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Conserved domains on  [gi|214010158|ref|NP_001135743|]
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dehydrogenase/reductase SDR family member 9 isoform 1 precursor [Homo sapiens]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10176849)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 30-306 1.54e-161

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: 451.35  E-value: 1.54e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTE--SGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLW 107
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 108 GLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAI-VGGGYTPSKYAVEGF 186
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFpAGGAYCASKAAVEAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 187 NDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEK-KLAIWEQLSPDIKQQYGEGYIEKSLDKLKGNKSYVNMDLSPVV 265
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKqAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 214010158 266 ECMDHALTSLFPKTHYAAGKDAKIFWIPLSHMPAALQDFLL 306
Cdd:cd09805  241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 30-306 1.54e-161

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: 451.35  E-value: 1.54e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTE--SGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLW 107
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 108 GLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAI-VGGGYTPSKYAVEGF 186
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFpAGGAYCASKAAVEAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 187 NDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEK-KLAIWEQLSPDIKQQYGEGYIEKSLDKLKGNKSYVNMDLSPVV 265
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKqAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 214010158 266 ECMDHALTSLFPKTHYAAGKDAKIFWIPLSHMPAALQDFLL 306
Cdd:cd09805  241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
27-305 6.02e-53

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 174.29  E-value: 6.02e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  27 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE---TSERLRTVLLDVTDPENVKRTAQWVKNQVGe 103
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAElraAGARVEVVALDVTDPDAVAALAEAVLARFG- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 104 kGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPSKY 181
Cdd:COG0300   82 -PIDVLVNNAGV-GGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPlMRARGRGRIVNVSSVAGLRGLPGmAAYAASKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 182 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAiweqLSPDIkqqygegyieksldklkgnksyvnmdl 261
Cdd:COG0300  160 ALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPL----LSPEE--------------------------- 208

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 214010158 262 spVVECMDHALTSlfPKTHYAAGKDAKIFWIPLSHMPAALQDFL 305
Cdd:COG0300  209 --VARAILRALER--GRAEVYVGWDARLLARLLRLLPRLFDRLL 248
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 30-217 6.90e-45

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 151.61  E-value: 6.90e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158   30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE---TSERLRTVLLDVTDPENVKRTAQWVKNQVGekGL 106
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKElgaLGGKALFIQGDVTDRAQVKALVEQAVERLG--RL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  107 WGLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLA-IVGGGYTPSKYAVE 184
Cdd:pfam00106  79 DILVNNAGITGL-GPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPyPGGSAYSASKAAVI 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 214010158  185 GFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPV 217
Cdd:pfam00106 158 GFTRSLALELAPHGIRVNAVAPGGVDTDMTKEL 190
PRK06914 PRK06914
SDR family oxidoreductase;
30-308 2.99e-44

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 152.49  E-value: 2.99e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAET-----SERLRTVLLDVTDPENVKrTAQWVKNQVGEK 104
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQAtqlnlQQNIKVQQLDVTDQNSIH-NFQLVLKEIGRI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 GLwgLINNAG--VPGVLaptDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSK 180
Cdd:PRK06914  83 DL--LVNNAGyaNGGFV---EEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGlSPYVSSK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 181 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNladpvkviekklaIWE------QLSPDIKQQYGEgYIEKSLDKL-KGN 253
Cdd:PRK06914 158 YALEGFSESLRLELKPFGIDVALIEPGSYNTN-------------IWEvgkqlaENQSETTSPYKE-YMKKIQKHInSGS 223

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 214010158 254 KSYVNMDlsPVVECMDHALTSLFPKTHYAAGKDAKIFWIPLSHMPAALQDFLLLK 308
Cdd:PRK06914 224 DTFGNPI--DVANLIVEIAESKRPKLRYPIGKGVKLMILAKKILPWRLWEYLVLK 276
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 30-306 1.54e-161

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: 451.35  E-value: 1.54e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTE--SGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLW 107
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 108 GLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAI-VGGGYTPSKYAVEGF 186
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFpAGGAYCASKAAVEAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 187 NDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEK-KLAIWEQLSPDIKQQYGEGYIEKSLDKLKGNKSYVNMDLSPVV 265
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKqAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 214010158 266 ECMDHALTSLFPKTHYAAGKDAKIFWIPLSHMPAALQDFLL 306
Cdd:cd09805  241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 30-288 9.69e-63

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: 199.38  E-value: 9.69e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRtaqwVKNQVGEKG--LW 107
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKA----AVKEVIERFgrID 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 108 GLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYAVEG 185
Cdd:cd05374   77 VLVNNAGY-GLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPlMRKQGSGRIVNVSSVAGLVPTPFLGpYCASKAALEA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 186 FNDSLRRDMKAFGVHVSCIEPGLFKTNLADPvkviekklaiweQLSPDIKQQYGEGY--IEKSLDKLKGNKSYVNMDLSP 263
Cdd:cd05374  156 LSESLRLELAPFGIKVTIIEPGPVRTGFADN------------AAGSALEDPEISPYapERKEIKENAAGVGSNPGDPEK 223

                        250       260
                 ....*....|....*....|....*
gi 214010158 264 VVECMDHALTSLFPKTHYAAGKDAK 288
Cdd:cd05374  224 VADVIVKALTSESPPLRYFLGSDAL 248
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
27-305 6.02e-53

