVDEVIARAGRIDV--L 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANGGG-YCVSKFGLEAFS 186
Cdd:PRK06179   78 VNNAGV-GLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGsGRIINISSVLGFLPAPYMAlYAASKHAVEGYS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 187 DSLRRDMAPFGVQVSIVEPGFFRtpvTNLEslENTLKacwarlPPATQAHYGEAFlTTYLQVQRRIMNLICDPDLtkVTS 266
Cdd:PRK06179  157 ESLDHEVRQFGIRVSLVEPAYTK---TNFD--ANAPE------PDSPLAEYDRER-AVVSKAVAKAVKKADAPEV--VAD 222

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2169419209 267 CLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVL 306
Cdd:PRK06179  223 TVVKAALGPWPKMRYTAGGQASLLSKLRRFMPAGAVDKSL 262
PRK05693 PRK05693
SDR family oxidoreductase;
30-206 1.17e-31

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 119.13  E-value: 1.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAgclTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLV 109
Cdd:PRK05693    3 VVLITGCSSGIGRALADAFKAAGYEVWA---TARKAEDVEALAAAGFTAVQLDVNDGAALARLAEELEAEHG--GLDVLI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 110 NNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAAN-GGGYCVSKFGLEAFSDS 188
Cdd:PRK05693   78 NNAGY-GAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTPfAGAYCASKAAVHALSDA 156

                         170
                  ....*....|....*...
gi 2169419209 189 LRRDMAPFGVQVSIVEPG 206
Cdd:PRK05693  157 LRLELAPFGVQVMEVQPG 174
PRK05993 PRK05993
SDR family oxidoreductase;
31-308 4.92e-30

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 115.12  E-value: 4.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPsgaEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGeTGLFGLVN 110
Cdd:PRK05993    7 ILITGCSSGIGAYCARALQSDGWRVFATCRKE---EDVAALEAEGLEAFQLDYAEPESIAALVAQVLELSG-GRLDALFN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 111 NaGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIAAN-GGGYCVSKFGLEAFSDS 188
Cdd:PRK05993   83 N-GAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIpVMRKQGQGRIVQCSSILGLVPMKyRGAYNASKFAIEGLSLT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 189 LRRDMAPFGVQVSIVEPGFFRTPVTNlesleNTLKACWARLPPATQAHYGEaflttYLQVQRRIMN------LICDPDlt 262
Cdd:PRK05993  162 LRMELQGSGIHVSLIEPGPIETRFRA-----NALAAFKRWIDIENSVHRAA-----YQQQMARLEGggsksrFKLGPE-- 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2169419209 263 KVTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVLAW 308
Cdd:PRK05993  230 AVYAVLLHALTAPRPRPHYRVTTPAKQGALLKRLLPARWLYRLLRK 275
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 31-210 9.28e-30

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: 113.16  E-value: 9.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQL-DQKGFQVLAGCLTPSGAEDLQQMAS--SRLHTTLLDITDPqnVQQVAKWVKTRVGETGLFG 107
Cdd:cd05325     1 VLITGASRGIGLELVRQLlARGNNTVIATCRDPSAATELAALGAshSRLHILELDVTDE--IAESAEAVAERLGDAGLDV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVT-LALLPLLQQARGRVVNITSVLGRIAANGGG----YCVSKFGL 182
Cdd:cd05325    79 LINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTqAFLPLLLKGARAKIINISSRVGSIGDNTSGgwysYRASKAAL 158

                         170       180
                  ....*....|....*....|....*...
gi 2169419209 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:cd05325   159 NMLTKSLAVELKRDGITVVSLHPGWVRT 186
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 30-213 1.47e-29

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 112.72  E-value: 1.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQM---ASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLf 106
Cdd:cd05339     1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNvrkAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTI- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 107 gLVNNAGVAgiIGPTPW-LTQDDFQRVLNVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIAANGGG-YCVSKFGLE 183
Cdd:cd05339    80 -LINNAGVV--SGKKLLeLPDEEIEKTFEVNTLAHFWTTKAFLpDMLERNHGHIVTIASVAGLISPAGLAdYCASKAAAV 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2169419209 184 AFSDSLRRDMAPF---GVQVSIVEPGFFRTPVT 213
Cdd:cd05339   157 GFHESLRLELKAYgkpGIKTTLVCPYFINTGMF 189
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 30-213 1.12e-28

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 110.67  E-value: 1.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPS-GAEDLQQMASS---RLHTTLLDITDPQNVQQVAKWVKTRVGetGL 105
Cdd:PRK05557    7 VALVTGASRGIGRAIAERLAAQGANVVINYASSEaGAEALVAEIGAlggKALAVQGDVSDAESVERAVDEAKAEFG--GV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 FGLVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRI-AANGGGYCVSKFGLE 183
Cdd:PRK05557   85 DILVNNAGIT-RDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRsGRIINISSVVGLMgNPGQANYAASKAGVI 163

                         170       180       190
                  ....*....|....*....|....*....|
gi 2169419209 184 AFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK05557  164 GFTKSLARELASRGITVNAVAPGFIETDMT 193
PRK09291 PRK09291
SDR family oxidoreductase;
31-210 5.61e-28

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 108.93  E-value: 5.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSR---LHTTLLDITDPQNVQQVAKW---Vktrvgetg 104
Cdd:PRK09291    5 ILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRglaLRVEKLDLTDAIDRAQAAEWdvdV-------- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 lfgLVNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPL-LQQARGRVVNITSVLGRIA-ANGGGYCVSKFGL 182
Cdd:PRK09291   77 ---LLNNAGI-GEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKmVARGKGKVVFTSSMAGLITgPFTGAYCASKHAL 152

                         170       180
                  ....*....|....*....|....*...
gi 2169419209 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK09291  153 EAIAEAMHAELKPFGIQVATVNPGPYLT 180
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 27-210 1.92e-27

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: 107.67  E-value: 1.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  27 RDAVIFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASSRL-------HTTLLDITDPQNVQQVAKWVKTR 99
Cdd:cd05332     2 QGKVVIITGASSGIGEELAYHLARLGARLV---LSARREERLEEVKSECLelgapspHVVPLDMSDLEDAEQVVEEALKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 100 VGetGLFGLVNNAGVAGiigPTPW--LTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANG-GGY 175
Cdd:cd05332    79 FG--GLDILINNAGISM---RSLFhdTSIDVDRKIMEVNYFGPVALTKAALPHLIERSqGSIVVVSSIAGKIGVPFrTAY 153

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2169419209 176 CVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:cd05332   154 AASKHALQGFFDSLRAELSEPNISVTVVCPGLIDT 188
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 30-281 3.68e-26

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


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 104.08  E-value: 3.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQL---DQKGFQVLAGCLTPSGAEDLQQMASSRLHTTL----LDITDPQNVQQVAKWVKTRVGE 102
Cdd:cd09806     2 VVLITGCSSGIGLHLAVRLasdPSKRFKVYATMRDLKKKGRLWEAAGALAGGTLetlqLDVCDSKSVAAAVERVTERHVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 103 TglfgLVNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGR--IAANGGgYCVSK 179
Cdd:cd09806    82 V----LVCNAGV-GLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGsGRILVTSSVGGLqgLPFNDV-YCASK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 180 FGLEAFSDSLRRDMAPFGVQVSIVEPGffrtPV-TNLES--LENTLKACWARLPPATQAHYGEAFLTTYLQVQRRIMNli 256
Cdd:cd09806   156 FALEGLCESLAVQLLPFNVHLSLIECG----PVhTAFMEkvLGSPEEVLDRTADDITTFHFFYQYLAHSKQVFREAAQ-- 229

                         250       260
                  ....*....|....*....|....*
gi 2169419209 257 cDPDltKVTSCLEHALTARHPRTRY 281
Cdd:cd09806   230 -NPE--EVAEVFLTAIRAPKPPLRY 251
PRK06482 PRK06482
SDR family oxidoreductase;
32-210 1.01e-25

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 103.27  E-value: 1.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  32 FITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVakwVKTRVGETGLFG-LVN 110
Cdd:PRK06482    6 FITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARYGDRLWVLQLDVTDSAAVRAV---VDRAFAALGRIDvVVS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 111 NAGVaGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANGGG-YCVSKFGLEAFSDS 188
Cdd:PRK06482   83 NAGY-GLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGgGRIVQVSSEGGQIAYPGFSlYHATKWGIEGFVEA 161

                         170       180
                  ....*....|....*....|..
gi 2169419209 189 LRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK06482  162 VAQEVAPFGIEFTIVEPGPART 183
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 30-224 1.01e-24

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: 99.36  E-value: 1.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAeDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLV 109
Cdd:cd08932     2 VALVTGASRGIGIEIARALARDGYRVSLGLRNPEDL-AALSASGGDVEAVPYDARDPEDARALVDALRDRFG--RIDVLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 110 NNAGvagIIGPTPWL--TQDDFQRVLNVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIAANG-GGYCVSKFGLEAF 185
Cdd:cd08932    79 HNAG---IGRPTTLRegSDAELEAHFSINVIAPAELTRALLpALREAGSGRVVFLNSLSGKRVLAGnAGYSASKFALRAL 155

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2169419209 186 SDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLENTLKA 224
Cdd:cd08932   156 AHALRQEGWDHGVRVSAVCPGFVDTPMAQGLTLVGAFPP 194
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 30-229 3.11e-24

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: 98.76  E-value: 3.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVlagCLTPSGAEDLQQMAS------SRLHTTLLDITDPQnvqQVAKWVKTRVGET 103
Cdd:cd08934     5 VALVTGASSGIGEATARALAAEGAAV---AIAARRVDRLEALADeleaegGKALVLELDVTDEQ---QVDAAVERTVEAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 104 G-LFGLVNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIAA-NGGGYCVSKF 180
Cdd:cd08934    79 GrLDILVNNAGI-MLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALpHHLLRNKGTIVNISSVAGRVAVrNSAVYNATKF 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2169419209 181 GLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLENTLKACWARL 229
Cdd:cd08934   158 GVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHITHTITKEAYEERI 206
PRK12826 PRK12826
SDR family oxidoreductase;
21-211 4.38e-24

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 98.45  E-value: 4.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  21 RQSLPARdaVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAE---DLQQMASSRLHTTLLDITDPQNVQQVAKWVK 97
Cdd:PRK12826    1 TRDLEGR--VALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAataELVEAAGGKARARQVDVRDRAALKAAVAAGV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  98 TRVGetGLFGLVNNAGVAGIiGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANGG--G 174
Cdd:PRK12826   79 EDFG--RLDILVANAGIFPL-TPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGgGRIVLTSSVAGPRVGYPGlaH 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2169419209 175 YCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK12826  156 YAASKAGLVGFTRALALELAARNITVNSVHPGGVDTP 192
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 30-213 1.29e-23

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: 96.85  E-value: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGA---EDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLF 106
Cdd:cd05333     2 VALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAaetVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFG--PVD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 107 GLVNNAGVagiigpT-----PWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGrIAANGG--GYCVS 178
Cdd:cd05333    80 ILVNNAGI------TrdnllMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRsGRIINISSVVG-LIGNPGqaNYAAS 152

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2169419209 179 KFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:cd05333   153 KAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMT 187
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 30-210 1.72e-23

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 97.42  E-value: 1.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNV-QQVAKWVKtRVGEtgLFGL 108
Cdd:PRK08263    5 VWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVfAAVETAVE-HFGR--LDIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VNNAGvAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIA-ANGGGYCVSKFGLEAFS 186
Cdd:PRK08263   82 VNNAG-YGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRsGHIIQISSIGGISAfPMSGIYHASKWALEGMS 160

                         170       180
                  ....*....|....*....|....
gi 2169419209 187 DSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK08263  161 EALAQEVAEFGIKVTLVEPGGYST 184
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 37-211 4.40e-23

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


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 95.19  E-value: 4.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  37 DSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASsRLHTTLL--DITDPQNVQQVAKWVKTRVGetGLFGLVNNAGV 114
Cdd:pfam13561   5 ESGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAE-ELGAAVLpcDVTDEEQVEALVAAAVEKFG--RLDILVNNAGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 115 AG-IIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQaRGRVVNITSVLGRIA-ANGGGYCVSKFGLEAFSDSLRRD 192
Cdd:pfam13561  82 APkLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKE-GGSIVNLSSIGAERVvPNYNAYGAAKAALEALTRYLAVE 160

                         170
                  ....*....|....*....
gi 2169419209 193 MAPFGVQVSIVEPGFFRTP 211
Cdd:pfam13561 161 LGPRGIRVNAISPGPIKTL 179
PRK05650 PRK05650
SDR family oxidoreductase;
31-217 5.87e-23

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 95.88  E-value: 5.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQV-LAGCLTPSGAEDLQQM--ASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:PRK05650    3 VMITGAASGLGRAIALRWAREGWRLaLADVNEEGGEETLKLLreAGGDGFYQRCDVRDYSQLTALAQACEEKWG--GIDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNAGVA--GIIGPtpwLTQDDFQRVLNVNTLGPI-GVTLALLPLLQQARGRVVNITSVLGRIAANG-GGYCVSKFGLE 183
Cdd:PRK05650   81 IVNNAGVAsgGFFEE---LSLEDWDWQIAINLMGVVkGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAmSSYNVAKAGVV 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2169419209 184 AFSDSLRRDMAPFGVQVSIVEPGFFRtpvTNLES 217
Cdd:PRK05650  158 ALSETLLVELADDEIGVHVVCPSFFQ---TNLLD 188
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
30-213 1.52e-22

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 94.07  E-value: 1.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQ---MASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLF 106
Cdd:PRK05653    7 TALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAelrAAGGEARVLVFDVSDEAAVRALIEAAVEAFG--ALD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 107 GLVNNAGVAGIiGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANGGG-YCVSKFGLEA 184
Cdd:PRK05653   85 ILVNNAGITRD-ALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARyGRIVNISSVSGVTGNPGQTnYSAAKAGVIG 163

                         170       180
                  ....*....|....*....|....*....
gi 2169419209 185 FSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK05653  164 FTKALALELASRGITVNAVAPGFIDTDMT 192
PRK07832 PRK07832
SDR family oxidoreductase;
32-214 1.64e-22

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 94.72  E-value: 1.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  32 FITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASS--------RLHTTLlDITDPQNVQQVAKWVKTRVGET 103
Cdd:PRK07832    4 FVTGAASGIGRATALRLAAQGAELF---LTDRDADGLAQTVADaralggtvPEHRAL-DISDYDAVAAFAADIHAAHGSM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 104 GLfgLVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGV--TLALLPLLQQARGRVVNITSVLGRIAAN-GGGYCVSKF 180
Cdd:PRK07832   80 DV--VMNIAGIS-AWGTVDRLTHEQWRRMVDVNLMGPIHVieTFVPPMVAAGRGGHLVNVSSAAGLVALPwHAAYSASKF 156

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2169419209 181 GLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN 214
Cdd:PRK07832  157 GLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVN 190
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 27-305 1.72e-22

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 94.62  E-value: 1.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  27 RDAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDlQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLf 106
Cdd:PRK07825    4 RGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKE-TAAELGLVVGGPLDVTDPASFAAFLDAVEADLGPIDV- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 107 gLVNNAGVAGIigpTPWLTQDD--FQRVLNVNTLGPI-GVTLALLPLLQQARGRVVNITSVLGRIAANGGG-YCVSKFGL 182
Cdd:PRK07825   82 -LVNNAGVMPV---GPFLDEPDavTRRILDVNVYGVIlGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMAtYCASKHAV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRtpvTNLESLENTLKAcwarLPPATQAhygeaflttylQVQRRIMNLIcdpdlt 262
Cdd:PRK07825  158 VGFTDAARLELRGTGVHVSVVLPSFVN---TELIAGTGGAKG----FKNVEPE-----------DVAAAIVGTV------ 213

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2169419209 263 kvtsclehaltaRHPRTRYS-PGWDAKLLWLpASYLPARVVDAV 305
Cdd:PRK07825  214 ------------AKPRPEVRvPRALGPLAQA-QRLLPRRVREAL 244
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 32-206 6.70e-22

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: 91.80  E-value: 6.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  32 FITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLVNN 111
Cdd:cd08929     4 LVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFG--GLDALVNN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 112 AGVaGIIGPTPWLTQDDFQR-VLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANGG-GYCVSKFGLEAFSDSL 189
Cdd:cd08929    82 AGV-GVMKPVEELTPEEWRLvLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGaAYNASKFGLLGLSEAA 160

                         170
                  ....*....|....*..
gi 2169419209 190 RRDMAPFGVQVSIVEPG 206
Cdd:cd08929   161 MLDLREANIRVVNVMPG 177
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 27-213 9.76e-22

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: 91.70  E-value: 9.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  27 RDAVIFITGCDSGFGR-LLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQ---QVAKWVKTrvge 102
Cdd:cd05354     2 KDKTVLVTGANRGIGKaFVESLLAHGAKKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKaaaAQAKDVDV---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 103 tglfgLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIA-ANGGGYCVSKF 180
Cdd:cd05354    78 -----VINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFApVLKANGGGAIVNLNSVASLKNfPAMGTYSASKS 152

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2169419209 181 GLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:cd05354   153 AAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMA 185
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 28-254 1.52e-21

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: 91.16  E-value: 1.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPS----GAEDLQQMA---SSRLHTTLLDITDPQNVQQVakwVKTRV 100
Cdd:cd08939     1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESkleeAVEEIEAEAnasGQKVSYISADLSDYEEVEQA---FAQAV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 101 GETGLFG-LVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANG-GGYCV 177
Cdd:cd08939    78 EKGGPPDlVVNCAGIS-IPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRpGHIVFVSSQAALVGIYGySAYCP 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2169419209 178 SKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP-VTNleslENTLKacwarlPPATQAHYGEAFLTTYLQVQRRIMN 254
Cdd:cd08939   157 SKFALRGLAESLRQELKPYNIRVSVVYPPDTDTPgFEE----ENKTK------PEETKAIEGSSGPITPEEAARIIVK 224
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 22-211 1.70e-21

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 91.47  E-value: 1.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  22 QSLPARdaVIFITGCDSGFGRLLALQLDQKGFQVLAGCltPSGAEDLQQMASS------RLHTTLLDITDPQNVQQVAKW 95
Cdd:PRK12825    2 GSLMGR--VALVTGAARGLGRAIALRLARAGADVVVHY--RSDEEAAEELVEAvealgrRAQAVQADVTDKAALEAAVAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  96 VKTRVGetGLFGLVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVlgriAANGG- 173
Cdd:PRK12825   78 AVERFG--RIDILVNNAGIF-EDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRgGRIVNISSV----AGLPGw 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2169419209 174 ----GYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK12825  151 pgrsNYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTD 192
PRK08264 PRK08264
SDR family oxidoreductase;
28-213 1.87e-21