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 174.29  E-value: 6.02e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  27 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE---TSERLRTVLLDVTDPENVKRTAQWVKNQVGe 103
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAElraAGARVEVVALDVTDPDAVAALAEAVLARFG- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 104 kGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPSKY 181
Cdd:COG0300   82 -PIDVLVNNAGV-GGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPlMRARGRGRIVNVSSVAGLRGLPGmAAYAASKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 182 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAiweqLSPDIkqqygegyieksldklkgnksyvnmdl 261
Cdd:COG0300  160 ALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPL----LSPEE--------------------------- 208

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 214010158 262 spVVECMDHALTSlfPKTHYAAGKDAKIFWIPLSHMPAALQDFL 305
Cdd:COG0300  209 --VARAILRALER--GRAEVYVGWDARLLARLLRLLPRLFDRLL 248
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 28-233 6.93e-53

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: 173.44  E-value: 6.93e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  28 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLW 107
Cdd:COG4221    4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFG--RLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 108 GLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYAVEG 185
Cdd:COG4221   82 VLVNNAGV-ALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPaMRARGSGHIVNISSIAGLRPYPGGAvYAATKAAVRG 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 214010158 186 FNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAI-----WEQLSPD 233
Cdd:COG4221  161 LSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAavyegLEPLTPE 213
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 30-217 6.90e-45

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 151.61  E-value: 6.90e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158   30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE---TSERLRTVLLDVTDPENVKRTAQWVKNQVGekGL 106
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKElgaLGGKALFIQGDVTDRAQVKALVEQAVERLG--RL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  107 WGLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLA-IVGGGYTPSKYAVE 184
Cdd:pfam00106  79 DILVNNAGITGL-GPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPyPGGSAYSASKAAVI 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 214010158  185 GFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPV 217
Cdd:pfam00106 158 GFTRSLALELAPHGIRVNAVAPGGVDTDMTKEL 190
PRK06914 PRK06914
SDR family oxidoreductase;
30-308 2.99e-44

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 152.49  E-value: 2.99e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAET-----SERLRTVLLDVTDPENVKrTAQWVKNQVGEK 104
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQAtqlnlQQNIKVQQLDVTDQNSIH-NFQLVLKEIGRI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 GLwgLINNAG--VPGVLaptDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSK 180
Cdd:PRK06914  83 DL--LVNNAGyaNGGFV---EEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGlSPYVSSK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 181 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNladpvkviekklaIWE------QLSPDIKQQYGEgYIEKSLDKL-KGN 253
Cdd:PRK06914 158 YALEGFSESLRLELKPFGIDVALIEPGSYNTN-------------IWEvgkqlaENQSETTSPYKE-YMKKIQKHInSGS 223

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 214010158 254 KSYVNMDlsPVVECMDHALTSLFPKTHYAAGKDAKIFWIPLSHMPAALQDFLLLK 308
Cdd:PRK06914 224 DTFGNPI--DVANLIVEIAESKRPKLRYPIGKGVKLMILAKKILPWRLWEYLVLK 276
PRK05993 PRK05993
SDR family oxidoreductase;
30-309 1.17e-43

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 150.95  E-value: 1.17e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETserLRTVLLDVTDPENVKRTAQWVKNQVGEKgLWGL 109
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEAEG---LEAFQLDYAEPESIAALVAQVLELSGGR-LDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 110 INNA--GVPGVLA--PTDWLtledyREPIEVNLFGLISVTLNMLPLVKK-AQGRVINVSSVGGRLAI-VGGGYTPSKYAV 183
Cdd:PRK05993  81 FNNGayGQPGAVEdlPTEAL-----RAQFEANFFGWHDLTRRVIPVMRKqGQGRIVQCSSILGLVPMkYRGAYNASKFAI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 184 EGFNDSLRRDMKAFGVHVSCIEPGLFKTNL-ADPVKVIEKKLaiweqlspDIKQQ-YGEGYiEKSLDKLKGNKSYVNMDL 261
Cdd:PRK05993 156 EGLSLTLRMELQGSGIHVSLIEPGPIETRFrANALAAFKRWI--------DIENSvHRAAY-QQQMARLEGGGSKSRFKL 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 214010158 262 SP--VVECMDHALTSLFPKTHYAAGKDAKIFWIPLSHMPAALQDFLLLKQ 309
Cdd:PRK05993 227 GPeaVYAVLLHALTAPRPRPHYRVTTPAKQGALLKRLLPARWLYRLLRKA 276
PRK06182 PRK06182
short chain dehydrogenase; Validated
 30-288 5.37e-40

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 141.25  E-value: 5.37e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAAC--------LTESGSTALKaetserlrtvlLDVTDPENVKRTAQWVKNQV 101
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYGAArrvdkmedLASLGVHPLS-----------LDVTDEASIKAAVDTIIAEE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 102 GEKGLwgLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLA-IVGGGYTPS 179
Cdd:PRK06182  73 GRIDV--LVNNAGY-GSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIYtPLGAWYHAT 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 180 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADpvkVIEKKLAIWEQLSPdikqqYGE--GYIEKSLDKLKGNksyv 257
Cdd:PRK06182 150 KFALEGFSDALRLEVAPFGIDVVVIEPGGIKTEWGD---IAADHLLKTSGNGA-----YAEqaQAVAASMRSTYGS---- 217