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 91.10  E-value: 1.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKG-FQVLAGCLTPSGAEDLQqmasSRLHTTLLDITDPQNVQQVAKwvktRVGETGLf 106
Cdd:PRK08264    6 GKVVLVTGANRGIGRAFVEQLLARGaAKVYAAARDPESVTDLG----PRVVPLQLDVTDPASVAAAAE----AASDVTI- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 107 gLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLA-LLPLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLEA 184
Cdd:PRK08264   77 -LVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAfAPVLAANGGGAIVNVLSVLSWVNfPNLGTYSASKAAAWS 155

                         170       180
                  ....*....|....*....|....*....
gi 2169419209 185 FSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK08264  156 LTQALRAELAPQGTRVLGVHPGPIDTDMA 184
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 31-206 3.85e-21

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: 90.42  E-value: 3.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMAS-------SRLHTTLLDITDPQNVQQV-----AKWVKT 98
Cdd:cd05346     3 VLITGASSGIGEATARRFAKAGAKLI---LTGRRAERLQELADelgakfpVKVLPLQLDVSDRESIEAAlenlpEEFRDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  99 RVgetglfgLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIA-ANGGGYC 176
Cdd:cd05346    80 DI-------LVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILpIMIARNQGHIINLGSIAGRYPyAGGNVYC 152

                         170       180       190
                  ....*....|....*....|....*....|
gi 2169419209 177 VSKFGLEAFSDSLRRDMAPFGVQVSIVEPG 206
Cdd:cd05346   153 ATKAAVRQFSLNLRKDLIGTGIRVTNIEPG 182
PRK06181 PRK06181
SDR family oxidoreductase;
30-210 8.19e-21

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 89.65  E-value: 8.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTL---LDITDPQNVQQVAKWVKTRVGetGLF 106
Cdd:PRK06181    3 VVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALvvpTDVSDAEACERLIEAAVARFG--GID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 107 GLVNNAGVagiigpTPWLTQDD------FQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANG-GGYCVSK 179
Cdd:PRK06181   81 ILVNNAGI------TMWSRFDEltdlsvFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTrSGYAASK 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2169419209 180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK06181  155 HALHGFFDSLRIELADDGVAVTVVCPGFVAT 185
PRK07326 PRK07326
SDR family oxidoreductase;
27-206 1.37e-20

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 88.53  E-value: 1.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  27 RDAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASS--RLHTTLLDITDPQNVQQVAKWVKTRVGetG 104
Cdd:PRK07326    5 KGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNkgNVLGLAADVRDEADVQRAVDAIVAAFG--G 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LFGLVNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLE 183
Cdd:PRK07326   83 LDVLIANAGV-GHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGTNFfAGGAAYNASKFGLV 161

                         170       180
                  ....*....|....*....|...
gi 2169419209 184 AFSDSLRRDMAPFGVQVSIVEPG 206
Cdd:PRK07326  162 GFSEAAMLDLRQYGIKVSTIMPG 184
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 30-213 4.22e-20

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 87.33  E-value: 4.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQ---MASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLF 106
Cdd:PRK12939    9 RALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAaleAAGGRAHAIAADLADPASVQRFFDAAAAALG--GLD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 107 GLVNNAGVAGIIGPTPwLTQDDFQRVLNVNTLGPIGVTLALLPL-LQQARGRVVNI-TSVLGRIAANGGGYCVSKFGLEA 184
Cdd:PRK12939   87 GLVNNAGITNSKSATE-LDIDTWDAVMNVNVRGTFLMLRAALPHlRDSGRGRIVNLaSDTALWGAPKLGAYVASKGAVIG 165

                         170       180
                  ....*....|....*....|....*....
gi 2169419209 185 FSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK12939  166 MTRSLARELGGRGITVNAIAPGLTATEAT 194
PRK09072 PRK09072
SDR family oxidoreductase;
28-205 1.78e-19

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 86.15  E-value: 1.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQ--MASSRLHTTLLDITDPQNVQQVAKWVKTRvgeTGL 105
Cdd:PRK09072    5 DKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAArlPYPGRHRWVVADLTSEAGREAVLARAREM---GGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 FGLVNNAGVAGIIgptpWLTQ---DDFQRVLNVNTLGPIGVTLALLPL-LQQARGRVVNITSVLGRIAANG-GGYCVSKF 180
Cdd:PRK09072   82 NVLINNAGVNHFA----LLEDqdpEAIERLLALNLTAPMQLTRALLPLlRAQPSAMVVNVGSTFGSIGYPGyASYCASKF 157

                         170       180
                  ....*....|....*....|....*
gi 2169419209 181 GLEAFSDSLRRDMAPFGVQVSIVEP 205
Cdd:PRK09072  158 ALRGFSEALRRELADTGVRVLYLAP 182
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 21-308 2.46e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 86.90  E-value: 2.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  21 RQSLPARDAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTL---LDITDPQNVQQVAKWVK 97
Cdd:PRK07109    1 MMLKPIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALavvADVADAEAVQAAADRAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  98 TRVGetGLFGLVNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPI-GVTLALLPLLQQARGRVVNITSVLGRI-----AAn 171
Cdd:PRK07109   81 EELG--PIDTWVNNAMV-TVFGPFEDVTPEEFRRVTEVTYLGVVhGTLAALRHMRPRDRGAIIQVGSALAYRsiplqSA- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 172 gggYCVSKFGLEAFSDSLR----RDMAPfgVQVSIVEPGFFRTPVTNleslentlkacWARlppatqahygeafltTYLQ 247
Cdd:PRK07109  157 ---YCAAKHAIRGFTDSLRcellHDGSP--VSVTMVQPPAVNTPQFD-----------WAR---------------SRLP 205

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2169419209 248 VQRRIMNLICDPDLtkVTSCLEHAltARHPRTRYSPGWDAKLLWLpASYLPARVVDAVLAW 308
Cdd:PRK07109  206 VEPQPVPPIYQPEV--VADAILYA--AEHPRRELWVGGPAKAAIL-GNRLAPGLLDRYLAR 261
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 29-211 3.10e-19

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: 84.74  E-value: 3.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  29 AVIFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMAS--SRLHTTLL----DITDPQNVQQVAKWVKTRVGE 102
Cdd:cd05360     1 QVVVITGASSGIGRATALAFAERGAKVV---LAARSAEALHELARevRELGGEAIavvaDVADAAQVERAADTAVERFGR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 103 TGLFglVNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPI-GVTLALLPLLQQARGRVVNITSVLG-RIAANGGGYCVSKF 180
Cdd:cd05360    78 IDTW--VNNAGV-AVFGRFEDVTPEEFRRVFDVNYLGHVyGTLAALPHLRRRGGGALINVGSLLGyRSAPLQAAYSASKH 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2169419209 181 GLEAFSDSLRRDMAPFG--VQVSIVEPGFFRTP 211
Cdd:cd05360   155 AVRGFTESLRAELAHDGapISVTLVQPTAMNTP 187
PRK06484 PRK06484
short chain dehydrogenase; Validated
 25-214 5.71e-19

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 87.21  E-value: 5.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  25 PARDA-VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGET 103
Cdd:PRK06484  265 LAESPrVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRL 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 104 GLfgLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIgVTLALLPLLQQARGRVVNITSVLGRIAANG-GGYCVSKFGL 182
Cdd:PRK06484  345 DV--LVNNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAF-ACARAAARLMSQGGVIVNLGSIASLLALPPrNAYCASKAAV 421

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2169419209 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN 214
Cdd:PRK06484  422 TMLSRSLACEWAPAGIRVNTVAPGYIETPAVL 453
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 30-210 1.02e-18

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: 83.06  E-value: 1.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGF-QVLAGCLTP-SGAEDLQQMASSRLHTTL--LDITDPQNVQQVAKWVKTRVGetGL 105
Cdd:cd05324     2 VALVTGANRGIGFEIVRQLAKSGPgTVILTARDVeRGQAAVEKLRAEGLSVRFhqLDVTDDASIEAAADFVEEKYG--GL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 FGLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIAAnggGYCVSKFGLEA 184
Cdd:cd05324    80 DILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLpLLKKSPAGRIVNVSSGLGSLTS---AYGVSKAALNA 156

                         170       180
                  ....*....|....*....|....*.
gi 2169419209 185 FSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:cd05324   157 LTRILAKELKETGIKVNACCPGWVKT 182
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 31-200 1.05e-18

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: 83.67  E-value: 1.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQVLAGcltpsG--AEDLQQMASSR--LHTTLLDITDPQNVQQVAKWVKTRVGEtgLF 106
Cdd:COG3967     8 ILITGGTSGIGLALAKRLHARGNTVIIT-----GrrEEKLEEAAAANpgLHTIVLDVADPASIAALAEQVTAEFPD--LN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 107 GLVNNAGVAGII----GPTPWltqDDFQRVLNVNTLGPIGVTLALLPL-LQQARGRVVNITSVLGRI-AANGGGYCVSKF 180
Cdd:COG3967    81 VLINNAGIMRAEdlldEAEDL---ADAEREITTNLLGPIRLTAAFLPHlKAQPEAAIVNVSSGLAFVpLAVTPTYSATKA 157

                         170       180
                  ....*....|....*....|
gi 2169419209 181 GLEAFSDSLRRDMAPFGVQV 200
Cdd:COG3967   158 ALHSYTQSLRHQLKDTSVKV 177
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 29-211 1.10e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 83.61  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  29 AVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSrlHTTLLDITDPQnvqqvakWVKTRVGETGLF-G 107
Cdd:PRK07060   10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGC--EPLRLDVGDDA-------AIRAALAAAGAFdG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQ--ARGRVVNITSvlgrIAANGG-----GYCVSKF 180
Cdd:PRK07060   81 LVNCAGIA-SLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAagRGGSIVNVSS----QAALVGlpdhlAYCASKA 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2169419209 181 GLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK07060  156 ALDAITRVLCVELGPHGIRVNSVNPTVTLTP 186
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 31-214 2.39e-18

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 82.38  E-value: 2.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQV-LAG----CLTPSGAEDLQQMASSRLHTtlLDITDPQNVQQVAKWVKTRVGetGL 105
Cdd:cd05350     1 VLITGASSGIGRALAREFAKAGYNVaLAArrtdRLDELKAELLNPNPSVEVEI--LDVTDEERNQLVIAELEAELG--GL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 FGLVNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPI-GVTLALLPLLQQARGRVVNITSVLG-RIAANGGGYCVSKFGLE 183
Cdd:cd05350    77 DLVIINAGV-GKGTSLGDLSFKAFRETIDTNLLGAAaILEAALPQFRAKGRGHLVLISSVAAlRGLPGAAAYSASKAALS 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2169419209 184 AFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN 214
Cdd:cd05350   156 SLAESLRYDVKKRGIRVTVINPGFIDTPLTA 186
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 28-214 3.95e-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: 82.07  E-value: 3.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVlagCLTPSGAEDLQQMASSRLHTTLL---------DITDPQNVQQVakwVKT 98
Cdd:cd05364     3 GKVAIITGSSSGIGAGTAILFARLGARL---ALTGRDAERLEETRQSCLQAGVSekkillvvaDLTEEEGQDRI---IST 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  99 RVGETG-LFGLVNNAGVAGIIGPTPwLTQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANGG-GYC 176
Cdd:cd05364    77 TLAKFGrLDILVNNAGILAKGGGED-QDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGRSFPGVlYYC 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2169419209 177 VSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN 214
Cdd:cd05364   156 ISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHR 193
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
33-211 5.29e-18

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 81.74  E-value: 5.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGA----EDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgL 108
Cdd:PRK12824    7 VTGAKRGIGSAIARELLNDGYRVIATYFSGNDCakdwFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGPVDI--L 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VNNAGVA--GIIGPtpwLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANGG-GYCVSKFGLEA 184
Cdd:PRK12824   85 VNNAGITrdSVFKR---MSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGyGRIINISSVNGLKGQFGQtNYSAAKAGMIG 161

                         170       180
                  ....*....|....*....|....*..
gi 2169419209 185 FSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK12824  162 FTKALASEGARYGITVNCIAPGYIATP 188
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 29-213 1.77e-17

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: 80.09  E-value: 1.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  29 AVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASS---RLHTTLLDITDPQNVQQVAKWVKTRVGETGL 105
Cdd:cd05347     6 KVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKegvEATAFTCDVSDEEAIKAAVEAIEEDFGKIDI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 fgLVNNAGvagIIGPTPWL--TQDDFQRVLNVNTLGPIGVTLALLPL-LQQARGRVVNITSV---LGRIaaNGGGYCVSK 179
Cdd:cd05347    86 --LVNNAG---IIRRHPAEefPEAEWRDVIDVNLNGVFFVSQAVARHmIKQGHGKIINICSLlseLGGP--PVPAYAASK 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2169419209 180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:cd05347   159 GGVAGLTKALATEWARHGIQVNAIAPGYFATEMT 192
PRK06484 PRK06484
short chain dehydrogenase; Validated
 26-216 3.24e-17

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 81.82  E-value: 3.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  26 ARDAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGL 105
Cdd:PRK06484    3 AQSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 fgLVNNagvAGIIGPTPWLTQD----DFQRVLNVNTLGPIGVTLALLPLLQQAR--GRVVNITSVLGRIAANG-GGYCVS 178
Cdd:PRK06484   83 --LVNN---AGVTDPTMTATLDttleEFARLQAINLTGAYLVAREALRLMIEQGhgAAIVNVASGAGLVALPKrTAYSAS 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2169419209 179 KFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP-VTNLE 216
Cdd:PRK06484  158 KAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQmVAELE 196
PRK12743 PRK12743
SDR family oxidoreductase;
30-216 3.36e-17

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 79.69  E-value: 3.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVlaGCLTPSGAEDLQQMAS------SRLHTTLLDITDPQNVQQVAKWVKTRVGet 103
Cdd:PRK12743    4 VAIVTASDSGIGKACALLLAQQGFDI--GITWHSDEEGAKETAEevrshgVRAEIRQLDLSDLPEGAQALDKLIQRLG-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 104 GLFGLVNNAGvAGIIGPTPWLTQDDFQRVLNVNTLGPI--GVTLALLPLLQQARGRVVNITSV---LGRIAAngGGYCVS 178
Cdd:PRK12743   80 RIDVLVNNAG-AMTKAPFLDMDFDEWRKIFTVDVDGAFlcSQIAARHMVKQGQGGRIINITSVhehTPLPGA--SAYTAA 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2169419209 179 KFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLE 216
Cdd:PRK12743  157 KHALGGLTKAMALELVEHGILVNAVAPGAIATPMNGMD 194
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 31-235 4.36e-17

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: 78.65  E-value: 4.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQ-QMASSRLHTTLLDITDPQNVQQVAKWVKTRVGEtGLFGLV 109
Cdd:cd08931     3 IFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAaELGAENVVAGALDVTDRAAWAAALADFAAATGG-RLDALF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 110 NNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPI-GVTLALLPLLQQARGRVVNITSVLG-----RIAAngggYCVSKFGLE 183
Cdd:cd08931    82 NNAGV-GRGGPFEDVPLAAHDRMVDINVKGVLnGAYAALPYLKATPGARVINTASSSAiygqpDLAV----YSATKFAVR 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2169419209 184 AFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLENTLKACWARLPPATQA 235
Cdd:cd08931   157 GLTEALDVEWARHGIRVADVWPWFVDTPILTKGETGAAPKKGLGRVLPVSDV 208
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 30-211 1.03e-16

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: 78.19  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQV-LAGCLTPSGAEDLQQMASS---RLHTTLLDITDPQNVQQVAKWVKTRVGetGL 105
Cdd:cd05366     4 VAIITGAAQGIGRAIAERLAADGFNIvLADLNLEEAAKSTIQEISEagyNAVAVGADVTDKDDVEALIDQAVEKFG--SF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 FGLVNNAGVAGIigpTPWL--TQDDFQRVLNVNTLGPI-GVTLALLPLLQQAR-GRVVNITSVLGRIA-ANGGGYCVSKF 180
Cdd:cd05366    82 DVMVNNAGIAPI---TPLLtiTEEDLKKVYAVNVFGVLfGIQAAARQFKKLGHgGKIINASSIAGVQGfPNLGAYSASKF 158

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2169419209 181 GLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd05366   159 AVRGLTQTAAQELAPKGITVNAYAPGIVKTE 189
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 22-211 1.32e-16

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 78.18  E-value: 1.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  22 QSLPARdaVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQ-QMASSRLHTTLLDITDPQNVQQVAKWVKTRV 100
Cdd:PRK12829    7 KPLDGL--RVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAaRLPGAKVTATVADVADPAQVERVFDTAVERF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 101 GetGLFGLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPI-GVTLALLPLLQQARGRVV-NITSVLGRIAANGG-GYCV 177
Cdd:PRK12829   85 G--GLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFyFARAAVPLLKASGHGGVIiALSSVAGRLGYPGRtPYAA 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2169419209 178 SKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK12829  163 SKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGP 196
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 28-246 2.24e-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: 77.04  E-value: 2.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASS---RLHTTLLDITDPQNVQQVAKWVKTRVGetG 104
Cdd:cd05341     5 GKVAIVTGGARGLGLAHARLLVAEGAKVV---LSDILDEEGQAAAAElgdAARFFHLDVTDEDGWTAVVDTAREAFG--R 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LFGLVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGP-IGVTLALLPLLQQARGRVVNITSVLGRI-AANGGGYCVSKFGL 182
Cdd:cd05341    80 LDVLVNNAGIL-TGGTVETTTLEEWRRLLDINLTGVfLGTRAVIPPMKEAGGGSIINMSSIEGLVgDPALAAYNASKGAV 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2169419209 183 EAFSDSLRRDMAP--FGVQVSIVEPGFFRTPVTnleslENTLKACWAR--LPPATQAHYGE----AFLTTYL 246
Cdd:cd05341   159 RGLTKSAALECATqgYGIRVNSVHPGYIYTPMT-----DELLIAQGEMgnYPNTPMGRAGEpdeiAYAVVYL 225
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 27-223 4.49e-16

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: 76.41  E-value: 4.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  27 RDAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAED-----LQQMASSRLHTTLLDITDpqnVQQVAKWVKTRVG 101
Cdd:cd05330     2 KDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAakaalLEIAPDAEVLLIKADVSD---EAQVEAYVDATVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 102 ETG-LFGLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGP-IGVTLALLPLLQQARGRVVNITSVLG-RIAANGGGYCVS 178
Cdd:cd05330    79 QFGrIDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVfYGLEKVLKVMREQGSGMIVNTASVGGiRGVGNQSGYAAA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2169419209 179 KFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVtnlesLENTLK 223
Cdd:cd05330   159 KHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPM-----VEGSLK 198
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 31-211 6.27e-16