                        250       260       270
                 ....*....|....*....|....*....|...
gi 214010158 258 NMDLSP--VVECMDHALTSLFPKTHYAAGKDAK 288
Cdd:PRK06182 218 GRLSDPsvIADAISKAVTARRPKTRYAVGFGAK 250
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 30-214 3.59e-38

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 136.58  E-value: 3.59e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGL 109
Cdd:PRK06180   5 KTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFG--PIDVL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 110 INNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPSKYAVEGFN 187
Cdd:PRK06180  83 VNNAGY-GHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPgMRARRRGHIVNITSMGGLITMPGiGYYCGSKFALEGIS 161

                        170       180
                 ....*....|....*....|....*..
gi 214010158 188 DSLRRDMKAFGVHVSCIEPGLFKTNLA 214
Cdd:PRK06180 162 ESLAKEVAPFGIHVTAVEPGSFRTDWA 188
PRK08017 PRK08017
SDR family oxidoreductase;
30-217 6.64e-38

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 135.21  E-value: 6.64e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLtesgstalKAETSERLRT-----VLLDVTDPENVKRTAQWVKNQVGEK 104
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAACR--------KPDDVARMNSlgftgILLDLDDPESVERAADEVIALTDNR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 gLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPSKYA 182
Cdd:PRK08017  75 -LYGLFNNAGF-GVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPaMLPHGEGRIVMTSSVMGLISTPGrGAYAASKYA 152

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 214010158 183 VEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPV 217
Cdd:PRK08017 153 LEAWSDALRMELRHSGIKVSLIEPGPIRTRFTDNV 187
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 32-226 1.19e-37

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


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 133.95  E-value: 1.19e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  32 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESG--STALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGL 109
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEAlaELAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFG--RLDIL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 110 INNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSKYAVEGFN 187
Cdd:cd05233   79 VNNAGI-ARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGgGRIVNISSVAGLRPLPGqAAYAASKAALEGLT 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 214010158 188 DSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAI 226
Cdd:cd05233  158 RSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKEL 196
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 26-232 2.06e-36

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: 131.06  E-value: 2.06e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVG 102
Cdd:COG1028    3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAaggRALAVAADVTDEAAVEALVAAAVAAFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 ekGLWGLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSK 180
Cdd:COG1028   83 --RLDILVNNAGITPP-GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGgGRIVNISSIAGLRGSPGqAAYAASK 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 214010158 181 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSP 232
Cdd:COG1028  160 AAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAARIP 211
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 27-216 5.08e-33

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: 122.31  E-value: 5.08e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  27 ITDKYIFITGCDSGFGNLAARTFDKKGFHVI-------------AACLTESGSTALkaetserlrTVLLDVTDPENVKRT 93
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVlsarreerleevkSECLELGAPSPH---------VVPLDMSDLEDAEQV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  94 AQWVKNQVGekGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIV 172
Cdd:cd05332   72 VEEALKLFG--GLDILINNAGI-SMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPhLIERSQGSIVVVSSIAGKIGVP 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 214010158 173 G-GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADP 216
Cdd:cd05332  149 FrTAYAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMN 193
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 30-211 1.18e-31

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


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 118.54  E-value: 1.18e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAAC-----LTESGSTaLKAETSERLRTVLLDVTDPENVKrtAQWVKNQVGEK 104
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLILTGrraerLQELADE-LGAKFPVKVLPLQLDVSDRESIE--AALENLPEEFR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 GLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYA 182
Cdd:cd05346   78 DIDILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPiMIARNQGHIINLGSIAGRYPYAGGNvYCATKAA 157

                        170       180
                 ....*....|....*....|....*....
gi 214010158 183 VEGFNDSLRRDMKAFGVHVSCIEPGLFKT 211
Cdd:cd05346  158 VRQFSLNLRKDLIGTGIRVTNIEPGLVET 186
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 34-309 1.22e-30

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 116.54  E-value: 1.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKGFHVIAaclteSGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwgLINNA 113
Cdd:PRK06179   9 VTGASSGIGRATAEKLARAGYRVFG-----TSRNPARAAPIPGVELLELDVTDDASVQAAVDEVIARAGRIDV--LVNNA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 114 GVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKA-QGRVINVSSVGGRL-AIVGGGYTPSKYAVEGFNDSLR 191
Cdd:PRK06179  82 GV-GLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQgSGRIINISSVLGFLpAPYMALYAASKHAVEGYSESLD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 192 RDMKAFGVHVSCIEPGLFKTNLadpvkviekklaiwEQLSPDIKQQYGEGYIEKSLDKLKGNKSYVNMDLSPVV-ECMDH 270
Cdd:PRK06179 161 HEVRQFGIRVSLVEPAYTKTNF--------------DANAPEPDSPLAEYDRERAVVSKAVAKAVKKADAPEVVaDTVVK 226