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


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 75.97  E-value: 6.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLtpsgAEDLQQMASSRLHTTLLDITDPQNV-QQVAKWVKtrvgETGLFG-L 108
Cdd:cd05331     1 VIVTGAAQGIGRAVARHLLQAGATVIALDL----PFVLLLEYGDPLRLTPLDVADAAAVrEVCSRLLA----EHGPIDaL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITS-VLGRIAANGGGYCVSKFGLEAFS 186
Cdd:cd05331    73 VNCAGVL-RPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRtGAIVTVASnAAHVPRISMAAYGASKAALASLS 151

                         170       180
                  ....*....|....*....|....*
gi 2169419209 187 DSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd05331   152 KCLGLELAPYGVRCNVVSPGSTDTA 176
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 30-205 9.28e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 75.47  E-value: 9.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgLV 109
Cdd:PRK06841   17 VAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRIDI--LV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 110 NNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQA-RGRVVNITSVLGRIAANGG-GYCVSKFGLEAFSD 187
Cdd:PRK06841   95 NSAGVA-LLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAgGGKIVNLASQAGVVALERHvAYCASKAGVVGMTK 173

                         170
                  ....*....|....*...
gi 2169419209 188 SLRRDMAPFGVQVSIVEP 205
Cdd:PRK06841  174 VLALEWGPYGITVNAISP 191
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 30-211 9.55e-16

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 75.31  E-value: 9.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQqmassrLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgLV 109
Cdd:PRK08220   10 TVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDYP------FATFVLDVSDAAAVAQVCQRLLAETGPLDV--LV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 110 NnagVAGII--GPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVlgriAANG-----GGYCVSKFG 181
Cdd:PRK08220   82 N---AAGILrmGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRsGAIVTVGSN----AAHVprigmAAYGASKAA 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 2169419209 182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK08220  155 LTSLAKCVGLELAPYGVRCNVVSPGSTDTD 184
PRK07454 PRK07454
SDR family oxidoreductase;
32-217 1.00e-15

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 75.00  E-value: 1.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  32 FITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMAS------SRLHTTLLDITDPQNVQQVAKWVKTRVGETGL 105
Cdd:PRK07454   10 LITGASSGIGKATALAFAKAGWDLA---LVARSQDALEALAAelrstgVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 fgLVNNAGVA--GIIGPTPWltqDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIA-ANGGGYCVSKFG 181
Cdd:PRK07454   87 --LINNAGMAytGPLLEMPL---SDWQWVIQLNLTSVFQCCSAVLPGMRARGgGLIINVSSIAARNAfPQWGAYCVSKAA 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2169419209 182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLES 217
Cdd:PRK07454  162 LAAFTKCLAEEERSHGIRVCTITLGAVNTPLWDTET 197
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 28-211 1.12e-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: 75.39  E-value: 1.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQmASSRLHTTLL-------DITDPQNVQQVAKWVKTRV 100
Cdd:cd05344     1 GKVALVTAASSGIGLAIARALAREGARVA---ICARNRENLER-AASELRAGGAgvlavvaDLTDPEDIDRLVEKAGDAF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 101 GetGLFGLVNNAGvAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGR------IAANgg 173
Cdd:cd05344    77 G--RVDILVNNAG-GPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLTVKepepnlVLSN-- 151

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2169419209 174 gycVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd05344   152 ---VARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTE 186
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 30-194 1.18e-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: 75.02  E-value: 1.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSgAEDLQQMAS-----SRLHTTLLDITDPQNVQQVAKWVKTRVGEtg 104
Cdd:cd05367     1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARS-EEPLQELKEelrpgLRVTTVKADLSDAAGVEQLLEAIRKLDGE-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LFGLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLAL--LPLLQQARGRVVNITSVLGRIAANG-GGYCVSKFG 181
Cdd:cd05367    78 RDLLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLlrAFKKRGLKKTVVNVSSGAAVNPFKGwGLYCSSKAA 157

                         170
                  ....*....|...
gi 2169419209 182 LeafsDSLRRDMA 194
Cdd:cd05367   158 R----DMFFRVLA 166
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 30-265 1.30e-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: 75.34  E-value: 1.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAED-----LQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGEtg 104
Cdd:cd05327     3 VVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEaaaeiKKETGNAKVEVIQLDLSSLASVRQFAEEFLARFPR-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LFGLVNNAGVAGiigPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIA---------ANGGG 174
Cdd:cd05327    81 LDILINNAGIMA---PPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASApSRIVNVSSIAHRAGpidfndldlENNKE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 175 ------YCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLENTLKACWARL---PPATQAhygeafltty 245
Cdd:cd05327   158 yspykaYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNGSFFLLYKLLRPFlkkSPEQGA---------- 227

                         250       260
                  ....*....|....*....|
gi 2169419209 246 lqvqRRIMNLICDPDLTKVT 265
Cdd:cd05327   228 ----QTALYAATSPELEGVS 243
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 28-207 2.43e-15

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 74.22  E-value: 2.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTL---LDITDPQNVQQVAKWVKTRVGetG 104
Cdd:PRK07890    5 GKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALavpTDITDEDQCANLVALALERFG--R 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LFGLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITS-VLGRIAANGGGYCVSKFGLE 183
Cdd:PRK07890   83 VDALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMINSmVLRHSQPKYGAYKMAKGALL 162

                         170       180
                  ....*....|....*....|....
gi 2169419209 184 AFSDSLRRDMAPFGVQVSIVEPGF 207
Cdd:PRK07890  163 AASQSLATELGPQGIRVNSVAPGY 186
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 25-231 3.40e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 74.62  E-value: 3.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  25 PARDAVIFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMA-----SSRLHTTLLDITDPQNVQQVAKWVKTR 99
Cdd:PRK05872    6 SLAGKVVVVTGAARGIGAELARRLHARGAKLA---LVDLEEAELAALAaelggDDRVLTVVADVTDLAAMQAAAEEAVER 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 100 VGetGLFGLVNNAGVAGiigPTPWLTQD--DFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSvLGRIAANGGG--Y 175
Cdd:PRK05872   83 FG--GIDVVVANAGIAS---GGSVAQVDpdAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSS-LAAFAAAPGMaaY 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2169419209 176 CVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN--LESLEnTLKACWARLPP 231
Cdd:PRK05872  157 CASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDLVRdaDADLP-AFRELRARLPW 213
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 30-211 4.39e-15

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 73.29  E-value: 4.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQV-LAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGL 108
Cdd:PRK12828    9 VVAITGGFGGLGRATAAWLAARGARVaLIGRGAAPLSQTLPGVPADALRIGGIDLVDPQAARRAVDEVNRQFG--RLDAL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VNNAGVagiigpTPW-----LTQDDFQRVLNVNTLGPI-GVTLALLPLLQQARGRVVNITSVLGRIAANG-GGYCVSKFG 181
Cdd:PRK12828   87 VNIAGA------FVWgtiadGDADTWDRMYGVNVKTTLnASKAALPALTASGGGRIVNIGAGAALKAGPGmGAYAAAKAG 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 2169419209 182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK12828  161 VARLTEALAAELLDRGITVNAVLPSIIDTP 190
PRK08219 PRK08219
SDR family oxidoreductase;
33-211 7.00e-15

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 72.66  E-value: 7.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  33 ITGCDSGFGRLLALQLdQKGFQVLAGCLTPSGAEDLQQmASSRLHTTLLDITDPQNVQqvakWVKTRVGEtgLFGLVNNA 112
Cdd:PRK08219    8 ITGASRGIGAAIAREL-APTHTLLLGGRPAERLDELAA-ELPGATPFPVDLTDPEAIA----AAVEQLGR--LDVLVHNA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 113 GVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLEAFSDSLRR 191
Cdd:PRK08219   80 GVA-DLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRAnPGWGSYAASKFALRALADALRE 158

                         170       180
                  ....*....|....*....|
gi 2169419209 192 DMAPfGVQVSIVEPGFFRTP 211
Cdd:PRK08219  159 EEPG-NVRVTSVHPGRTDTD 177
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 31-206 9.21e-15

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: 72.34  E-value: 9.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSrLHTTLLDITDPQNVQQVAKWVKTRVGEtgLFGLVN 110
Cdd:cd05370     8 VLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN-IHTIVLDVGDAESVEALAEALLSEYPN--LDILIN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 111 NAGVA---GIIGPTPWLtqDDFQRVLNVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLEAF 185
Cdd:cd05370    85 NAGIQrpiDLRDPASDL--DKADTEIDTNLIGPIRLIKAFLpHLKKQPEATIVNVSSGLAFVPmAANPVYCATKAALHSY 162

                         170       180
                  ....*....|....*....|..
gi 2169419209 186 SDSLRRDMAPFGVQV-SIVEPG 206
Cdd:cd05370   163 TLALRHQLKDTGVEVvEIVPPA 184
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 29-211 1.07e-14

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 72.45  E-value: 1.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  29 AVIFITGCDSGFGRLLALQLDQKGFQVLAGCL-TPSGAEDLQQMAS------SRLHTTLLDITDPQNVQQVakwVKTRVG 101
Cdd:PRK12827    7 RRVLITGGSGGLGRAIAVRLAADGADVIVLDIhPMRGRAEADAVAAgieaagGKALGLAFDVRDFAATRAA---LDAGVE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 102 ETG-LFGLVNNAGVAGIiGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR--GRVVNITSVLGRIAANGG-GYCV 177
Cdd:PRK12827   84 EFGrLDILVNNAGIATD-AAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARrgGRIVNIASVAGVRGNRGQvNYAA 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2169419209 178 SKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK12827  163 SKAGLIGLTKTLANELAPRGITVNAVAPGAINTP 196
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 30-206 1.08e-14

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 72.47  E-value: 1.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPS-GAEDLQ---QMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGL 105
Cdd:PRK12937    7 VAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAaAADELVaeiEAAGGRAIAVQADVADAAAVTRLFDAAETAFG--RI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 FGLVNNAGVAGIiGPTPWLTQDDFQRVLNVNTLGPIgVTLALLPLLQQARGRVVNI-TSVLGRIAANGGGYCVSKFGLEA 184
Cdd:PRK12937   85 DVLVNNAGVMPL-GTIADFDLEDFDRTIATNLRGAF-VVLREAARHLGQGGRIINLsTSVIALPLPGYGPYAASKAAVEG 162

                         170       180
                  ....*....|....*....|..
gi 2169419209 185 FSDSLRRDMAPFGVQVSIVEPG 206
Cdd:PRK12937  163 LVHVLANELRGRGITVNAVAPG 184
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 28-211 1.23e-14

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 72.32  E-value: 1.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQmASSRLHTTLLDITDPQNVQQVAKWVKTRVGEtgLFG 107
Cdd:cd05371     2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAK-LGDNCRFVPVDVTSEKDVKAALALAKAKFGR--LDI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNAGVA------GIIGPTPwLTQDDFQRVLNVNTLGPIGVTLALLPLLQQA-------RGRVVNITSVlgriAANGG- 173
Cdd:cd05371    79 VVNCAGIAvaaktyNKKGQQP-HSLELFQRVINVNLIGTFNVIRLAAGAMGKNepdqggeRGVIINTASV----AAFEGq 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2169419209 174 ----GYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd05371   154 igqaAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTP 195
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 30-223 1.56e-14

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: 72.03  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLT-PSGAEDLQQMASSRLHTTLL---DITDPQNVQQVAKWVKTRVGetGL 105
Cdd:cd05358     5 VALVTGASSGIGKAIAIRLATAGANVVVNYRSkEDAAEEVVEEIKAVGGKAIAvqaDVSKEEDVVALFQSAIKEFG--TL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 FGLVNNAGVAGIIgPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR--GRVVNITSVLGRIAANG-GGYCVSKFGL 182
Cdd:cd05358    83 DILVNNAGLQGDA-SSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKikGKIINMSSVHEKIPWPGhVNYAASKGGV 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2169419209 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT-----NLESLENTLK 223
Cdd:cd05358   162 KMMTKTLAQEYAPKGIRVNAIAPGAINTPINaeawdDPEQRADLLS 207
PRK05855 PRK05855
SDR family oxidoreductase;
25-214 2.86e-14

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 73.09  E-value: 2.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  25 PARDAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAE---DLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVG 101
Cdd:PRK05855  312 PFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAErtaELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHG 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 102 ETGLfgLVNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPI-------------GVTlallpllqqarGRVVNITSVlgri 168
Cdd:PRK05855  392 VPDI--VVNNAGI-GMAGGFLDTSAEDWDRVLDVNLWGVIhgcrlfgrqmverGTG-----------GHIVNVASA---- 453

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2169419209 169 AANG-----GGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN 214
Cdd:PRK05855  454 AAYApsrslPAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVA 504
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 30-210 4.61e-14

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 70.64  E-value: 4.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQV-LAGCLTPSGAEDLQQMASSRLHTTLL---DITDPQNVQQVAKWVKTRVGetGL 105
Cdd:PRK05565    7 VAIVTGASGGIGRAIAELLAKEGAKVvIAYDINEEAAQELLEEIKEEGGDAIAvkaDVSSEEDVENLVEQIVEKFG--KI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 FGLVNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRI-AANGGGYCVSKFGLE 183
Cdd:PRK05565   85 DILVNNAGI-SNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKsGVIVNISSIWGLIgASCEVLYSASKGAVN 163

                         170       180
                  ....*....|....*....|....*..
gi 2169419209 184 AFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK05565  164 AFTKALAKELAPSGIRVNAVAPGAIDT 190
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 30-206 6.05e-14

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 70.17  E-value: 6.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQV-----AKWVKTRVgetg 104
Cdd:PRK10538    2 IVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMlaslpAEWRNIDV---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 lfgLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIAANGGG-YCVSKFGL 182
Cdd:PRK10538   78 ---LVNNAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLpGMVERNHGHIINIGSTAGSWPYAGGNvYGATKAFV 154

                         170       180
                  ....*....|....*....|....
gi 2169419209 183 EAFSDSLRRDMAPFGVQVSIVEPG 206
Cdd:PRK10538  155 RQFSLNLRTDLHGTAVRVTDIEPG 178
FabG-like PRK07231
SDR family oxidoreductase;
30-211 7.09e-14

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 70.24  E-value: 7.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVlagCLTPSGAEDLQQMAS-----SRLHTTLLDITDPQNVQQVAKWVKTRVGetG 104
Cdd:PRK07231    7 VAIVTGASSGIGEGIARRFAAEGARV---VVTDRNEEAAERVAAeilagGRAIAVAADVSDEADVEAAVAAALERFG--S 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LFGLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLG-RIAANGGGYCVSKFGL 182
Cdd:PRK07231   82 VDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGgGAIVNVASTAGlRPRPGLGWYNASKGAV 161

                         170       180
                  ....*....|....*....|....*....
gi 2169419209 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK07231  162 ITLTKALAAELGPDKIRVNAVAPVVVETG 190
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 22-205 7.43e-14

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 69.72  E-value: 7.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  22 QSLPARDAviFITGCDSGFGRLLALQLDQKGFQVlagCLTPSGAEDLQQMASS------RLHTTLLDITDPQNVQQVAKW 95
Cdd:PRK07666    3 QSLQGKNA--LITGAGRGIGRAVAIALAKEGVNV---GLLARTEENLKAVAEEveaygvKVVIATADVSDYEEVTAAIEQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  96 VKTRVGETGLfgLVNNAGVAGIiGPTPWLTQDDFQRVLNVNTLGPIGVTLALL-PLLQQARGRVVNITSVLG-RIAANGG 173
Cdd:PRK07666   78 LKNELGSIDI--LINNAGISKF-GKFLELDPAEWEKIIQVNLMGVYYATRAVLpSMIERQSGDIINISSTAGqKGAAVTS 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2169419209 174 GYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEP 205
Cdd:PRK07666  155 AYSASKFGVLGLTESLMQEVRKHNIRVTALTP 186
PRK08267 PRK08267
SDR family oxidoreductase;
31-313 7.74e-14

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 69.97  E-value: 7.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDL-QQMASSRLHTTLLDITDPQNVQQ-VAKWVKTRVGetGLFGL 108
Cdd:PRK08267    4 IFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALaAELGAGNAWTGALDVTDRAAWDAaLADFAAATGG--RLDVL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPI-GVTLALLPLLQQARGRVVNITSVLG-----RIAAngggYCVSKFGL 182
Cdd:PRK08267   82 FNNAGI-LRGGPFEDIPLEAHDRVIDINVKGVLnGAHAALPYLKATPGARVINTSSASAiygqpGLAV----YSATKFAV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLEN---TLKACWARLPPATQAhygeaflttylqvqrrimnlicdp 259
Cdd:PRK08267  157 RGLTEALDLEWRRHGIRVADVMPLFVDTAMLDGTSNEVdagSTKRLGVRLTPEDVA------------------------ 212

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2169419209 260 dltkvtsclEHALTARHPRTR--YSPGWDAKLLWLPASYLPARVVDAVLAWvLPRP 313
Cdd:PRK08267  213 ---------EAVWAAVQHPTRlhWPVGKQAKLLAFLARLSPGFVRRLINKS-LARP 258
PRK06124 PRK06124
SDR family oxidoreductase;
19-228 1.10e-13

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 69.74  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  19 RDRQSLPARDAVIfiTGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASS------RLHTTLLDITDPQNVQQV 92
Cdd:PRK06124    4 LQRFSLAGQVALV--TGSARGLGFEIARALAGAGAHVL---VNGRNAATLEAAVAAlraaggAAEALAFDIADEEAVAAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  93 AKWVKTRVGetGLFGLVNNAGvAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIA-A 170
Cdd:PRK06124   79 FARIDAEHG--RLDILVNNVG-ARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGyGRIIAITSIAGQVArA 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2169419209 171 NGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPvTNLESLENTLKACWAR 228
Cdd:PRK06124  156 GDAVYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATE-TNAAMAADPAVGPWLA 212
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
30-211 1.20e-13

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 69.37  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLFG-L 108
Cdd:PRK08643    4 VALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDLNvV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VNNAGVAGIIgPTPWLTQDDFQRVLNVNTLGPI-GVTLALLPLLQQARG-RVVNITSVLGRIA-ANGGGYCVSKFGLEAF 185
Cdd:PRK08643   84 VNNAGVAPTT-PIETITEEQFDKVYNINVGGVIwGIQAAQEAFKKLGHGgKIINATSQAGVVGnPELAVYSSTKFAVRGL 162

                         170       180
                  ....*....|....*....|....*.
gi 2169419209 186 SDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK08643  163 TQTAARDLASEGITVNAYAPGIVKTP 188
PRK06101 PRK06101
SDR family oxidoreductase;
30-219 1.53e-13