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 214010158 271 ALTSLFPKTHYAAGKDAKIFWIPLSHMPAALQDFLLLKQ 309
Cdd:PRK06179 227 AALGPWPKMRYTAGGQASLLSKLRRFMPAGAVDKSLRKT 265
PRK09291 PRK09291
SDR family oxidoreductase;
28-215 1.33e-30

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 115.87  E-value: 1.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  28 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSER---LRTVLLDVTDPENVKRTAQW---Vknqv 101
Cdd:PRK09291   1 MSKTILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRglaLRVEKLDLTDAIDRAQAAEWdvdV---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 102 gekglwgLINNAGV--PGVLAPtdwLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG-YT 177
Cdd:PRK09291  77 -------LLNNAGIgeAGAVVD---IPVELVRELFETNVFGPLELTQGFVRkMVARGKGKVVFTSSMAGLITGPFTGaYC 146

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 214010158 178 PSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 215
Cdd:PRK09291 147 ASKHALEAIAEAMHAELKPFGIQVATVNPGPYLTGFND 184
PRK05693 PRK05693
SDR family oxidoreductase;
32-214 1.24e-29

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 113.73  E-value: 1.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  32 IFITGCDSGFGNLAARTFDKKGFHVIAacltesgsTALKAETSERL-----RTVLLDVTDPENVKRTAQWVKNQVGekGL 106
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWA--------TARKAEDVEALaaagfTAVQLDVNDGAALARLAEELEAEHG--GL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 107 WGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAI-VGGGYTPSKYAVEG 185
Cdd:PRK05693  74 DVLINNAGY-GAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTpFAGAYCASKAAVHA 152

                        170       180
                 ....*....|....*....|....*....
gi 214010158 186 FNDSLRRDMKAFGVHVSCIEPGLFKTNLA 214
Cdd:PRK05693 153 LSDALRLELAPFGVQVMEVQPGAIASQFA 181
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 28-241 1.96e-29

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 113.21  E-value: 1.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  28 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEkgLW 107
Cdd:PRK08263   2 MEKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGR--LD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 108 GLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVGGG-YTPSKYAVEG 185
Cdd:PRK08263  80 IVVNNAGY-GLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRsGHIIQISSIGGISAFPMSGiYHASKWALEG 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 214010158 186 FNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSPDIKQQYGEG 241
Cdd:PRK08263 159 MSEALAQEVAEFGIKVTLVEPGGYSTDWAGTSAKRATPLDAYDTLREELAEQWSER 214
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 27-237 2.94e-29

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: 112.25  E-value: 2.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  27 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE-TSE--RLRTVLLDVTDPENVKRTAQWVKNQVGe 103
Cdd:cd08934    1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADElEAEggKALVLELDVTDEQQVDAAVERTVEALG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 104 kGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVK-KAQGRVINVSSVGGRLAIVG-GGYTPSKY 181
Cdd:cd08934   80 -RLDILVNNAGI-MLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLlRNKGTIVNISSVAGRVAVRNsAVYNATKF 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 214010158 182 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSPDIKQQ 237
Cdd:cd08934  158 GVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHITHTITKEAYEERISTIRKLQ 213
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 38-232 4.61e-29

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


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 111.37  E-value: 4.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158   38 DSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVL-LDVTDPENVKRTAQWVKNQVGekGLWGLINNAGV- 115
Cdd:pfam13561   5 ESGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAEELGAAVLpCDVTDEEQVEALVAAAVEKFG--RLDILVNNAGFa 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  116 PGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKaQGRVINVSSVGGRLAIVGGG-YTPSKYAVEGFNDSLRRDM 194
Cdd:pfam13561  83 PKLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKE-GGSIVNLSSIGAERVVPNYNaYGAAKAALEALTRYLAVEL 161

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 214010158  195 KAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSP 232
Cdd:pfam13561 162 GPRGIRVNAISPGPIKTLAASGIPGFDELLAAAEARAP 199
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 30-214 8.64e-29

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: 110.40  E-value: 8.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFH--VIAACLTESGSTALKAETSERL--RTVLLDVTDPENVKRTAQWVKNQVGekG 105
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPGtvILTARDVERGQAAVEKLRAEGLsvRFHQLDVTDDASIEAAADFVEEKYG--G 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIvggGYTPSKYAVE 184
Cdd:cd05324   79 LDILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPaGRIVNVSSGLGSLTS---AYGVSKAALN 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 214010158 185 GFNDSLRRDMKAFGVHVSCIEPGLFKTNLA 214
Cdd:cd05324  156 ALTRILAKELKETGIKVNACCPGWVKTDMG 185
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 27-214 2.41e-28

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


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 109.42  E-value: 2.41e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  27 ITDKYIFITGCDSGFGNLAARTFDKKGF-HVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNqvgekg 105
Cdd:cd05354    1 IKDKTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAAQAKD------ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKA-QGRVINVSSVGGRLAIVG-GGYTPSKYAV 183
Cdd:cd05354   75 VDVVINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANgGGAIVNLNSVASLKNFPAmGTYSASKSAA 154

                        170       180       190
                 ....*....|....*....|....*....|.
gi 214010158 184 EGFNDSLRRDMKAFGVHVSCIEPGLFKTNLA 214
Cdd:cd05354  155 YSLTQGLRAELAAQGTLVLSVHPGPIDTRMA 185
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 26-225 2.20e-27

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 107.20  E-value: 2.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTES-GSTALKAETSERLRTVLL---DVTDPENVKRTAQWVKNQV 101
Cdd:PRK05557   2 SLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEaGAEALVAEIGALGGKALAvqgDVSDAESVERAVDEAKAEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 102 GekGLWGLINNAGVpgvlapTDW-----LTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG 175
Cdd:PRK05557  82 G--GVDILVNNAGI------TRDnllmrMKEEDWDRVIDTNLTGVFNLTKAVARpMMKQRSGRIINISSVVGLMGNPGQA 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 214010158 176 -YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT--NLADPVKVIEKKLA 225
Cdd:PRK05557 154 nYAASKAGVIGFTKSLARELASRGITVNAVAPGFIETdmTDALPEDVKEAILA 206
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
28-212 2.69e-26

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 104.09  E-value: 2.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  28 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGek 104
Cdd:PRK05653   4 QGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAaggEARVLVFDVSDEAAVRALIEAAVEAFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 GLWGLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGlisvTLNML-----PLVKKAQGRVINVSSVGGRLAIVGGG-YTP 178
Cdd:PRK05653  82 ALDILVNNAGITRD-ALLPRMSEEDWDRVIDVNLTG----TFNVVraalpPMIKARYGRIVNISSVSGVTGNPGQTnYSA 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 214010158 179 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTN 212
Cdd:PRK05653 157 AKAGVIGFTKALALELASRGITVNAVAPGFIDTD 190
PRK07326 PRK07326
SDR family oxidoreductase;
25-215 4.16e-26

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 103.55  E-value: 4.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  25 EDITDKYIFITGCDSGFGNLAARTFDKKGFHV-IAACLTESGSTALKA-ETSERLRTVLLDVTDPENVKRTAQWVKNQVG 102
Cdd:PRK07326   2 MSLKGKVALITGGSKGIGFAIAEALLAEGYKVaITARDQKELEEAAAElNNKGNVLGLAADVRDEADVQRAVDAIVAAFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 ekGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGG-GYTPSKY 181
Cdd:PRK07326  82 --GLDVLIANAGV-GHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGTNFFAGGaAYNASKF 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 214010158 182 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 215
Cdd:PRK07326 159 GLVGFSEAAMLDLRQYGIKVSTIMPGSVATHFNG 192
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 29-221 5.31e-26

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: 103.10  E-value: 5.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE-------TSERLRTVLLDVTDPENVKRtaqwVKNQV 101
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEieaeanaSGQKVSYISADLSDYEEVEQ----AFAQA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 102 GEKGLWG--LINNAG--VPGVLapTDwLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GG 175
Cdd:cd08939   77 VEKGGPPdlVVNCAGisIPGLF--ED-LTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRpGHIVFVSSQAALVGIYGySA 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 214010158 176 YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT------NLADP--VKVIE 221
Cdd:cd08939  154 YCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTpgfeeeNKTKPeeTKAIE 207
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 30-215 8.27e-26

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


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 102.59  E-value: 8.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGL 109
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFG--GLDAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 110 INNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLN-MLPLVKKAQGRVINVSSVGGRLAIVGG-GYTPSKYAVEGFN 187
Cdd:cd08929   79 VNNAGV-GVMKPVEELTPEEWRLVLDTNLTGAFYCIHKaAPALLRRGGGTIVNVGSLAGKNAFKGGaAYNASKFGLLGLS 157

                        170       180
                 ....*....|....*....|....*...
gi 214010158 188 DSLRRDMKAFGVHVSCIEPGLFKTNLAD 215
Cdd:cd08929  158 EAAMLDLREANIRVVNVMPGSVDTGFAG 185
PRK05650 PRK05650
SDR family oxidoreductase;
32-215 9.68e-26

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 103.20  E-value: 9.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  32 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGekGLWG 108
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREaggDGFYQRCDVRDYSQLTALAQACEEKWG--GIDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAGVP--GVLAPtdwLTLEDYREPIEVNLFGLISVTLNMLPLVKKA-QGRVINVSSVGGRLAIVG-GGYTPSKYAVE 184
Cdd:PRK05650  81 IVNNAGVAsgGFFEE---LSLEDWDWQIAINLMGVVKGCKAFLPLFKRQkSGRIVNIASMAGLMQGPAmSSYNVAKAGVV 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 214010158 185 GFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 215
Cdd:PRK05650 158 ALSETLLVELADDEIGVHVVCPSFFQTNLLD 188
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 32-217 1.16e-25

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 102.37  E-value: 1.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  32 IFITGCDSGFGNLAARTF-DKKGFHVIAACLTESGSTALKAETSERLRTVL--LDVTDPenVKRTAQWVKNQVGEKGLWG 108
Cdd:cd05325    1 VLITGASRGIGLELVRQLlARGNNTVIATCRDPSAATELAALGASHSRLHIleLDVTDE--IAESAEAVAERLGDAGLDV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKA-QGRVINVSSVGGRLA-IVGGG---YTPSKYAV 183
Cdd:cd05325   79 LINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGaRAKIINISSRVGSIGdNTSGGwysYRASKAAL 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 214010158 184 EGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPV 217
Cdd:cd05325  159 NMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPF 192
PRK12826 PRK12826
SDR family oxidoreductase;
26-217 1.41e-25