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 69.13  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQmASSRLHTTLLDITDPQNVQQVAKWVKTrVGETGLFglv 109
Cdd:PRK06101    3 AVLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDELHT-QSANIFTLAFDVTDHPGTKAALSQLPF-IPELWIF--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 110 nNAGVAGIIgptpwltqDD-------FQRVLNVNTLGPIGVTLALLPLLQqaRG-RVVNITSVLGRIA-ANGGGYCVSKF 180
Cdd:PRK06101   78 -NAGDCEYM--------DDgkvdatlMARVFNVNVLGVANCIEGIQPHLS--CGhRVVIVGSIASELAlPRAEAYGASKA 146

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2169419209 181 GLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLE 219
Cdd:PRK06101  147 AVAYFARTLQLDLRPKGIEVVTVFPGFVATPLTDKNTFA 185
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 30-213 1.73e-13

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: 69.03  E-value: 1.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTL----LDITDPQNVQQVAKWVKTRVGetGL 105
Cdd:cd05337     3 VAIVTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAGRRAiyfqADIGELSDHEALLDQAWEDFG--RL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 FGLVNNAGVAGII-GPTPWLTQDDFQRVLNVNTLGPIGVTLALL-------PLLQQARGRVVNITSV-LGRIAANGGGYC 176
Cdd:cd05337    81 DCLVNNAGIAVRPrGDLLDLTEDSFDRLIAINLRGPFFLTQAVArrmveqpDRFDGPHRSIIFVTSInAYLVSPNRGEYC 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2169419209 177 VSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:cd05337   161 ISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMT 197
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
30-210 2.17e-13

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 68.50  E-value: 2.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGC--LTPSGAEDLQQMAS--SRLHTTLLDITDPQNVQQVAKWVKTRVGETGL 105
Cdd:PRK12938    5 IAYVTGGMGGIGTSICQRLHKDGFKVVAGCgpNSPRRVKWLEDQKAlgFDFIASEGNVGDWDSTKAAFDKVKAEVGEIDV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 fgLVNNAGVAGIIGPTPwLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANG-GGYCVSKFGLE 183
Cdd:PRK12938   85 --LVNNAGITRDVVFRK-MTREDWTAVIDTNLTSLFNVTKQVIDGMVERGwGRIINISSVNGQKGQFGqTNYSTAKAGIH 161

                         170       180
                  ....*....|....*....|....*..
gi 2169419209 184 AFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK12938  162 GFTMSLAQEVATKGVTVNTVSPGYIGT 188
PRK07023 PRK07023
SDR family oxidoreductase;
29-206 2.18e-13

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 68.50  E-value: 2.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  29 AVIFI-TGCDSGFGRLLALQLDQKGFQVLagCLTPSGAEDLQQMASSRLHTTLLDITDPQnvqQVAKWVKTRVGETGLFG 107
Cdd:PRK07023    1 AVRAIvTGHSRGLGAALAEQLLQPGIAVL--GVARSRHPSLAAAAGERLAEVELDLSDAA---AAAAWLAGDLLAAFVDG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 -----LVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLA-LLPLLQQARGRVVNITSVLGRIAANG-GGYCVSKF 180
Cdd:PRK07023   76 asrvlLINNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAAlAQAASDAAERRILHISSGAARNAYAGwSVYCATKA 155

                         170       180
                  ....*....|....*....|....*.
gi 2169419209 181 GLEAFSDSLRRDmAPFGVQVSIVEPG 206
Cdd:PRK07023  156 ALDHHARAVALD-ANRALRIVSLAPG 180
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 30-211 2.92e-13

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: 68.07  E-value: 2.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPS-GAEDLQ---QMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGL 105
Cdd:cd05362     5 VALVTGASRGIGRAIAKRLARDGASVVVNYASSKaAAEEVVaeiEAAGGKAIAVQADVSDPSQVARLFDAAEKAFG--GV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 FGLVNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQArGRVVNITSVLGRIAA-NGGGYCVSKFGLEA 184
Cdd:cd05362    83 DILVNNAGV-MLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDG-GRIINISSSLTAAYTpNYGAYAGSKAAVEA 160

                         170       180
                  ....*....|....*....|....*..
gi 2169419209 185 FSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd05362   161 FTRVLAKELGGRGITVNAVAPGPVDTD 187
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 27-205 3.88e-13

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: 67.88  E-value: 3.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  27 RDAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPsgaEDLQQMASSRLH--TTLLDITDpqnvqqvakWVKTR--VGE 102
Cdd:cd05351     6 AGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQ---ADLDSLVRECPGiePVCVDLSD---------WDATEeaLGS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 103 TGLF-GLVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPL--LQQARGRVVNITSVLGRIA-ANGGGYCVS 178
Cdd:cd05351    74 VGPVdLLVNNAAVA-ILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGmiARGVPGSIVNVSSQASQRAlTNHTVYCST 152

                         170       180
                  ....*....|....*....|....*..
gi 2169419209 179 KFGLEAFSDSLRRDMAPFGVQVSIVEP 205
Cdd:cd05351   153 KAALDMLTKVMALELGPHKIRVNSVNP 179
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 30-282 3.89e-13

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: 67.95  E-value: 3.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLaGCltPSGAEDLQ------QMASSRLHTTLLDITDPQNVQQVAKWVKTRVGET 103
Cdd:cd08945     5 VALVTGATSGIGLAIARRLGKEGLRVF-VC--ARGEEGLAttvkelREAGVEADGRTCDVRSVPEIEALVAAAVARYGPI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 104 GLfgLVNNAGVAGIiGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPL---LQQARGRVVNITSVLGRIAA-NGGGYCVSK 179
Cdd:cd08945    82 DV--LVNNAGRSGG-GATAELADELWLDVVETNLTGVFRVTKEVLKAggmLERGTGRIINIASTGGKQGVvHAAPYSASK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPvtnleslentlkacwarLPPATQAHYGEAFLTTYLQVQRRImnlicdp 259
Cdd:cd08945   159 HGVVGFTKALGLELARTGITVNAVCPGFVETP-----------------MAASVREHYADIWEVSTEEAFDRI------- 214

                         250       260
                  ....*....|....*....|...
gi 2169419209 260 dltkvtsclehalTARHPRTRYS 282
Cdd:cd08945   215 -------------TARVPLGRYV 224
PRK07024 PRK07024
SDR family oxidoreductase;
31-213 4.64e-13

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 67.65  E-value: 4.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASS-----RLHTTLLDITDPQNVQQVAKWVKTRVGETGL 105
Cdd:PRK07024    5 VFITGASSGIGQALAREYARQGATLG---LVARRTDALQAFAARlpkaaRVSVYAADVRDADALAAAAADFIAAHGLPDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 fgLVNNAGVA-GIigptpwLTQ-----DDFQRVLNVNTLGPIGV-TLALLPLLQQARGRVVNITSVLG-RIAANGGGYCV 177
Cdd:PRK07024   82 --VIANAGISvGT------LTEeredlAVFREVMDTNYFGMVATfQPFIAPMRAARRGTLVGIASVAGvRGLPGAGAYSA 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2169419209 178 SKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK07024  154 SKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPMT 189
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 30-262 4.81e-13

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: 67.71  E-value: 4.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLT--PSGAEDLQQMASS---RLHTTllDITDPQnvQQVAKWVKTRVGETG 104
Cdd:cd05323     2 VAIITGGASGIGLATAKLLLKKGAKVAILDRNenPGAAAELQAINPKvkaTFVQC--DVTSWE--QLAAAFKKAIEKFGR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LFGLVNNAGvagiIGPTPWLTQD-----DFQRVLNVNTLGPI-GVTLALLPLLQQAR---GRVVNITSVLGRIAANGGG- 174
Cdd:cd05323    78 VDILINNAG----ILDEKSYLFAgklppPWEKTIDVNLTGVInTTYLALHYMDKNKGgkgGVIVNIGSVAGLYPAPQFPv 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 175 YCVSKFGLEAFSDSLRRDM-APFGVQVSIVEPGFFRTPVtnlesLENTLKACWARLPPATqahygeafLTTYLQVQRRIM 253
Cdd:cd05323   154 YSASKHGVVGFTRSLADLLeYKTGVRVNAICPGFTNTPL-----LPDLVAKEAEMLPSAP--------TQSPEVVAKAIV 220


                  ....*....
gi 2169419209 254 NLICDPDLT 262
Cdd:cd05323   221 YLIEDDEKN 229
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-224 1.11e-12

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 66.52  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  27 RDAVIFITGCDSGFGRLLALQLDQKGFQvLAgcLTPSGAEDLQQ------MASSRLHTTLLDITDPQNVQQVAKWVKTRV 100
Cdd:PRK08217    4 KDKVIVITGGAQGLGRAMAEYLAQKGAK-LA--LIDLNQEKLEEavaecgALGTEVRGYAANVTDEEDVEATFAQIAEDF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 101 GetGLFGLVNNAGVA----------GIIGPTPWLTQddFQRVLNVNTLGPI--GVTLALLPLLQQARGRVVNITSVlGRi 168
Cdd:PRK08217   81 G--QLNGLINNAGILrdgllvkakdGKVTSKMSLEQ--FQSVIDVNLTGVFlcGREAAAKMIESGSKGVIINISSI-AR- 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2169419209 169 AANGG--GYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT---NLESLENTLKA 224
Cdd:PRK08217  155 AGNMGqtNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTaamKPEALERLEKM 215
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 24-214 1.55e-12

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 66.09  E-value: 1.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  24 LPARDAVIfiTGCDSGFGRLLALQLDQKGFQVlagCLTPSGAEDLQQMASS---RLHTTLLDITDPQNVQQVAKWVKTRV 100
Cdd:PRK12936    4 LSGRKALV--TGASGGIGEEIARLLHAQGAIV---GLHGTRVEKLEALAAElgeRVKIFPANLSDRDEVKALGQKAEADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 101 GetGLFGLVNNAGVAGIiGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGrIAANGG--GYCV 177
Cdd:PRK12936   79 E--GVDILVNNAGITKD-GLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRyGRIINITSVVG-VTGNPGqaNYCA 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2169419209 178 SKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN 214
Cdd:PRK12936  155 SKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTG 191
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 27-211 1.79e-12

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: 65.68  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  27 RDAVIFITGCDSGFGRLLALQLDQKGFQV-LAGCLTPSGAEDLQQMASSRLHTTLLDITD-----PQNVQQVAKWVKTRV 100
Cdd:cd05340     3 NDRIILVTGASDGIGREAALTYARYGATViLLGRNEEKLRQVADHINEEGGRQPQWFILDlltctSENCQQLAQRIAVNY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 101 GEtgLFGLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRI-AANGGGYCVS 178
Cdd:cd05340    83 PR--LDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQgRANWGAYAVS 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2169419209 179 KFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd05340   161 KFATEGL*QVLADEYQQRNLRVNCINPGGTRTA 193
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
31-210 2.43e-12

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 65.86  E-value: 2.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQVLagCLTPSGAEDLQQMAS---SRLHTTLLDITDPQNVQQVAKWVKTRVGETGLFG 107
Cdd:PRK06924    4 VIITGTSQGLGEAIANQLLEKGTHVI--SISRTENKELTKLAEqynSNLTFHSLDLQDVHELETNFNEILSSIQEDNVSS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 --LVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQARG--RVVNITSVLGRIAANG-GGYCVSKFGL 182
Cdd:PRK06924   82 ihLINNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKVdkRVINISSGAAKNPYFGwSAYCSSKAGL 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 2169419209 183 EAFSDS--LRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK06924  162 DMFTQTvaTEQEEEEYPVKIVAFSPGVMDT 191
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
30-212 2.69e-12

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 65.59  E-value: 2.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTT--LLDITDPQNVQQVAKWVKTRVGETGLfg 107
Cdd:PRK08226    8 TALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADELCGRGHRCTavVADVRDPASVAAAIKRAKEKEGRIDI-- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIAANGG--GYCVSKFGLEA 184
Cdd:PRK08226   86 LVNNAGVC-RLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLpEMIARKDGRIVMMSSVTGDMVADPGetAYALTKAAIVG 164

                         170       180
                  ....*....|....*....|....*...
gi 2169419209 185 FSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:PRK08226  165 LTKSLAVEYAQSGIRVNAICPGYVRTPM 192
PRK06949 PRK06949
SDR family oxidoreductase;
30-210 2.83e-12

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 65.55  E-value: 2.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASS------RLHTTLLDITDPQNVQQVAKWVKTRVGET 103
Cdd:PRK06949   11 VALVTGASSGLGARFAQVLAQAGAKVV---LASRRVERLKELRAEieaeggAAHVVSLDVTDYQSIKAAVAHAETEAGTI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 104 GLfgLVNNAGVAG---IIGPTPwltqDDFQRVLNVNTLGPIGVTL---------ALLPLLQQARGRVVNITSVLG-RIAA 170
Cdd:PRK06949   88 DI--LVNNSGVSTtqkLVDVTP----ADFDFVFDTNTRGAFFVAQevakrmiarAKGAGNTKPGGRIINIASVAGlRVLP 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2169419209 171 NGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK06949  162 QIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDT 201
PRK06194 PRK06194
hypothetical protein; Provisional
 22-210 4.53e-12

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 65.42  E-value: 4.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  22 QSLPARDAVIfiTGCDSGFGRLLALQLDQKGFQ-VLAgcltpsgaeDLQQMASSRLHTTL-----------LDITDPQNV 89
Cdd:PRK06194    2 KDFAGKVAVI--TGAASGFGLAFARIGAALGMKlVLA---------DVQQDALDRAVAELraqgaevlgvrTDVSDAAQV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  90 QQVAKWVKTRVGETGLfgLVNNAGVAGiiGPTPWL-TQDDFQRVLNVNTLGPI-GVTL------ALLPLLQQARGRVVNI 161
Cdd:PRK06194   71 EALADAALERFGAVHL--LFNNAGVGA--GGLVWEnSLADWEWVLGVNLWGVIhGVRAftplmlAAAEKDPAYEGHIVNT 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2169419209 162 TSVLGRIAA-NGGGYCVSKFGLEAFSDSLRRDMAPFGVQV--SIVEPGFFRT 210
Cdd:PRK06194  147 ASMAGLLAPpAMGIYNVSKHAVVSLTETLYQDLSLVTDQVgaSVLCPYFVPT 198
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 33-224 7.39e-12

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 64.20  E-value: 7.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  33 ITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQmASSRLH----TTLL---DITDPQNVQQVAKWVKTRVGETGL 105
Cdd:PRK08213   17 VTGGSRGLGLQIAEALGEAGARVV---LSARKAEELEE-AAAHLEalgiDALWiaaDVADEADIERLAEETLERFGHVDI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 fgLVNNAGVA-GiiGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR--GRVVNITSVLGRIAANGG-----GYCV 177
Cdd:PRK08213   93 --LVNNAGATwG--APAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRSMIPRgyGRIINVASVAGLGGNPPEvmdtiAYNT 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2169419209 178 SKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN--LESLENTLKA 224
Cdd:PRK08213  169 SKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRgtLERLGEDLLA 217
PRK08589 PRK08589
SDR family oxidoreductase;
28-212 8.93e-12

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 64.41  E-value: 8.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQM--ASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGL 105
Cdd:PRK08589    6 NKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDKIksNGGKAKAYHVDISDEQQVKDFASEIKEQFGRVDV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 fgLVNNAGV---AGIIGPTPwltQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFG 181
Cdd:PRK08589   86 --LFNNAGVdnaAGRIHEYP---VDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAAdLYRSGYNAAKGA 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2169419209 182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:PRK08589  161 VINFTKSIAIEYGRDGIRANAIAPGTIETPL 191
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 30-212 1.55e-11

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 63.38  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGA----EDLQQMASSRLHTTLlDITDPQNVQQVAKWVKTRVGETGL 105
Cdd:PRK13394    9 TAVVTGAASGIGKEIALELARAGAAVAIADLNQDGAnavaDEINKAGGKAIGVAM-DVTNEDAVNAGIDKVAERFGSVDI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 fgLVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR--GRVVNITSVLGRIAANG-GGYCVSKFGL 182
Cdd:PRK13394   88 --LVSNAGIQ-IVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHSHEASPLkSAYVTAKHGL 164

                         170       180       190
                  ....*....|....*....|....*....|
gi 2169419209 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:PRK13394  165 LGLARVLAKEGAKHNVRSHVVCPGFVRTPL 194
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 30-213 2.07e-11

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 62.67  E-value: 2.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAgcltpsgaEDLQQ--MASSRLHTTLLDITDPqnVQQVAKWVKTrvgetgLFG 107
Cdd:PRK06550    7 TVLITGAASGIGLAQARAFLAQGAQVYG--------VDKQDkpDLSGNFHFLQLDLSDD--LEPLFDWVPS------VDI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLAL-LPLLQQARGRVVNITSVLGRIAANGG-GYCVSKFGLEAF 185
Cdd:PRK06550   71 LCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYlPQMLERKSGIIINMCSIASFVAGGGGaAYTASKHALAGF 150

                         170       180
                  ....*....|....*....|....*...
gi 2169419209 186 SDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK06550  151 TKQLALDYAKDGIQVFGIAPGAVKTPMT 178
PRK06114 PRK06114
SDR family oxidoreductase;
21-211 2.30e-11

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 62.88  E-value: 2.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  21 RQSLPARDAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSG--AEDLQQMASSRLHTTLL--DITDPQNVQQVAKWV 96
Cdd:PRK06114    1 PQLFDLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDglAETAEHIEAAGRRAIQIaaDVTSKADLRAAVART 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  97 KTRVGETGLfgLVNNAGVAGIIgPTPWLTQDDFQRVLNVNTLGP-IGVTLALLPLLQQARGRVVNITSVLGRIAANG--- 172
Cdd:PRK06114   81 EAELGALTL--AVNAAGIANAN-PAEEMEEEQWQTVMDINLTGVfLSCQAEARAMLENGGGSIVNIASMSGIIVNRGllq 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2169419209 173 GGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK06114  158 AHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATP 196
PRK07774 PRK07774
SDR family oxidoreductase;
28-230 2.35e-11

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 62.84  E-value: 2.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTL---LDITDPQNVQQVAKWVKTRVGetG 104
Cdd:PRK07774    6 DKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIavqVDVSDPDSAKAMADATVSAFG--G 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LFGLVNNAGVAGIIGPTPWLTQ--DDFQRVLNVNTLGPIGVTLALLPLLQQARG-RVVNITSVLGRIAanGGGYCVSKFG 181
Cdd:PRK07774   84 IDYLVNNAAIYGGMKLDLLITVpwDYYKKFMSVNLDGALVCTRAVYKHMAKRGGgAIVNQSSTAAWLY--SNFYGLAKVG 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2169419209 182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLENTLKACWARLP 230
Cdd:PRK07774  162 LNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVTPKEFVADMVKGIP 210
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 30-211 2.80e-11

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 62.60  E-value: 2.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASSRLHTTL------LDITDPQNVQQVAKWVKTRVGet 103
Cdd:PRK12429    6 VALVTGAASGIGLEIALALAKEGAKVV---IADLNDEAAAAAAEALQKAGGkaigvaMDVTDEEAINAGIDYAVETFG-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 104 GLFGLVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANG-GGYCVSKFG 181
Cdd:PRK12429   81 GVDILVNNAGIQ-HVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGgGRIINMASVHGLVGSAGkAAYVSAKHG 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 2169419209 182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK12429  160 LIGLTKVVALEGATHGVTVNAICPGYVDTP 189
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 31-213 2.97e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 62.46  E-value: 2.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAE----DLQQMAsSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLf 106
Cdd:PRK08085   12 ILITGSAQGIGFLLATGLAEYGAEIIINDITAERAElavaKLRQEG-IKAHAAPFNVTHKQEVEAAIEHIEKDIGPIDV- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 107 gLVNNAGVAGiIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQ-ARGRVVNITSV---LGRIAANggGYCVSKFGL 182
Cdd:PRK08085   90 -LINNAGIQR-RHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKrQAGKIINICSMqseLGRDTIT--PYAASKGAV 165

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2169419209 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK08085  166 KMLTRGMCVELARHNIQVNGIAPGYFKTEMT 196
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 30-213 3.43e-11

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 62.29  E-value: 3.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPS-GAEDLQQMASS---RLHTTLLDITD----PQNVQQVAKWvktrvg 101
Cdd:PRK12745    4 VALVTGGRRGIGLGIARALAAAGFDLAINDRPDDeELAATQQELRAlgvEVIFFPADVADlsahEAMLDAAQAA------ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 102 etglFG----LVNNAGVAGII-GPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQARGR-------VVNITSVLGRIA 169
Cdd:PRK12745   78 ----WGridcLVNNAGVGVKVrGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPeelphrsIVFVSSVNAIMV 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2169419209 170 A-NGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK12745  154 SpNRGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMT 198
PRK07201 PRK07201
SDR family oxidoreductase;
30-187 6.71e-11

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 63.05  E-value: 6.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASS------RLHTTLLDITDPQNVQQVAKWVKTRVGET 103
Cdd:PRK07201  373 VVLITGASSGIGRATAIKVAEAGATVF---LVARNGEALDELVAEirakggTAHAYTCDLTDSAAVDHTVKDILAEHGHV 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 104 GLfgLVNNAGVAgiIGPTPWLTQD---DFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITS--VLGRiAANGGGYCV 177
Cdd:PRK07201  450 DY--LVNNAGRS--IRRSVENSTDrfhDYERTMAVNYFGAVRLILGLLPHMRERRfGHVVNVSSigVQTN-APRFSAYVA 524

                         170
                  ....*....|
gi 2169419209 178 SKFGLEAFSD 187
Cdd:PRK07201  525 SKAALDAFSD 534
PRK07069 PRK07069
short chain dehydrogenase; Validated
 32-212 6.90e-11

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 61.65  E-value: 6.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  32 FITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASSRL---HTTLLDITDPQNVQQVAKWvKTRVGET----- 103
Cdd:PRK07069    3 FITGAAGGLGRAIARRMAEQGAKVF---LTDINDAAGLDAFAAEInaaHGEGVAFAAVQDVTDEAQW-QALLAQAadamg 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 104 GLFGLVNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPI-GVTLALLPLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFG 181
Cdd:PRK07069   79 GLSVLVNNAGV-GSFGAIEQIELDEWRRVMAINVESIFlGCKHALPYLRASQPASIVNISSVAAFKAePDYTAYNASKAA 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2169419209 182 LEAFSDSLRRDMAPFGVQV--SIVEPGFFRTPV 212
Cdd:PRK07069  158 VASLTKSIALDCARRGLDVrcNSIHPTFIRTGI 190
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 28-212 7.65e-11

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: 61.40  E-value: 7.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQ-MASSRLHTTLL---DITDPQNVQQVAKWVKTRVGEt 103
Cdd:cd08933     9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESeLNRAGPGSCKFvpcDVTKEEDIKTLISVTVERFGR- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 104 gLFGLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGL 182
Cdd:cd08933    88 -IDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIGqKQAAPYVATKGAI 166

                         170       180       190
                  ....*....|....*....|....*....|
gi 2169419209 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:cd08933   167 TAMTKALAVDESRYGVRVNCISPGNIWTPL 196
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 30-213 8.34e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 61.23  E-value: 8.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTP----SGAEDLQQmASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGL 105
Cdd:PRK07097   12 IALITGASYGIGFAIAKAYAKAGATIVFNDINQelvdKGLAAYRE-LGIEAHGYVCDVTDEDGVQAMVSQIEKEVGVIDI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 fgLVNNAGvagIIGPTPWL--TQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNI---TSVLGRiaANGGGYCVSK 179
Cdd:PRK07097   91 --LVNNAG---IIKRIPMLemSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGhGKIINIcsmMSELGR--ETVSAYAAAK 163

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2169419209 180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK07097  164 GGLKMLTKNIASEYGEANIQCNGIGPGYIATPQT 197
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 30-239 1.14e-10

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 60.79  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGC-LTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLFG- 107
Cdd:PRK12935    8 VAIVTGGAKGIGKAITVALAQEGAKVVINYnSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFGKVDi 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNAGVAGIIGPTPwLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANG-GGYCVSKFGLEAF 185
Cdd:PRK12935   88 LVNNAGITRDRTFKK-LNREDWERVIDVNLSSVFNTTSAVLPYITEAEeGRIISISSIIGQAGGFGqTNYSAAKAGMLGF 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2169419209 186 SDSLRRDMAPFGVQVSIVEPGFFRTPVTnLESLENTLKACWARLPPATQAHYGE 239
Cdd:PRK12935  167 TKSLALELAKTNVTVNAICPGFIDTEMV-AEVPEEVRQKIVAKIPKKRFGQADE 219
PRK06172 PRK06172
SDR family oxidoreductase;
30-210 1.41e-10

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 60.54  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAED---LQQMASSRLHTTLLDITDPQNVQQ-VAKWVKTrvgetgl 105
Cdd:PRK06172    9 VALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEEtvaLIREAGGEALFVACDVTRDAEVKAlVEQTIAA------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 FGLV----NNAGVAGIIGPTPWLTQDDFQRVLNVNTLGP-IGVTLALLPLLQQARGRVVNITSVLGRIAANG-GGYCVSK 179
Cdd:PRK06172   82 YGRLdyafNNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVwLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKmSIYAASK 161

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2169419209 180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK06172  162 HAVIGLTKSAAIEYAKKGIRVNAVCPAVIDT 192
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 30-211 1.50e-10

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: 60.54  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQ-VLAGCLTPSGAEDLQQMASSRLHTTLL----DITDPQNVQQVAKWVKTRVGetG 104
Cdd:cd08940     4 VALVTGSTSGIGLGIARALAAAGANiVLNGFGDAAEIEAVRAGLAAKHGVKVLyhgaDLSKPAAIEDMVAYAQRQFG--G 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LFGLVNNAGVAGIiGPTPWLTQDDFQRVLNVNTLGP-IGVTLALLPLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGL 182
Cdd:cd08940    82 VDILVNNAGIQHV-APIEDFPTEKWDAIIALNLSAVfHTTRLALPHMKKQGWGRIINIASVHGLVAsANKSAYVAAKHGV 160

                         170       180
                  ....*....|....*....|....*....
gi 2169419209 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd08940   161 VGLTKVVALETAGTGVTCNAICPGWVLTP 189
PRK06139 PRK06139
SDR family oxidoreductase;
25-211 1.86e-10

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 60.89  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  25 PARDAVIFITGCDSGFGRLLALQLDQKGFQ-VLAGcltpSGAEDLQQMASS--RLHTTLL----DITDPQNVQQVAKWVK 97
Cdd:PRK06139    4 PLHGAVVVITGASSGIGQATAEAFARRGARlVLAA----RDEEALQAVAEEcrALGAEVLvvptDVTDADQVKALATQAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  98 TRVGETGLFglVNNAGVaGIIG---PTPWltqDDFQRVLNVNTLG---------PIGVTLAllpllqqaRGRVVNITSVL 165
Cdd:PRK06139   80 SFGGRIDVW--VNNVGV-GAVGrfeETPI---EAHEQVIQTNLIGymrdahaalPIFKKQG--------HGIFINMISLG 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2169419209 166 GRIAAN-GGGYCVSKFGLEAFSDSLRRDMAPF-GVQVSIVEPGFFRTP 211
Cdd:PRK06139  146 GFAAQPyAAAYSASKFGLRGFSEALRGELADHpDIHVCDVYPAFMDTP 193
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 30-224 3.32e-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: 59.41  E-value: 3.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQqmASSRLHTTLLDITDPQNVQQVAKwvktRVGETGLfgLV 109
Cdd:cd05368     4 VALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELE--RGPGITTRVLDVTDKEQVAALAK----EEGRIDV--LF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 110 NNAGVAGIiGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAA--NGGGYCVSKFGLEAFS 186
Cdd:cd05368    76 NCAGFVHH-GSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKdGSIINMSSVASSIKGvpNRFVYSTTKAAVIGLT 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2169419209 187 DSLRRDMAPFGVQVSIVEPGFFRTPvtnleSLENTLKA 224
Cdd:cd05368   155 KSVAADFAQQGIRCNAICPGTVDTP-----SLEERIQA 187
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 108-211 3.55e-10

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 58.30  E-value: 3.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRI-AANGGGYCVSKFGLEAF 185
Cdd:cd02266    35 VVHNAAI-LDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRlGRFILISSVAGLFgAPGLGGYAASKAALDGL 113

                          90       100
                  ....*....|....*....|....*.
gi 2169419209 186 SDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd02266   114 AQQWASEGWGNGLPATAVACGTWAGS 139
PRK06947 PRK06947
SDR family oxidoreductase;
30-212 4.39e-10

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 59.05  E-value: 4.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQ----QMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGL 105
Cdd:PRK06947    4 VVLITGASRGIGRATAVLAAARGWSVGINYARDAAAAEETadavRAAGGRACVVAGDVANEADVIAMFDAVQSAFG--RL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 FGLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR----GRVVNITSVLGRIAANGG--GYCVSK 179
Cdd:PRK06947   82 DALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRggrgGAIVNVSSIASRLGSPNEyvDYAGSK 161

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2169419209 180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:PRK06947  162 GAVDTLTLGLAKELGPHGVRVNAVRPGLIETEI 194
PRK07814 PRK07814
SDR family oxidoreductase;
28-206 4.82e-10

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 59.02  E-value: 4.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSG----AEDLQQmASSRLHTTLLDITDPQNVQQVAKWVKTRVGET 103
Cdd:PRK07814   10 DQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQldevAEQIRA-AGRRAHVVAADLAHPEATAGLAGQAVEAFGRL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 104 GLfgLVNNAGVAGiigPTPWLT------QDDFQrvLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANG-GGYC 176
Cdd:PRK07814   89 DI--VVNNVGGTM---PNPLLStstkdlADAFT--FNVATAHALTVAAVPLMLEHSGGGSVINISSTMGRLAGRGfAAYG 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 2169419209 177 VSKFGLEAFSDSLRRDMAPfGVQVSIVEPG 206
Cdd:PRK07814  162 TAKAALAHYTRLAALDLCP-RIRVNAIAPG 190
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 32-210 5.32e-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: 58.90  E-value: 5.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  32 FITGCDSGFGRLLALQLDQKGFQVLAGCLTPS--GAEDLQQMASSRLHTTLL--DITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:cd05359     2 LVTGGSRGIGKAIALRLAERGADVVINYRKSKdaAAEVAAEIEELGGKAVVVraDVSQPQDVEEMFAAVKERFG--RLDV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNAGvAGIIGPTPWLTQDDFQRVLNVNTLGPI-GVTLALLPLLQQARGRVVNITSVL-GRIAANGGGYCVSKFGLEAF 185
Cdd:cd05359    80 LVSNAA-AGAFRPLSELTPAHWDAKMNTNLKALVhCAQQAAKLMRERGGGRIVAISSLGsIRALPNYLAVGTAKAALEAL 158

                         170       180
                  ....*....|....*....|....*
gi 2169419209 186 SDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:cd05359   159 VRYLAVELGPRGIRVNAVSPGVIDT 183
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 30-210 5.82e-10

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


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 58.62  E-value: 5.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCL-TPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgL 108
Cdd:cd05349     2 VVLVTGASRGLGAAIARSFAREGARVVVNYYrSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDT--I 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VNNAGVAGIIGPTPWLTQD-----DFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSvlgRIAANG----GGYCVS 178
Cdd:cd05349    80 VNNALIDFPFDPDQRKTFDtidweDYQQQLEGAVKGALNLLQAVLPDFKERGsGRVINIGT---NLFQNPvvpyHDYTTA 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2169419209 179 KFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:cd05349   157 KAALLGFTRNMAKELGPYGITVNMVSGGLLKV 188
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 25-213 6.13e-10

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 59.85  E-value: 6.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  25 PARDAVIFITGCDSGFGRLLALQLDQKGFQVLagCL-TPSGAEDLQQMASsRLH-TTL-LDITDPQNVQQVAKWVKTRVG 101
Cdd:PRK08261  207 PLAGKVALVTGAARGIGAAIAEVLARDGAHVV--CLdVPAAGEALAAVAN-RVGgTALaLDITAPDAPARIAEHLAERHG 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 102 etGLFGLVNNAGV------AGiigptpwLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGrIAANGG- 173
Cdd:PRK08261  284 --GLDIVVHNAGItrdktlAN-------MDEARWDSVLAVNLLAPLRITEALLAAGALGDgGRIVGVSSISG-IAGNRGq 353

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2169419209 174 -GYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK08261  354 tNYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQMT 394
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
30-205 6.18e-10

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 60.24  E-value: 6.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLH--TTLLDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:PRK08324  424 VALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPDRalGVACDVTDEAAVQAAFEEAALAFG--GVDI 501

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLG---------------PIGvtlallpllqqarGRVVNITSVLGRIA-AN 171
Cdd:PRK08324  502 VVSNAGIA-ISGPIEETSDEDWRRSFDVNATGhflvareavrimkaqGLG-------------GSIVFIASKNAVNPgPN 567

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2169419209 172 GGGYCVSKfgleAFSDSLRR----DMAPFGVQVSIVEP 205
Cdd:PRK08324  568 FGAYGAAK----AAELHLVRqlalELGPDGIRVNGVNP 601
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 30-213 7.91e-10

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: 58.27  E-value: 7.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQnvqQVAKWVKTRVGETG-LFGL 108
Cdd:cd08944     5 VAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQ---QVAALFERAVEEFGgLDLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIgVTLALLPLLQQARG--RVVNITSVLGRIAANG-GGYCVSKFGLEAF 185
Cdd:cd08944    82 VNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTF-LCCRHAAPRMIARGggSIVNLSSIAGQSGDPGyGAYGASKAAIRNL 160

                         170       180
                  ....*....|....*....|....*...
gi 2169419209 186 SDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:cd08944   161 TRTLAAELRHAGIRCNALAPGLIDTPLL 188
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 30-206 8.51e-10

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 58.51  E-value: 8.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDL-----QQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETG 104
Cdd:PRK12384    4 VAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVaqeinAEYGEGMAYGFGADATSEQSVLALSRGVDEIFGRVD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LfgLVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPI--GVTLALLPLLQQARGRVVNITSVLGRIAA-NGGGYCVSKFG 181
Cdd:PRK12384   84 L--LVYNAGIA-KAAFITDFQLGDFDRSLQVNLVGYFlcAREFSRLMIRDGIQGRIIQINSKSGKVGSkHNSGYSAAKFG 160

                         170       180
                  ....*....|....*....|....*
gi 2169419209 182 LEAFSDSLRRDMAPFGVQVSIVEPG 206
Cdd:PRK12384  161 GVGLTQSLALDLAEYGITVHSLMLG 185
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 21-213 9.13e-10

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: 58.23  E-value: 9.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  21 RQSLPARDAVIfiTGCDSGFGRLLALQLDQKGFQVLAgCLTPSGAED--LQQMASSRLHTTLL--DITDPQNVQQVAKWV 96
Cdd:cd05329     1 RWNLEGKTALV--TGGTKGIGYAIVEELAGLGAEVYT-CARNQKELDecLTEWREKGFKVEGSvcDVSSRSERQELMDTV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  97 KTRVGETgLFGLVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTLAL-LPLLQQARGRVVNITSVLGRIAANGGG- 174
Cdd:cd05329    78 ASHFGGK-LNILVNNAGTN-IRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAhPLLKASGNGNIVFISSVAGVIAVPSGAp 155

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2169419209 175 YCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:cd05329   156 YGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLV 194
PRK07074 PRK07074
SDR family oxidoreductase;
28-211 1.03e-09

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 58.24  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDL-QQMASSRLHTTLLDITDPQNVQQVakwVKTRVGETGLF 106
Cdd:PRK07074    2 KRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFaDALGDARFVPVACDLTDAASLAAA---LANAAAERGPV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 107 G-LVNNAGVAGIIG--PTpwlTQDDFQRVLNVNTLGP-IGVTLALLPLLQQARGRVVNITSVLGRIAANGGGYCVSKFGL 182
Cdd:PRK07074   79 DvLVANAGAARAASlhDT---TPASWRADNALNLEAAyLCVEAVLEGMLKRSRGAVVNIGSVNGMAALGHPAYSAAKAGL 155

                         170       180
                  ....*....|....*....|....*....
gi 2169419209 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK07074  156 IHYTKLLAVEYGRFGIRANAVAPGTVKTQ 184
PRK09730 PRK09730
SDR family oxidoreductase;
29-210 1.14e-09

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 57.94  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  29 AVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGA--EDLQQMASSRLHTTLL--DITDPQNVQQVAKWVKtRVGETg 104
Cdd:PRK09730    2 AIALVTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAaqEVVNLITQAGGKAFVLqaDISDENQVVAMFTAID-QHDEP- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LFGLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR----GRVVNITSVLGRIAANGG--GYCVS 178
Cdd:PRK09730   80 LAALVNNAGILFTQCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALKHggsgGAIVNVSSAASRLGAPGEyvDYAAS 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2169419209 179 KFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK09730  160 KGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYT 191
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 28-211 1.94e-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: 57.24  E-value: 1.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:cd05363     3 GKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWG--SIDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNAGVAGiIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQA--RGRVVNITSVLGRIA-ANGGGYCVSKFGLEA 184
Cdd:cd05363    81 LVNNAALFD-LAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgrGGKIINMASQAGRRGeALVGVYCATKAAVIS 159