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 102.30  E-value: 1.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALkAETSE----RLRTVLLDVTDPENVKRTAQWVKNQV 101
Cdd:PRK12826   3 DLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAAT-AELVEaaggKARARQVDVRDRAALKAAVAAGVEDF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 102 GekGLWGLINNAGVPGvLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGR-LAIVGG-GYTP 178
Cdd:PRK12826  82 G--RLDILVANAGIFP-LTPFAEMDDEQWERVIDVNLTGTFLLTQAALPaLIRAGGGRIVLTSSVAGPrVGYPGLaHYAA 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 214010158 179 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPV 217
Cdd:PRK12826 159 SKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNL 197
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 32-219 1.69e-25

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: 101.94  E-value: 1.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  32 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALK---AETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwg 108
Cdd:cd05339    2 VLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETAnnvRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTI-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAGVPGVLAPTDwLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYAVEGF 186
Cdd:cd05339   80 LINNAGVVSGKKLLE-LPDEEIEKTFEVNTLAHFWTTKAFLPdMLERNHGHIVTIASVAGLISPAGLAdYCASKAAAVGF 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 214010158 187 NDSLRRDMKAF---GVHVSCIEPGLFKTNLADPVKV 219
Cdd:cd05339  159 HESLRLELKAYgkpGIKTTLVCPYFINTGMFQGVKT 194
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 30-207 1.93e-25

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: 102.15  E-value: 1.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFG-NLAARTF--DKKGFHVIAACLTESGSTALKAETSER----LRTVLLDVTDPENVkrtAQWVkNQVG 102
Cdd:cd09806    1 TVVLITGCSSGIGlHLAVRLAsdPSKRFKVYATMRDLKKKGRLWEAAGALaggtLETLQLDVCDSKSV---AAAV-ERVT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 EKGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKK-AQGRVINVSSVGGRLAIVGGG-YTPSK 180
Cdd:cd09806   77 ERHVDVLVCNAGV-GLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRrGSGRILVTSSVGGLQGLPFNDvYCASK 155

                        170       180
                 ....*....|....*....|....*..
gi 214010158 181 YAVEGFNDSLRRDMKAFGVHVSCIEPG 207
Cdd:cd09806  156 FALEGLCESLAVQLLPFNVHLSLIECG 182
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 32-211 2.93e-25

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: 101.31  E-value: 2.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  32 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGEKGLWg 108
Cdd:cd05360    3 VVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRElggEAIAVVADVADAAQVERAADTAVERFGRIDTW- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 lINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIV-GGGYTPSKYAVEGF 186
Cdd:cd05360   82 -VNNAGV-AVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGgGALINVGSLLGYRSAPlQAAYSASKHAVRGF 159

                        170       180
                 ....*....|....*....|....*..
gi 214010158 187 NDSLRRDMKAFG--VHVSCIEPGLFKT 211
Cdd:cd05360  160 TESLRAELAHDGapISVTLVQPTAMNT 186
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 26-214 7.40e-25

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 101.17  E-value: 7.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTEsgstALKAETSERLRTVL---LDVTDPENVKRTAQWVKNQVG 102
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDE----ALAKETAAELGLVVggpLDVTDPASFAAFLDAVEADLG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 EKGLwgLINNAGV-P--GVLAPTDWLTledyREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG-YT 177
Cdd:PRK07825  78 PIDV--LVNNAGVmPvgPFLDEPDAVT----RRILDVNVYGVILGSKLAAPrMVPRGRGHVVNVASLAGKIPVPGMAtYC 151

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 214010158 178 PSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLA 214
Cdd:PRK07825 152 ASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELI 188
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
34-240 7.56e-25

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 100.23  E-value: 7.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGST----ALKAETSERLRTVLLDVTDPENVKRTaqwVKNQVGEKGLWG- 108
Cdd:PRK12824   7 VTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAkdwfEEYGFTEDQVRLKELDVTDTEECAEA---LAEIEEEEGPVDi 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAGVP--GVLAPtdwLTLEDYREPIEVNLFGLISVTLNMLPLVK-KAQGRVINVSSVGGRLAIVGG-GYTPSKYAVE 184
Cdd:PRK12824  84 LVNNAGITrdSVFKR---MSHQEWNDVINTNLNSVFNVTQPLFAAMCeQGYGRIINISSVNGLKGQFGQtNYSAAKAGMI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 214010158 185 GFNDSLRRDMKAFGVHVSCIEPGLFKTNLAdpvkviekklaiwEQLSPDIKQQYGE 240
Cdd:PRK12824 161 GFTKALASEGARYGITVNCIAPGYIATPMV-------------EQMGPEVLQSIVN 203
PRK06482 PRK06482
SDR family oxidoreductase;
33-214 9.52e-25

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 100.96  E-value: 9.52e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  33 FITGCDSGFGNLAARTFDKKGfHVIAACLTESGSTA-LKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwgLIN 111
Cdd:PRK06482   6 FITGASSGFGRGMTERLLARG-DRVAATVRRPDALDdLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAALGRIDV--VVS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 112 NAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYAVEGFNDS 189
Cdd:PRK06482  83 NAGY-GLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPhLRRQGGGRIVQVSSEGGQIAYPGFSlYHATKWGIEGFVEA 161