                         170       180
                  ....*....|....*....|....*..
gi 2169419209 185 FSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd05363   160 LTQSAGLNLIRHGINVNAIAPGVVDGE 186
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 28-212 2.11e-09

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: 57.08  E-value: 2.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKG-FQVLAGCLTPSGAE---DLQQMASSRLHTtllDITDPQNVQQVAKWVKTRVGEt 103
Cdd:cd05326     4 GKVAIITGGASGIGEATARLFAKHGaRVVIADIDDDAGQAvaaELGDPDISFVHC---DVTVEADVRAAVDTAVARFGR- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 104 gLFGLVNNAGVAGiiGPTPWL---TQDDFQRVLNVNTLGP-IGVTLALLPLLQQARGRVVNITSVLGRIAanGGG---YC 176
Cdd:cd05326    80 -LDIMFNNAGVLG--APCYSIletSLEEFERVLDVNVYGAfLGTKHAARVMIPAKKGSIVSVASVAGVVG--GLGphaYT 154

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2169419209 177 VSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:cd05326   155 ASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPL 190
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 28-216 2.36e-09

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 56.94  E-value: 2.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDlqqmasSRLHTTLLDITDPQNVQQVAKWVKTRVGEtgLFG 107
Cdd:PRK06171    9 GKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQH------ENYQFVPTDVSSAEEVNHTVAEIIEKFGR--IDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNAGVAG---IIGPTP-----WLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANGGG-YCV 177
Cdd:PRK06171   81 LVNNAGINIprlLVDEKDpagkyELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHdGVIVNMSSEAGLEGSEGQScYAA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2169419209 178 SKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFR-TPVTNLE 216
Cdd:PRK06171  161 TKAALNSFTRSWAKELGKHNIRVVGVAPGILEaTGLRTPE 200
PRK12746 PRK12746
SDR family oxidoreductase;
30-212 3.98e-09

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 56.20  E-value: 3.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLA--GCLTPSGAEDLQQMASSRLHTTLL--DITDPQNVQQVAKWVKT----RVG 101
Cdd:PRK12746    8 VALVTGASRGIGRAIAMRLANDGALVAIhyGRNKQAADETIREIESNGGKAFLIeaDLNSIDGVKKLVEQLKNelqiRVG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 102 ETGLFGLVNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGPIGVTlALLPLLQQARGRVVNITSVLGRIAANGG-GYCVSKF 180
Cdd:PRK12746   88 TSEIDILVNNAGI-GTQGTIENTTEEIFDEIMAVNIKAPFFLI-QQTLPLLRAEGRVINISSAEVRLGFTGSiAYGLSKG 165

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2169419209 181 GLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:PRK12746  166 ALNTMTLPLAKHLGERGITVNTIMPGYTKTDI 197
PRK05867 PRK05867
SDR family oxidoreductase;
32-210 4.14e-09

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 56.20  E-value: 4.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  32 FITGCDSGFGRLLALQLDQKGFQVlagCLTPSGAEDLQQMASS------RLHTTLLDITDPQnvqQVAKWVKTRVGETGl 105
Cdd:PRK05867   13 LITGASTGIGKRVALAYVEAGAQV---AIAARHLDALEKLADEigtsggKVVPVCCDVSQHQ---QVTSMLDQVTAELG- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 fGLVNNAGVAGIIGPTPWLTQ--DDFQRVLNVNTLGpIGVTLALLPLLQQARGR---VVNITSVLGRI---AANGGGYCV 177
Cdd:PRK05867   86 -GIDIAVCNAGIITVTPMLDMplEEFQRLQNTNVTG-VFLTAQAAAKAMVKQGQggvIINTASMSGHIinvPQQVSHYCA 163

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2169419209 178 SKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK05867  164 SKAAVIHLTKAMAVELAPHKIRVNSVSPGYILT 196
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 30-205 4.23e-09

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: 56.24  E-value: 4.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVakwVKTRVGETG-LFGL 108
Cdd:cd05345     7 VAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAM---VEAALSKFGrLDIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGpIGVTLALLPLLQQARGRVVNITsvlgrIAANGGG--------YCVSKF 180
Cdd:cd05345    84 VNNAGITHRNKPMLEVDEEEFDRVFAVNVKS-IYLSAQALVPHMEEQGGGVIIN-----IASTAGLrprpgltwYNASKG 157

                         170       180
                  ....*....|....*....|....*
gi 2169419209 181 GLEAFSDSLRRDMAPFGVQVSIVEP 205
Cdd:cd05345   158 WVVTATKAMAVELAPRNIRVNCLCP 182
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 27-210 4.41e-09

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 56.03  E-value: 4.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  27 RDAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDIT------DPQNVQQVAKWVKTRV 100
Cdd:PRK08945   11 KDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIIPldlltaTPQNYQQLADTIEEQF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 101 GEtgLFGLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPL-LQQARGRVVNITSVLGRIA-ANGGGYCVS 178
Cdd:PRK08945   91 GR--LDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLlLKSPAASLVFTSSSVGRQGrANWGAYAVS 168

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2169419209 179 KFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK08945  169 KFATEGMMQVLADEYQGTNLRVNCINPGGTRT 200
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
28-211 5.12e-09

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 56.19  E-value: 5.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:PRK07067    6 GKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFG--GIDI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNAGVAGiIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR--GRVVNITSVLGRIA-ANGGGYCVSKFGLEA 184
Cdd:PRK07067   84 LFNNAALFD-MAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGrgGKIINMASQAGRRGeALVSHYCATKAAVIS 162

                         170       180
                  ....*....|....*....|....*..
gi 2169419209 185 FSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK07067  163 YTQSAALALIRHGINVNAIAPGVVDTP 189
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 30-210 5.17e-09

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: 56.32  E-value: 5.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAED-----LQQMASSRLHTTLLDITDPQNVQQVAKWVKTRvgETG 104
Cdd:cd09807     3 TVIITGANTGIGKETARELARRGARVIMACRDMAKCEEaaaeiRRDTLNHEVIVRHLDLASLKSIRAFAAEFLAE--EDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LFGLVNNAGVagIIGPTpWLTQDDFQRVLNVNTLGPIGVTLALL-PLLQQARGRVVNITSVL---GRIAAN--------- 171
Cdd:cd09807    81 LDVLINNAGV--MRCPY-SKTEDGFEMQFGVNHLGHFLLTNLLLdLLKKSAPSRIVNVSSLAhkaGKINFDdlnseksyn 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2169419209 172 -GGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:cd09807   158 tGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRT 197
PRK08628 PRK08628
SDR family oxidoreductase;
27-230 8.62e-09

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 55.35  E-value: 8.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  27 RDAVIFITGCDSGFGRLLALQLDQKG-FQVLAGCLTPSG--AEDLQQmASSRLHTTLLDITDPQnvqQVAKWVKTRVGET 103
Cdd:PRK08628    6 KDKVVIVTGGASGIGAAISLRLAEEGaIPVIFGRSAPDDefAEELRA-LQPRAEFVQVDLTDDA---QCRDAVEQTVAKF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 104 G-LFGLVNNAGVAGIIGptpwL--TQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGrIAANGG--GYCVS 178
Cdd:PRK08628   82 GrIDGLVNNAGVNDGVG----LeaGREAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISSKTA-LTGQGGtsGYAAA 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2169419209 179 KFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP-----VTNLESLENTLKACWARLP 230
Cdd:PRK08628  157 KGAQLALTREWAVALAKDGVRVNAVIPAEVMTPlyenwIATFDDPEAKLAAITAKIP 213
PRK06953 PRK06953
SDR family oxidoreductase;
29-210 1.41e-08

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 54.31  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  29 AVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASsrlHTTLLDITDPQNVQQVAkWVKTrvGETGLFGL 108
Cdd:PRK06953    2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQALGA---EALALDVADPASVAGLA-WKLD--GEALDAAV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VnnagVAGIIGP----TPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANGGG----YCVSKF 180
Cdd:PRK06953   76 Y----VAGVYGPrtegVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSRMGSIGDATGTtgwlYRASKA 151

                         170       180       190
                  ....*....|....*....|....*....|
gi 2169419209 181 GLEAFSDSLRRDmAPFGVQVSIvEPGFFRT 210
Cdd:PRK06953  152 ALNDALRAASLQ-ARHATCIAL-HPGWVRT 179
PRK07063 PRK07063
SDR family oxidoreductase;
30-213 1.49e-08

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 54.67  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVL-----AGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetG 104
Cdd:PRK07063    9 VALVTGAAQGIGAAIARAFAREGAAVAladldAALAERAAAAIARDVAGARVLAVPADVTDAASVAAAVAAAEEAFG--P 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LFGLVNNAGVAGIIGPTPwLTQDDFQRVLNVNTLGPI-GVTLALLPLLQQARGRVVNITSVLG-RIAANGGGYCVSKFGL 182
Cdd:PRK07063   87 LDVLVNNAGINVFADPLA-MTDEDWRRCFAVDLDGAWnGCRAVLPGMVERGRGSIVNIASTHAfKIIPGCFPYPVAKHGL 165

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2169419209 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK07063  166 LGLTRALGIEYAARNVRVNAIAPGYIETQLT 196
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-213 1.55e-08

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 54.40  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  27 RDAVIFITGCDSGFGRLLALQLDQKGFQVLAgcLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLf 106
Cdd:PRK06463    6 KGKVALITGGTRGIGRAIAEAFLREGAKVAV--LYNSAENEAKELREKGVFTIKCDVGNRDQVKKSKEVVEKEFGRVDV- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 107 gLVNNAGVAGIIgptPWLTQDD--FQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSV--LGRIAANGGGYCVSKFG 181
Cdd:PRK06463   83 -LVNNAGIMYLM---PFEEFDEekYNKMIKINLNGAIYTTYEFLPLLKLSKnGAIVNIASNagIGTAAEGTTFYAITKAG 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2169419209 182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK06463  159 IIILTRRLAFELGKYGIRVNAVAPGWVETDMT 190
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 28-210 1.56e-08

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 54.47  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQ---QMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETG 104
Cdd:PRK06113   11 GKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVdeiQQLGGQAFACRCDITSEQELSALADFALSKLGKVD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LfgLVNNAGVAgiiGPTPW-LTQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVV-NITSVLGR-IAANGGGYCVSKFG 181
Cdd:PRK06113   91 I--LVNNAGGG---GPKPFdMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVIlTITSMAAEnKNINMTSYASSKAA 165

                         170       180
                  ....*....|....*....|....*....
gi 2169419209 182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK06113  166 ASHLVRNMAFDLGEKNIRVNGIAPGAILT 194
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
30-213 2.25e-08

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 53.97  E-value: 2.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAE-----DLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETG 104
Cdd:PRK06935   17 VAIVTGGNTGLGQGYAVALAKAGADII---ITTHGTNwdetrRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKID 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LfgLVNNAGvagIIGPTPWL--TQDDFQRVLNVNtLGPIGVTLALLPLLQQAR--GRVVNITSVLgriAANGG----GYC 176
Cdd:PRK06935   94 I--LVNNAG---TIRRAPLLeyKDEDWNAVMDIN-LNSVYHLSQAVAKVMAKQgsGKIINIASML---SFQGGkfvpAYT 164

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2169419209 177 VSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK06935  165 ASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANT 201
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 30-210 2.29e-08

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: 54.11  E-value: 2.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAE---DLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLF 106
Cdd:cd05365     1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEavaAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFG--GIT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 107 GLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIAA-NGGGYCVSKFGLEA 184
Cdd:cd05365    79 ILVNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCApHMQKAGGGAILNISSMSSENKNvRIAAYGSSKAAVNH 158

                         170       180
                  ....*....|....*....|....*.
gi 2169419209 185 FSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:cd05365   159 MTRNLAFDLGPKGIRVNAVAPGAVKT 184
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 33-212 3.29e-08

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 53.62  E-value: 3.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPS---GAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgLV 109
Cdd:PRK07523   15 VTGSSQGIGYALAEGLAQAGAEVILNGRDPAklaAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGPIDI--LV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 110 NNAGVAgIIGPTPWLTQDDFQRVL--NVNTLGPIGvTLALLPLLQQARGRVVNITSVLGRIAANG-GGYCVSKFGLEAFS 186
Cdd:PRK07523   93 NNAGMQ-FRTPLEDFPADAFERLLrtNISSVFYVG-QAVARHMIARGAGKIINIASVQSALARPGiAPYTATKGAVGNLT 170

                         170       180
                  ....*....|....*....|....*.
gi 2169419209 187 DSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:PRK07523  171 KGMATDWAKHGLQCNAIAPGYFDTPL 196
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 29-207 9.05e-08

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: 51.89  E-value: 9.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  29 AVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAED--LQQMASSRLHTTLL--DITDPQNVQQVAKWVKTRVGETG 104
Cdd:cd05357     1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQrlKDELNALRNSAVLVqaDLSDFAACADLVAAAFRAFGRCD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LfgLVNNAGV--AGIIGPTPWltqDDFQRVLNVNTLGPIGVTLA-LLPLLQQARGRVVNIT-SVLGRIAANGGGYCVSKF 180
Cdd:cd05357    81 V--LVNNASAfyPTPLGQGSE---DAWAELFGINLKAPYLLIQAfARRLAGSRNGSIINIIdAMTDRPLTGYFAYCMSKA 155

                         170       180
                  ....*....|....*....|....*..
gi 2169419209 181 GLEAFSDSLRRDMAPFgVQVSIVEPGF 207
Cdd:cd05357   156 ALEGLTRSAALELAPN-IRVNGIAPGL 181
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 27-210 1.06e-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: 52.13  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  27 RDAVIFITGCDSGFGRLLALQLDQKGFQVLaGC-----LTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVG 101
Cdd:cd05343     5 RGRVALVTGASVGIGAAVARALVQHGMKVV-GCarrvdKIEALAAECQSAGYPTLFPYQCDLSNEEQILSMFSAIRTQHQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 102 etGLFGLVNNAGVAgiiGPTPWLT--QDDFQRVLNVNTLGPIGVTLALL---PLLQQARGRVVNITSVLGRIAANG---G 173
Cdd:cd05343    84 --GVDVCINNAGLA---RPEPLLSgkTEGWKEMFDVNVLALSICTREAYqsmKERNVDDGHIININSMSGHRVPPVsvfH 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2169419209 174 GYCVSKFGLEAFSDSLRRDM--APFGVQVSIVEPGFFRT 210
Cdd:cd05343   159 FYAATKHAVTALTEGLRQELreAKTHIRATSISPGLVET 197
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 28-206 1.28e-07

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: 51.95  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAED----LQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGET 103
Cdd:cd08930     2 DKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQlkeeLTNLYKNRVIALELDITSKESIKELIESYLEKFGRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 104 GlfGLVNNAGVAGIIGPTPW--LTQDDFQRVLNVNTLGPIGVTLALLPL-LQQARGRVVNITSVLGRIAAN-----GGG- 174
Cdd:cd08930    82 D--ILINNAYPSPKVWGSRFeeFPYEQWNEVLNVNLGGAFLCSQAFIKLfKKQGKGSIINIASIYGVIAPDfriyeNTQm 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2169419209 175 -----YCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPG 206
Cdd:cd08930   160 yspveYSVIKAGIIHLTKYLAKYYADTGIRVNAISPG 196
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 30-218 1.38e-07

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


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 51.70  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLL----DITDPQNVQQVAKWVKTRVGETGL 105
Cdd:cd05322     4 VAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYGEKAYgfgaDATNEQSVIALSKGVDEIFKRVDL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 fgLVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPI--GVTLALLPLLQQARGRVVNITSVLGRIAA-NGGGYCVSKFGL 182
Cdd:cd05322    84 --LVYSAGIA-KSAKITDFELGDFDRSLQVNLVGYFlcAREFSKLMIRDGIQGRIIQINSKSGKVGSkHNSGYSAAKFGG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2169419209 183 EAFSDSLRRDMAPFGVQVSIVEPG-FFRTPVtnLESL 218
Cdd:cd05322   161 VGLTQSLALDLAEHGITVNSLMLGnLLKSPM--FQSL 195
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 25-210 1.55e-07

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: 51.72  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  25 PARDAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKwvktRVGETG 104
Cdd:cd08951     4 PPPMKRIFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSSLAETRKLAD----QVNAIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LF-GLVNNAGVagIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLqqargRVVNITSVL--------------GRIA 169
Cdd:cd08951    80 RFdAVIHNAGI--LSGPNRKTPDTGIPAMVAVNVLAPYVLTALIRRPK-----RLIYLSSGMhrggnaslddidwfNRGE 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2169419209 170 ANGGGYCVSKFGLEAFSDSLRRdmAPFGVQVSIVEPGFFRT 210
Cdd:cd08951   153 NDSPAYSDSKLHVLTLAAAVAR--RWKDVSSNAVHPGWVPT 191
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 28-214 1.95e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 51.08  E-value: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASS------RLHTTLLDITDPQNVQQVAKWVKTRVG 101
Cdd:PRK07478    6 GKVAIITGASSGIGRAAAKLFAREGAKVV---VGARRQAELDQLVAEiraeggEAVALAGDVRDEAYAKALVALAVERFG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 102 etGLFGLVNNAGVAGIIGPTPWLTQDDFQRVLNVN-TLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANGG--GYCVS 178
Cdd:PRK07478   83 --GLDIAFNNAGTLGEMGPVAEMSLEGWRETLATNlTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHTAGFPGmaAYAAS 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2169419209 179 KFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN 214
Cdd:PRK07478  161 KAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGR 196
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 30-237 2.55e-07

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: 50.85  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLL--DITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:cd08943     3 VALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQGGPRALGVqcDVTSEAQVQSAFEQAVLEFG--GLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR--GRVVNITSVLGrIAA--NGGGYCVSKfgle 183
Cdd:cd08943    81 VVSNAGIA-TSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGigGNIVFNASKNA-VAPgpNAAAYSAAK---- 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2169419209 184 AFSDSLRR----DMAPFGVQVSIVEP-GFFRTPVTNleslENTLKACWARLPPATQAHY 237
Cdd:cd08943   155 AAEAHLARclalEGGEDGIRVNTVNPdAVFRGSKIW----EGVWRAARAKAYGLLEEEY 209
PRK07577 PRK07577
SDR family oxidoreductase;
28-206 2.75e-07

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 50.50  E-value: 2.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAgcLTPSGAEDLqqmaSSRLHTTllDITDPqnvQQVAKWVKTRVGETGLFG 107
Cdd:PRK07577    3 SRTVLVTGATKGIGLALSLRLANLGHQVIG--IARSAIDDF----PGELFAC--DLADI---EQTAATLAQINEIHPVDA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANGGGYCVSKFGLEAFS 186
Cdd:PRK07577   72 IVNNVGIA-LPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREqGRIVNICSRAIFGALDRTSYSAAKSALVGCT 150

                         170       180
                  ....*....|....*....|
gi 2169419209 187 DSLRRDMAPFGVQVSIVEPG 206
Cdd:PRK07577  151 RTWALELAEYGITVNAVAPG 170
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 64-231 2.93e-07

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: 50.79  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  64 GAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGEtgLFGLVNNAGVA---GIIGptpwLTQDDFQRVLNVNTLGP 140
Cdd:cd05352    48 KAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFGK--IDILIANAGITvhkPALD----YTYEQWNKVIDVNLNGV 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 141 IGV-TLALLPLLQQARGRVVNITSVLGRIA---ANGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLE 216
Cdd:cd05352   122 FNCaQAAAKIFKKQGKGSLIITASMSGTIVnrpQPQAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFV 201

                         170
                  ....*....|....*
gi 2169419209 217 SLEntLKACWARLPP 231
Cdd:cd05352   202 DKE--LRKKWESYIP 214
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 33-210 3.27e-07

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: 50.29  E-value: 3.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  33 ITGCDSGFGRLLALQLDQKGFQVlagCLTPSGAEDLQQMASS-------RLHTTLLDITD-PQNVQQVAKWVKTRvgETG 104
Cdd:cd05356     6 VTGATDGIGKAYAEELAKRGFNV---ILISRTQEKLDAVAKEieekygvETKTIAADFSAgDDIYERIEKELEGL--DIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LfgLVNNAGVAGIIgPTPWL--TQDDFQRVLNVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRI-AANGGGYCVSKF 180
Cdd:cd05356    81 I--LVNNVGISHSI-PEYFLetPEDELQDIINVNVMATLKMTRLILpGMVKRKKGAIVNISSFAGLIpTPLLATYSASKA 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 2169419209 181 GLEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:cd05356   158 FLDFFSRALYEEYKSQGIDVQSLLPYLVAT 187
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
28-230 4.34e-07

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 50.10  E-value: 4.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGA-----EDLQQMASsRLHTTLLDITDPQNVQQVAKWVKTRVGe 102
Cdd:PRK08063    4 GKVALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAaeetaEEIEALGR-KALAVKANVGDVEKIKEMFAQIDEEFG- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 103 tGLFGLVNNAGvAGIIGPTPWLTQDDFQRVLNVNTLG-PIGVTLALLPLLQQARGRVVNITSvLG--RIAANGGGYCVSK 179
Cdd:PRK08063   82 -RLDVFVNNAA-SGVLRPAMELEESHWDWTMNINAKAlLFCAQEAAKLMEKVGGGKIISLSS-LGsiRYLENYTTVGVSK 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2169419209 180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRT-PVTNLESLENTLKACWARLP 230
Cdd:PRK08063  159 AALEALTRYLAVELAPKGIAVNAVSGGAVDTdALKHFPNREELLEDARAKTP 210
PRK06138 PRK06138
SDR family oxidoreductase;
28-211 4.42e-07

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 50.15  E-value: 4.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQM--ASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGL 105
Cdd:PRK06138    5 GRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAiaAGGRAFARQGDVGSAEAVEALVDFVAARWG--RL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 106 FGLVNNAGVaGIIGPTPWLTQDDFQRVLNVNTLGP-IGVTLALLPLLQQARGRVVNITSVLGRIAANG-GGYCVSKFGLE 183
Cdd:PRK06138   83 DVLVNNAGF-GCGGTVVTTDEADWDAVMRVNVGGVfLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGrAAYVASKGAIA 161

                         170       180
                  ....*....|....*....|....*...
gi 2169419209 184 AFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK06138  162 SLTRAMALDHATDGIRVNAVAPGTIDTP 189
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 24-218 4.47e-07

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 50.34  E-value: 4.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  24 LPARDAVIfiTGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEdlQQMASSR-----LHTTLLDITDPQNVQQVAKWVKT 98
Cdd:PRK05876    4 FPGRGAVI--TGGASGIGLATGTEFARRGARVVLGDVDKPGLR--QAVNHLRaegfdVHGVMCDVRHREEVTHLADEAFR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  99 RVGETGLfgLVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTLA--LLPLLQQARGRVVNITSVLGRIAANG-GGY 175
Cdd:PRK05876   80 LLGHVDV--VFSNAGIV-VGGPIVEMTHDDWRWVIDVDLWGSIHTVEAflPRLLEQGTGGHVVFTASFAGLVPNAGlGAY 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2169419209 176 CVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP-VTNLESL 218
Cdd:PRK05876  157 GVAKYGVVGLAETLAREVTADGIGVSVLCPMVVETNlVANSERI 200
PRK08177 PRK08177
SDR family oxidoreductase;
31-210 5.27e-07

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 49.64  E-value: 5.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTtlLDITDPQNVQQVAkwvkTRVGETGLFGLVN 110
Cdd:PRK08177    4 ALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIEK--LDMNDPASLDQLL----QRLQGQRFDLLFV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 111 NAGVAgiiGPTPW----LTQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANGGG----YCVSKFGL 182
Cdd:PRK08177   78 NAGIS---GPAHQsaadATAAEIGQLFLTNAIAPIRLARRLLGQVRPGQGVLAFMSSQLGSVELPDGGemplYKASKAAL 154

                         170       180
                  ....*....|....*....|....*...
gi 2169419209 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK08177  155 NSMTRSFVAELGEPTLTVLSMHPGWVKT 182
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
30-230 7.68e-07

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 49.52  E-value: 7.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLA-GCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgL 108
Cdd:PRK12481   10 VAIITGCNTGLGQGMAIGLAKAGADIVGvGVAEAPETQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGHIDI--L 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VNNagvAGIIGPTPWL--TQDDFQRVLNVN--TLGPIGVTLALLPLLQQARGRVVNITSVLgriAANGG----GYCVSKF 180
Cdd:PRK12481   88 INN---AGIIRRQDLLefGNKDWDDVININqkTVFFLSQAVAKQFVKQGNGGKIINIASML---SFQGGirvpSYTASKS 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2169419209 181 GLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN-LESLENTLKACWARLP 230
Cdd:PRK12481  162 AVMGLTRALATELSQYNINVNAIAPGYMATDNTAaLRADTARNEAILERIP 212
PRK09135 PRK09135
pteridine reductase; Provisional
 30-206 8.71e-07

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 49.16  E-value: 8.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTpSGAEdLQQMA----SSRLHTTLL---DITDPQNVQQVAKWVKTRVGe 102
Cdd:PRK09135    8 VALITGGARRIGAAIARTLHAAGYRVAIHYHR-SAAE-ADALAaelnALRPGSAAAlqaDLLDPDALPELVAACVAAFG- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 103 tGLFGLVNNAGVagiIGPTPW--LTQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLG-RIAANGGGYCVSK 179
Cdd:PRK09135   85 -RLDALVNNASS---FYPTPLgsITEAQWDDLFASNLKAPFFLSQAAAPQLRKQRGAIVNITDIHAeRPLKGYPVYCAAK 160

                         170       180
                  ....*....|....*....|....*..
gi 2169419209 180 FGLEAFSDSLRRDMAPfGVQVSIVEPG 206
Cdd:PRK09135  161 AALEMLTRSLALELAP-EVRVNAVAPG 186
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 28-221 8.80e-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: 49.38  E-value: 8.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVlagcltpsGAEDLQQmasSRLHTTLLDITD--------PQNVQQVAKWVKTR 99
Cdd:cd08935     5 NKVAVITGGTGVLGGAMARALAQAGAKV--------AALGRNQ---EKGDKVAKEITAlggraialAADVLDRASLERAR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 100 VGETGLFG----LVNNAGV---AGIIGPTPW----------LTQDDFQRVLNVNTLG---PIGVtlALLPLLQQARGRVV 159
Cdd:cd08935    74 EEIVAQFGtvdiLINGAGGnhpDATTDPEHYepeteqnffdLDEEGWEFVFDLNLNGsflPSQV--FGKDMLEQKGGSII 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2169419209 160 NITSV-----LGRIAAngggYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPvTNLESLENT 221
Cdd:cd08935   152 NISSMnafspLTKVPA----YSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTP-QNRKLLINP 213
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 30-212 1.38e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 48.85  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLV 109
Cdd:PRK08265    8 VAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFG--RVDILV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 110 NNA------GVAGiigptpwlTQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANGGG-YCVSKFGL 182
Cdd:PRK08265   86 NLActylddGLAS--------SRADWLAALDVNLVSAAMLAQAAHPHLARGGGAIVNFTSISAKFAQTGRWlYPASKAAI 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 2169419209 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:PRK08265  158 RQLTRSMAMDLAPDGIRVNSVSPGWTWSRV 187
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 30-210 1.54e-06

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


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 48.34  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLV 109
Cdd:cd09761     3 VAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLG--RIDVLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 110 NNAGVAGIiGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLG-RIAANGGGYCVSKFGLEAFSDS 188
Cdd:cd09761    81 NNAARGSK-GILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAfQSEPDSEAYAASKGGLVALTHA 159

                         170       180
                  ....*....|....*....|..
gi 2169419209 189 LRRDMAPFgVQVSIVEPGFFRT 210
Cdd:cd09761   160 LAMSLGPD-IRVNCISPGWINT 180
PRK07102 PRK07102
SDR family oxidoreductase;
131-213 1.64e-06

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 48.38  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 131 RVLNVNTLGPIGV-TLALLPLLQQARGRVVNITSVLG-RIAANGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFF 208
Cdd:PRK07102  102 REFRTNFEGPIALlTLLANRFEARGSGTIVGISSVAGdRGRASNYVYGSAKAALTAFLSGLRNRLFKSGVHVLTVKPGFV 181


                  ....*
gi 2169419209 209 RTPVT 213
Cdd:PRK07102  182 RTPMT 186
PRK06128 PRK06128
SDR family oxidoreductase;
24-212 2.03e-06

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 48.70  E-value: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  24 LPARDAVIfiTGCDSGFGRLLALQLDQKGFQVLAGCLtPSGAEDLQQM-----ASSRLHTTLL-DITDPQNVQQVAKWVK 97
Cdd:PRK06128   53 LQGRKALI--TGADSGIGRATAIAFAREGADIALNYL-PEEEQDAAEVvqliqAEGRKAVALPgDLKDEAFCRQLVERAV 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  98 TRVGetGLFGLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLG------------PIGVTlallpllqqargrVVNITSVL 165
Cdd:PRK06128  130 KELG--GLDILVNIAGKQTAVKDIADITTEQFDATFKTNVYAmfwlckaaiphlPPGAS-------------IINTGSIQ 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2169419209 166 G-RIAANGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:PRK06128  195 SyQPSPTLLDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPL 242
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 28-206 2.07e-06

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 48.36  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAED-----LQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVge 102
Cdd:cd09809     1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAavsriLEEWHKARVEAMTLDLASLRSVQRFAEAFKAKN-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 103 TGLFGLVNNAGVAGIigptPW-LTQDDFQRVLNVNTLGPIGVTLALLPL-LQQARGRVVNITSVLGRIA----ANGG--- 173
Cdd:cd09809    79 SPLHVLVCNAAVFAL----PWtLTEDGLETTFQVNHLGHFYLVQLLEDVlRRSAPARVIVVSSESHRFTdlpdSCGNldf 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2169419209 174 --------------GYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPG 206
Cdd:cd09809   155 sllsppkkkywsmlAYNRAKLCNILFSNELHRRLSPRGITSNSLHPG 201
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 30-227 2.09e-06

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 48.15  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLA--GCLTPSGAEDLQQMASS-----RLHTTLLDITDPQNV-QQVAKWVKTRVG 101
Cdd:PRK12747    6 VALVTGASRGIGRAIAKRLANDGALVAIhyGNRKEEAEETVYEIQSNggsafSIGANLESLHGVEALySSLDNELQNRTG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 102 ETGLFGLVNNAGvagiIGPTPWL---TQDDFQRVLNVNTLGPIGVTlALLPLLQQARGRVVNITSVLGRIA-ANGGGYCV 177
Cdd:PRK12747   86 STKFDILINNAG----IGPGAFIeetTEQFFDRMVSVNAKAPFFII-QQALSRLRDNSRIINISSAATRISlPDFIAYSM 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2169419209 178 SKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVtNLESLENTLKACWA 227
Cdd:PRK12747  161 TKGAINTMTFTLAKQLGARGITVNAILPGFIKTDM-NAELLSDPMMKQYA 209
PRK07775 PRK07775
SDR family oxidoreductase;
22-206 2.49e-06

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 48.21  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  22 QSLPARDAVIfITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTL---LDITDPQNVQQVAKWVKT 98
Cdd:PRK07775    5 EPHPDRRPAL-VAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAVafpLDVTDPDSVKSFVAQAEE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  99 RVGETGLfgLVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGV-TLALLPLLQQARGRVVNITS-VLGRIAANGGGYC 176
Cdd:PRK07775   84 ALGEIEV--LVSGAGDT-YFGKLHEISTEQFESQVQIHLVGANRLaTAVLPGMIERRRGDLIFVGSdVALRQRPHMGAYG 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 2169419209 177 VSKFGLEAFSDSLRRDMAPFGVQVSIVEPG 206
Cdd:PRK07775  161 AAKAGLEAMVTNLQMELEGTGVRASIVHPG 190
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
30-230 3.34e-06

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 47.56  E-value: 3.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLaGCLTPSGAEDLQQMASsrLHTTLLDIT-DPQNVQQVAKWVKTRVGETGLFG- 107
Cdd:PRK08993   12 VAVVTGCDTGLGQGMALGLAEAGCDIV-GINIVEPTETIEQVTA--LGRRFLSLTaDLRKIDGIPALLERAVAEFGHIDi 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNagvAGIIGPTPWL--TQDDFQRVLNVN--TLGPIGVTLALLPLLQQARGRVVNITSVLgriAANGG----GYCVSK 179
Cdd:PRK08993   89 LVNN---AGLIRREDAIefSEKDWDDVMNLNikSVFFMSQAAAKHFIAQGNGGKIINIASML---SFQGGirvpSYTASK 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2169419209 180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN-LESLENTLKACWARLP 230
Cdd:PRK08993  163 SGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQqLRADEQRSAEILDRIP 214
PRK07831 PRK07831
SDR family oxidoreductase;
75-211 3.72e-06

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 47.34  E-value: 3.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  75 RLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLVNNAGVAGIiGPTPWLTQDDFQRVLNVNTLGPIGVT--LALLPLLQ 152
Cdd:PRK07831   70 RVEAVVCDVTSEAQVDALIDAAVERLG--RLDVLVNNAGLGGQ-TPVVDMTDDEWSRVLDVTLTGTFRATraALRYMRAR 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 153 QARGRVVNITSVLG-RIAANGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK07831  147 GHGGVIVNNASVLGwRAQHGQAHYAAAKAGVMALTRCSALEAAEYGVRINAVAPSIAMHP 206
PRK05717 PRK05717
SDR family oxidoreductase;
30-207 4.09e-06

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 47.19  E-value: 4.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETG-LFGL 108
Cdd:PRK05717   12 VALVTGAARGIGLGIAAWLIAEGWQVV---LADLDRERGSKVAKALGENAWFIAMDVADEAQVAAGVAEVLGQFGrLDAL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VNNAGVAGIIGPT-PWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLEAFS 186
Cdd:PRK05717   89 VCNAAIADPHNTTlESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHNGAIVNLASTRARQSePDTEAYAASKGGLLALT 168

                         170       180
                  ....*....|....*....|.
gi 2169419209 187 DSLRRDMAPfGVQVSIVEPGF 207
Cdd:PRK05717  169 HALAISLGP-EIRVNAVSPGW 188
PRK05866 PRK05866
SDR family oxidoreductase;
21-211 6.36e-06

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 47.04  E-value: 6.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  21 RQSLPARDAVIFITGCDSGFGRLLALQLDQKGFQVLAgclTPSGAEDLQQMAS------SRLHTTLLDITDPQNVQQVAK 94
Cdd:PRK05866   33 RQPVDLTGKRILLTGASSGIGEAAAEQFARRGATVVA---VARREDLLDAVADritragGDAMAVPCDLSDLDAVDALVA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  95 WVKTRVGetGLFGLVNNAGVAgIIGPTP-----WltqDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITS--VLG 166
Cdd:PRK05866  110 DVEKRIG--GVDILINNAGRS-IRRPLAesldrW---HDVERTMVLNYYAPLRLIRGLAPGMLERGdGHIINVATwgVLS 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2169419209 167 RIAANGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK05866  184 EASPLFSVYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATP 228
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 28-206 1.78e-05

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: 45.42  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGEtgLFG 107
Cdd:cd05348     4 GEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGK--LDC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNAGV----AGIIGpTPWLTQDD-FQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGrIAANGGG--YCVSKF 180
Cdd:cd05348    82 FIGNAGIwdysTSLVD-IPEEKLDEaFDELFHINVKGYILGAKAALPALYATEGSVIFTVSNAG-FYPGGGGplYTASKH 159

                         170       180
                  ....*....|....*....|....*.
gi 2169419209 181 GLEAFSDSLRRDMAPFgVQVSIVEPG 206
Cdd:cd05348   160 AVVGLVKQLAYELAPH-IRVNGVAPG 184
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 30-210 1.86e-05

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 45.47  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCL-TPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETgLFGL 108
Cdd:PRK08642    7 TVLVTGGSRGLGAAIARAFAREGARVVVNYHqSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEHFGKP-ITTV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VNNAGVAGIIGPT-----PWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNI-TSVLGRIAANGGGYCVSKFG 181
Cdd:PRK08642   86 VNNALADFSFDGDarkkaDDITWEDFQQQLEGSVKGALNTIQAALPGMREQGfGRIINIgTNLFQNPVVPYHDYTTAKAA 165

                         170       180
                  ....*....|....*....|....*....
gi 2169419209 182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK08642  166 LLGLTRNLAAELGPYGITVNMVSGGLLRT 194
PRK08251 PRK08251
SDR family oxidoreductase;
31-213 2.02e-05

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 45.31  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQvLAGC------LTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetG 104
Cdd:PRK08251    5 ILITGASSGLGAGMAREFAAKGRD-LALCarrtdrLEELKAELLARYPGIKVAVAALDVNDHDQVFEVFAEFRDELG--G 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LFGLVNNAGvagiIGPTPWLTQDDFQ---RVLNVNTLGPIG-VTLALLPLLQQARGRVVNITSVL------GRIAAnggg 174
Cdd:PRK08251   82 LDRVIVNAG----IGKGARLGTGKFWankATAETNFVAALAqCEAAMEIFREQGSGHLVLISSVSavrglpGVKAA---- 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2169419209 175 YCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK08251  154 YAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMN 192
PLN02253 PLN02253
xanthoxin dehydrogenase
 30-205 4.19e-05