                        170       180
                 ....*....|....*....|....*
gi 214010158 190 LRRDMKAFGVHVSCIEPGLFKTNLA 214
Cdd:PRK06482 162 VAQEVAPFGIEFTIVEPGPARTNFG 186
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 30-218 1.59e-24

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


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 99.06  E-value: 1.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAET-SERLRTVLLDVTDPENVKRT-AQWVKNQVGekGLW 107
Cdd:cd08931    1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELgAENVVAGALDVTDRAAWAAAlADFAAATGG--RLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 108 GLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQG-RVINVSSVGG-----RLAIvgggYTPSKY 181
Cdd:cd08931   79 ALFNNAGV-GRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGaRVINTASSSAiygqpDLAV----YSATKF 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 214010158 182 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVK 218
Cdd:cd08931  154 AVRGLTEALDVEWARHGIRVADVWPWFVDTPILTKGE 190
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 26-276 2.16e-23

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 96.67  E-value: 2.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKG--FHVIAACLTESGSTALKAETSERLRTVLlDVTDPENVKRTAQWVKNQVGe 103
Cdd:PRK12829   8 PLDGLRVLVTGGASGIGRAIAEAFAEAGarVHVCDVSEAALAATAARLPGAKVTATVA-DVADPAQVERVFDTAVERFG- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 104 kGLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVK--KAQGRVINVSSVGGRLAIVGG-GYTPSK 180
Cdd:PRK12829  86 -GLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKasGHGGVIIALSSVAGRLGYPGRtPYAASK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 181 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVkviekklaiweqlSPDIKQQYGEGYIEKSLDKLKGnksyvnMD 260
Cdd:PRK12829 165 WAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRV-------------IEARAQQLGIGLDEMEQEYLEK------IS 225

                        250
                 ....*....|....*.
gi 214010158 261 LSPVVECMDHALTSLF 276
Cdd:PRK12829 226 LGRMVEPEDIAATALF 241
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 26-213 3.93e-23

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: 95.61  E-value: 3.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGnLA-ARTFDKKGFHVIAACLTESGSTALKAETsERLRTVLLDVTDPENVKRTAQWVKNQVGEk 104
Cdd:COG3967    2 KLTGNTILITGGTSGIG-LAlAKRLHARGNTVIITGRREEKLEEAAAAN-PGLHTIVLDVADPASIAALAEQVTAEFPD- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 gLWGLINNAgvpGVLAPTDWL----TLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVggrLAIVGGGYTP- 178
Cdd:COG3967   79 -LNVLINNA---GIMRAEDLLdeaeDLADAEREITTNLLGPIRLTAAFLPhLKAQPEAAIVNVSSG---LAFVPLAVTPt 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 214010158 179 ---SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:COG3967  152 ysaTKAALHSYTQSLRHQLKDTSVKVIELAPPAVDTDL 189
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 25-227 4.65e-23

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 95.41  E-value: 4.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  25 EDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTEsgstalKAETSERLRTVLLDVTDPenVKRTAQWVKnQVGEk 104
Cdd:PRK06550   1 QEFMTKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQD------KPDLSGNFHFLQLDLSDD--LEPLFDWVP-SVDI- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 glwgLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAivGGG---YTPSK 180
Cdd:PRK06550  71 ----LCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPqMLERKSGIIINMCSIASFVA--GGGgaaYTASK 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 214010158 181 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT--NLADpvkVIEKKLAIW 227
Cdd:PRK06550 145 HALAGFTKQLALDYAKDGIQVFGIAPGAVKTpmTAAD---FEPGGLADW 190
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 32-218 6.38e-23

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


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 95.09  E-value: 6.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  32 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGekGLWG 108
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNpnpSVEVEILDVTDEERNQLVIAELEAELG--GLDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGG-GYTPSKYAVEGF 186
Cdd:cd05350   79 VIINAGV-GKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPqFRAKGRGHLVLISSVAALRGLPGAaAYSASKAALSSL 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 214010158 187 NDSLRRDMKAFGVHVSCIEPGLFKTNLADPVK 218
Cdd:cd05350  158 AESLRYDVKKRGIRVTVINPGFIDTPLTANMF 189
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 25-214 6.62e-23

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 95.14  E-value: 6.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  25 EDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQV 101
Cdd:PRK07666   3 QSLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAygvKVVIATADVSDYEEVTAAIEQLKNEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 102 GEKGLwgLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGG-RLAIVGGGYTPS 179
Cdd:PRK07666  83 GSIDI--LINNAGI-SKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPsMIERQSGDIINISSTAGqKGAAVTSAYSAS 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 214010158 180 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLA 214
Cdd:PRK07666 160 KFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMA 194
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 32-208 7.18e-23

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 95.21  E-value: 7.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  32 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRT-----AQWVKNQVgekgl 106
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMlaslpAEWRNIDV----- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 107 wgLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYAVE 184
Cdd:PRK10538  78 --LVNNAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPgMVERNHGHIINIGSTAGSWPYAGGNvYGATKAFVR 155