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 44.43  E-value: 4.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVlagCLTpsgaeDLQQMASSRLHTTL----------LDITDPQNVQQVAKWVKTR 99
Cdd:PLN02253   20 VALVTGGATGIGESIVRLFHKHGAKV---CIV-----DLQDDLGQNVCDSLggepnvcffhCDVTVEDDVSRAVDFTVDK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 100 VGETGLfgLVNNAGVAGiiGPTPWLTQ---DDFQRVLNVNTLGP-IGVTLALLPLLQQARGRVVNITSVLGRIAANG-GG 174
Cdd:PLN02253   92 FGTLDI--MVNNAGLTG--PPCPDIRNvelSEFEKVFDVNVKGVfLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGpHA 167

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2169419209 175 YCVSKFGLEAFSDSLRRDMAPFGVQVSIVEP 205
Cdd:PLN02253  168 YTGSKHAVLGLTRSVAAELGKHGIRVNCVSP 198
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 30-139 4.29e-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: 44.12  E-value: 4.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQ-----QMASSRLHTTLLDITDPQNVQQVAKWVKTRVGEtg 104
Cdd:cd09808     3 SFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARkeietESGNQNIFLHIVDMSDPKQVWEFVEEFKEEGKK-- 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2169419209 105 LFGLVNNAGVagiIGPTPWLTQDDFQRVLNVNTLG 139
Cdd:cd09808    81 LHVLINNAGC---MVNKRELTEDGLEKNFATNTLG 112
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 25-212 5.77e-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: 43.67  E-value: 5.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  25 PARDAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQM--ASSRLHTTLLDITDPQNVQQVAKWVKTRVGE 102
Cdd:cd08937     1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAEIlaAGDAAHVHTADLETYAGAQGVVRAAVERFGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 103 TGLfgLVNNAGvaGIIGPTPWLTQDDFQRVLNVN-TLGPIGVTLALLPLLQQAR--GRVVNITSVLGRiAANGGGYCVSK 179
Cdd:cd08937    81 VDV--LINNVG--GTIWAKPYEHYEEEQIEAEIRrSLFPTLWCCRAVLPHMLERqqGVIVNVSSIATR-GIYRIPYSAAK 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2169419209 180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:cd08937   156 GGVNALTASLAFEHARDGIRVNAVAPGGTEAPP 188
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 75-206 7.37e-05

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 43.62  E-value: 7.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  75 RLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgLVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQA 154
Cdd:PRK12859   69 KVSSMELDLTQNDAPKELLNKVTEQLGYPHI--LVNNAAYS-TNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKK 145

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2169419209 155 RG-RVVNITS------VLGRIAangggYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPG 206
Cdd:PRK12859  146 SGgRIINMTSgqfqgpMVGELA-----YAATKGAIDALTSSLAAEVAHLGITVNAINPG 199
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 27-211 9.19e-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: 43.43  E-value: 9.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  27 RDAVIFITGCDSGFGRLLALQLDQKGFQVLAGCL--TPSGAEDLQQMASSRLHTTLL---DITDPQNVQQVAKWVKTRVG 101
Cdd:cd05355    25 KGKKALITGGDSGIGRAVAIAFAREGADVAINYLpeEEDDAEETKKLIEEEGRKCLLipgDLGDESFCRDLVKEVVKEFG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 102 etGLFGLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQArGRVVNITSVLGRiaaNGGG----YCV 177
Cdd:cd05355   105 --KLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKKG-SSIINTTSVTAY---KGSPhlldYAA 178

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2169419209 178 SKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd05355   179 TKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTP 212
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 28-206 1.01e-04

(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: 43.08  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLtpsGAEDLQQMASSRLHTTLLD---------ITDPQNVQQVAKWVKT 98
Cdd:cd05353     5 GRVVLVTGAGGGLGRAYALAFAERGAKVVVNDL---GGDRKGSGKSSSAADKVVDeikaaggkaVANYDSVEDGEKIVKT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  99 RVGEtglFG----LVNNAGV------AGIigptpwlTQDDFQRVLNVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGr 167
Cdd:cd05353    82 AIDA---FGrvdiLVNNAGIlrdrsfAKM-------SEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKfGRIINTSSAAG- 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2169419209 168 IAANGG--GYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPG 206
Cdd:cd05353   151 LYGNFGqaNYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA 191
PRK12742 PRK12742
SDR family oxidoreductase;
108-206 1.18e-04

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 42.82  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 108 LVNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQArGRVVNITSVLG-RIAANGG-GYCVSKFGLEAF 185
Cdd:PRK12742   79 LVVNAGIA-VFGDALELDADDIDRLFKINIHAPYHASVEAARQMPEG-GRIIIIGSVNGdRMPVAGMaAYAASKSALQGM 156

                          90       100
                  ....*....|....*....|.
gi 2169419209 186 SDSLRRDMAPFGVQVSIVEPG 206
Cdd:PRK12742  157 ARGLARDFGPRGITINVVQPG 177
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 30-228 1.19e-04

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: 42.77  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVL-----AGCLTPSGAEDLQQMAssrlHTTLLDI-----------TDPQNVQQVA 93
Cdd:cd05338     5 VAFVTGASRGIGRAIALRLAKAGATVVvaaktASEGDNGSAKSLPGTI----EETAEEIeaaggqalpivVDVRDEDQVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  94 KWVKTRVGETG-LFGLVNNAGVA--GIIGPTPwltQDDFQRVLNVNTLGP-IGVTLALLPLLQQARGRVVNITSVLGRIA 169
Cdd:cd05338    81 ALVEATVDQFGrLDILVNNAGAIwlSLVEDTP---AKRFDLMQRVNLRGTyLLSQAALPHMVKAGQGHILNISPPLSLRP 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 170 ANGG-GYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPgffRTPVTNLESLENTLKACWAR 228
Cdd:cd05338   158 ARGDvAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWP---STAIETPAATELSGGSDPAR 214
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 23-225 1.23e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 42.87  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  23 SLPARDAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTP----SGAEDLQQMA-SSRLHTTLLDITDPQnvqQVAKWVK 97
Cdd:PRK05875    2 QLSFQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPdklaAAAEEIEALKgAGAVRYEPADVTDED---QVARAVD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  98 TRVGETG-LFGLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTL-ALLPLLQQARGRVVNITSvlgrIAANG--- 172
Cdd:PRK05875   79 AATAWHGrLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKhAARELVRGGGGSFVGISS----IAASNthr 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2169419209 173 --GGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRT----PVTNLESLENTLKAC 225
Cdd:PRK05875  155 wfGAYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTdlvaPITESPELSADYRAC 213
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 32-211 2.08e-04

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: 41.74  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  32 FITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASSRlhTTLLDITDPQNVQQvakwVKTRVGETGLFGLVNN 111
Cdd:cd11730     2 LILGATGGIGRALARALAGRGWRLL---LSGRDAGALAGLAAEV--GALARPADVAAELE----VWALAQELGPLDLLVY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 112 AgvAGIIGPTPWL--TQDDFQRVLNVNTLGPIGVTLALLPLLQQArGRVVNITSVLGRIAANG-GGYCVSKFGLEAFSDS 188
Cdd:cd11730    73 A--AGAILGKPLArtKPAAWRRILDANLTGAALVLKHALALLAAG-ARLVFLGAYPELVMLPGlSAYAAAKAALEAYVEV 149

                         170       180
                  ....*....|....*....|...
gi 2169419209 189 LRRDMApfGVQVSIVEPGFFRTP 211
Cdd:cd11730   150 ARKEVR--GLRLTLVRPPAVDTG 170
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 27-211 2.40e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 41.94  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  27 RDAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSG-AEDLQQMASSRLHTTLL---DITDPQNVQQ-VAKWVKTrvg 101
Cdd:PRK06701   45 KGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEdANETKQRVEKEGVKCLLipgDVSDEAFCKDaVEETVRE--- 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 102 etglFG----LVNNAG----VAGIigptPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQArGRVVNITSVLGrIAANGG 173
Cdd:PRK06701  122 ----LGrldiLVNNAAfqypQQSL----EDITAEQLDKTFKTNIYSYFHMTKAALPHLKQG-SAIINTGSITG-YEGNET 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2169419209 174 --GYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK06701  192 liDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTP 231
PRK07985 PRK07985
SDR family oxidoreductase;
19-212 2.51e-04

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 41.90  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  19 RDRQSLpardavifITGCDSGFGRLLALQLDQKGFQVLAGCLtPSGAEDLQQMAS----SRLHTTLL--DITDPQNVQQV 92
Cdd:PRK07985   48 KDRKAL--------VTGGDSGIGRAAAIAYAREGADVAISYL-PVEEEDAQDVKKiieeCGRKAVLLpgDLSDEKFARSL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  93 AKWVKTRVGETGLFGLVnnAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQArGRVVNITSVLG-RIAAN 171
Cdd:PRK07985  119 VHEAHKALGGLDIMALV--AGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPKG-ASIITTSSIQAyQPSPH 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2169419209 172 GGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:PRK07985  196 LLDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTAL 236
PRK07035 PRK07035
SDR family oxidoreductase;
30-210 2.98e-04

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 41.54  E-value: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASS------RLHTTLLDITDPQNVQQVAKWVKTRVGEt 103
Cdd:PRK07035   10 IALVTGASRGIGEAIAKLLAQQGAHVI---VSSRKLDGCQAVADAivaaggKAEALACHIGEMEQIDALFAHIRERHGR- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 104 gLFGLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGV-TLALLPLLQQARGRVVNITSVLGRIAANGGG-YCVSKFG 181
Cdd:PRK07035   86 -LDILVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMsVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGiYSITKAA 164

                         170       180
                  ....*....|....*....|....*....
gi 2169419209 182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK07035  165 VISMTKAFAKECAPFGIRVNALLPGLTDT 193
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
31-139 3.04e-04

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 41.89  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCdSGF-GRLLALQLDQKGFQVLAGCLTPSGAEDLQQMAssRLHTTLLDITDPQNVQQVAKWVKTrvgetglfgLV 109
Cdd:COG0451     2 ILVTGG-AGFiGSHLARRLLARGHEVVGLDRSPPGAANLAALP--GVEFVRGDLRDPEALAAALAGVDA---------VV 69

                          90       100       110
                  ....*....|....*....|....*....|
gi 2169419209 110 NNAGVAGIigptpwlTQDDFQRVLNVNTLG 139
Cdd:COG0451    70 HLAAPAGV-------GEEDPDETLEVNVEG 92
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 30-135 5.31e-04

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 40.82  E-value: 5.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMAS------SRLHTTLLDITDPQNVQQVAKWVKTRVGEt 103
Cdd:PRK07677    3 VVIITGGSSGMGKAMAKRFAEEGANVV---ITGRTKEKLEEAKLeieqfpGQVLTVQMDVRNPEDVQKMVEQIDEKFGR- 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2169419209 104 gLFGLVNNAgvAG-IIGPTPWLTQDDFQRVLNV 135
Cdd:PRK07677   79 -IDALINNA--AGnFICPAEDLSVNGWNSVIDI 108
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-210 9.38e-04

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 40.09  E-value: 9.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  27 RDAVIFITGCDSGFGRLLALQLDQKGFQVLAGclTPSGAEDLQQM------ASSRLHTTLLDITDPQNVQQVAKWVKTRV 100
Cdd:PRK06077    5 KDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVN--AKKRAEEMNETlkmvkeNGGEGIGVLADVSTREGCETLAKATIDRY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 101 GetGLFGLVNNAGVaGIIgpTPWLTQDD--FQRVLNVNTLGPIGVTLALLPLLQQArGRVVNITSVLGRIAANG-GGYCV 177
Cdd:PRK06077   83 G--VADILVNNAGL-GLF--SPFLNVDDklIDKHISTDFKSVIYCSQELAKEMREG-GAIVNIASVAGIRPAYGlSIYGA 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2169419209 178 SKFGLEAFSDSLRRDMAPfGVQVSIVEPGFFRT 210
Cdd:PRK06077  157 MKAAVINLTKYLALELAP-KIRVNAIAPGFVKT 188
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 30-218 1.11e-03

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 39.94  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLV 109
Cdd:PRK06200    8 VALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAFG--KLDCFV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 110 NNAGV----AGIIGpTPWLTQDD-FQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGrIAANGGG--YCVSKFGL 182
Cdd:PRK06200   86 GNAGIwdynTSLVD-IPAETLDTaFDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLSNSS-FYPGGGGplYTASKHAV 163

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2169419209 183 EAFSDSLRRDMAPfGVQVSIVEPGFFRTPVTNLESL 218
Cdd:PRK06200  164 VGLVRQLAYELAP-KIRVNGVAPGGTVTDLRGPASL 198
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 30-166 1.60e-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: 39.40  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEdlqqmassrlhttlLDITDPQNVQQVAKWVKTRVGEtGLFGLV 109
Cdd:cd05328     1 TIVITGAASGIGAATAELLEDAGHTVIGIDLREADVI--------------ADLSTPEGRAAAIADVLARCSG-VLDGLV 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2169419209 110 NNAGVAgiiGPTPwltQDDfqrVLNVNTLGPIGVTLALL-PLLQQARGRVVNITSVLG 166
Cdd:cd05328    66 NCAGVG---GTTV---AGL---VLKVNYFGLRALMEALLpRLRKGHGPAAVVVSSIAG 114
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 30-265 1.94e-03

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


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 39.35  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQV-LAG-CLTPSGAEDLQQMASS--RLHTTLLDITDPQNVQQVAKWVKTRvgETG- 104
Cdd:cd09763     5 IALVTGASRGIGRGIALQLGEAGATVyITGrTILPQLPGTAEEIEARggKCIPVRCDHSDDDEVEALFERVARE--QQGr 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 105 LFGLVNNA--GVAGIIG----------PTPWltqDDfqrvlnVNTLG------------PIGVTlallpllqQARGRVVN 160
Cdd:cd09763    83 LDILVNNAyaAVQLILVgvakpfweepPTIW---DD------INNVGlrahyacsvyaaPLMVK--------AGKGLIVI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 161 ITSVLGRIAANGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTpvtnlesleNTLKACWARLPPATQAHYGEA 240
Cdd:cd09763   146 ISSTGGLEYLFNVAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRT---------ELVLEMPEDDEGSWHAKERDA 216

                         250       260
                  ....*....|....*....|....*...
gi 2169419209 241 FL---TTYLqVQRRIMNLICDPDLTKVT 265
Cdd:cd09763   217 FLngeTTEY-SGRCVVALAADPDLMELS 243
PRK07062 PRK07062
SDR family oxidoreductase;
23-138 2.51e-03

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 38.87  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  23 SLPARDAVIFITGCDSGFGRLLALQLDQKGFQVlAGC------LTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWV 96
Cdd:PRK07062    3 QIQLEGRVAVVTGGSSGIGLATVELLLEAGASV-AICgrdeerLASAEARLREKFPGARLLAARCDVLDEADVAAFAAAV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2169419209  97 KTRVGetGLFGLVNNAG---VA-------------------GIIGPT----PWLTQDDFQRVLNVNTL 138
Cdd:PRK07062   82 EARFG--GVDMLVNNAGqgrVStfadttddawrdelelkyfSVINPTraflPLLRASAAASIVCVNSL 147
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 75-206 4.88e-03

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 37.75  E-value: 4.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  75 RLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgLVNNAGVAGIiGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQA 154
Cdd:PRK12748   68 RCEHMEIDLSQPYAPNRVFYAVSERLGDPSI--LINNAAYSTH-TRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGK 144

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2169419209 155 R-GRVVNITS------VLGRIAangggYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPG 206
Cdd:PRK12748  145 AgGRIINLTSgqslgpMPDELA-----YAATKGAIEAFTKSLAPELAEKGITVNAVNPG 198
PRK07856 PRK07856
SDR family oxidoreductase;
28-210 5.02e-03

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 37.99  E-value: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  28 DAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLqqmASSRLHTTllDITDPQnvqQVAKWVKTRVGETG-LF 106
Cdd:PRK07856    6 GRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETVDG---RPAEFHAA--DVRDPD---QVAALVDAIVERHGrLD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 107 GLVNNAGVAgiigptPWLTQDD-----FQRVLNVNTLGPIGVTLALLPL--LQQARGRVVNITSVLGRIAANG-GGYCVS 178
Cdd:PRK07856   78 VLVNNAGGS------PYALAAEasprfHEKIVELNLLAPLLVAQAANAVmqQQPGGGSIVNIGSVSGRRPSPGtAAYGAA 151

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2169419209 179 KFGLEAFSDSLRRDMAPfGVQVSIVEPGFFRT 210
Cdd:PRK07856  152 KAGLLNLTRSLAVEWAP-KVRVNAVVVGLVRT 182
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 30-170 5.99e-03

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 37.70  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  30 VIFITGCDSGFGRLLALQLDQKGFQV-LAGCLTPSGAEDLQQMASSRLHTTL----LDITDPQNVQQVAKWVKTRVGETG 104
Cdd:PRK06197   18 VAVVTGANTGLGYETAAALAAKGAHVvLAVRNLDKGKAAAARITAATPGADVtlqeLDLTSLASVRAAADALRAAYPRID 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2169419209 105 LfgLVNNAGVagiIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQARG-RVVNITSVLGRIAA 170
Cdd:PRK06197   98 L--LINNAGV---MYTPKQTTADGFELQFGTNHLGHFALTGLLLDRLLPVPGsRVVTVSSGGHRIRA 159
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 31-211 9.20e-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: 36.79  E-value: 9.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209  31 IFITGCDSGFGRLLALQLDQKGFQVL-AGcltpSGAEDLQqmassrlhttlLDITDPQNVQQVAKwvktrvgETGLF-GL 108
Cdd:cd11731     1 IIVIGATGTIGLAVAQLLSAHGHEVItAG----RSSGDYQ-----------VDITDEASIKALFE-------KVGHFdAI 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419209 109 VNNAGVAgIIGPTPWLTQDDFQRVLNVNTLGPIGVTlALLPLLQQARGRVVNITSVLG-RIAANGGGYCVSKFGLEAFSD 187
Cdd:cd11731    59 VSTAGDA-EFAPLAELTDADFQRGLNSKLLGQINLV-RHGLPYLNDGGSITLTSGILAqRPIPGGAAAATVNGALEGFVR 136

                         170       180
                  ....*....|....*....|....
gi 2169419209 188 SLRRDMaPFGVQVSIVEPGFFRTP 211
Cdd:cd11731   137 AAAIEL-PRGIRINAVSPGVVEES 159
 
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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