                        170       180
                 ....*....|....*....|....
gi 214010158 185 GFNDSLRRDMKAFGVHVSCIEPGL 208
Cdd:PRK10538 156 QFSLNLRTDLHGTAVRVTDIEPGL 179
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 29-213 9.02e-23

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: 95.37  E-value: 9.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE-----TSERLRTVLLDVTDPENVKRTAQWVKNQVGE 103
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEikketGNAKVEVIQLDLSSLASVRQFAEEFLARFPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 104 kgLWGLINNAgvpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKK-AQGRVINVSSVGGRLAIVGG-----GYT 177
Cdd:cd05327   81 --LDILINNA---GIMAPPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKAsAPSRIVNVSSIAHRAGPIDFndldlENN 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 214010158 178 PSKYAVEGFNDS----------LRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:cd05327  156 KEYSPYKAYGQSklanilftreLARRLEGTGVTVNALHPGVVRTEL 201
PRK06181 PRK06181
SDR family oxidoreductase;
29-213 9.30e-23

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 95.05  E-value: 9.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVL---LDVTDPENVKRTAQWVKNQVGekG 105
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALvvpTDVSDAEACERLIEAAVARFG--G 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LWGLINNAGVpGVLAPTDWLT-LEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVG-GGYTPSKYAV 183
Cdd:PRK06181  79 IDILVNNAGI-TMWSRFDELTdLSVFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTrSGYAASKHAL 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 214010158 184 EGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK06181 158 HGFFDSLRIELADDGVAVTVVCPGFVATDI 187
PRK08267 PRK08267
SDR family oxidoreductase;
30-301 1.98e-22

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 94.23  E-value: 1.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE-TSERLRTVLLDVTDPenvkrtAQWvKNQVGEKGLWG 108
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAElGAGNAWTGALDVTDR------AAW-DAALADFAAAT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 ------LINNAGVP--GVLAPTDwltLEDYREPIEVNLFGLISVTLNMLPLVKKAQG-RVINVSSVGG-----RLAIvgg 174
Cdd:PRK08267  75 ggrldvLFNNAGILrgGPFEDIP---LEAHDRVIDINVKGVLNGAHAALPYLKATPGaRVINTSSASAiygqpGLAV--- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 175 gYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADpvkviekklaiweqlspdikqQYGEGYIEKSLDKLkgnk 254
Cdd:PRK08267 149 -YSATKFAVRGLTEALDLEWRRHGIRVADVMPLFVDTAMLD---------------------GTSNEVDAGSTKRL---- 202

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 214010158 255 syvNMDLSP------VVECMDHAltslfPKTHYAAGKDAKIFWIPLSHMPAAL 301
Cdd:PRK08267 203 ---GVRLTPedvaeaVWAAVQHP-----TRLHWPVGKQAKLLAFLARLSPGFV 247
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 30-225 2.12e-22

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: 93.38  E-value: 2.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE---TSERLRTVLLDVTDPENVKRTAQWVKNQVGekGL 106
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEikaLGGNAAALEADVSDREAVEALVEKVEAEFG--PV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 107 WGLINNAGVpgvlapT-DWL----TLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPS 179
Cdd:cd05333   79 DILVNNAGI------TrDNLlmrmSEEDWDAVINVNLTGVFNVTQAVIRaMIKRRSGRIINISSVVGLIGNPGqANYAAS 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 214010158 180 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD--PVKVIEKKLA 225
Cdd:cd05333  153 KAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDalPEKVKEKILK 200
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 27-211 2.33e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 95.37  E-value: 2.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  27 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGE 103
Cdd:PRK07109   6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAaggEALAVVADVADAEAVQAAADRAEEELGP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 104 KGLWglINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAI-VGGGYTPSKY 181
Cdd:PRK07109  86 IDTW--VNNAMV-TVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRhMRPRDRGAIIQVGSALAYRSIpLQSAYCAAKH 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 214010158 182 AVEGFNDSLRRDMKAFG--VHVSCIEPGLFKT 211
Cdd:PRK07109 163 AIRGFTDSLRCELLHDGspVSVTMVQPPAVNT 194
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 26-217 6.76e-22

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: 92.42  E-value: 6.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLT-ESGSTALKAETSE--RLRTVLLDVTDPENVKRTAQWVKNQVG 102
Cdd:cd05347    2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNeEKAEEAQQLIEKEgvEATAFTCDVSDEEAIKAAVEAIEEDFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 EKGLwgLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVggrLAIVGG----GYT 177
Cdd:cd05347   82 KIDI--LVNNAGI-IRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARhMIKQGHGKIINICSL---LSELGGppvpAYA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 214010158 178 PSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPV 217
Cdd:cd05347  156 ASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTEAV 195
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 30-221 1.25e-21

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 91.57  E-value: 1.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAAclteSGSTALKAETSERLR-------TVLLDVTDPENVKRTAQWVKNQVG 102
Cdd:PRK12939   8 KRALVTGAARGLGAAFAEALAEAGATVAFN----DGLAAEARELAAALEaaggrahAIAADLADPASVQRFFDAAAAALG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 ekGLWGLINNAGVPgVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSS-VGGRLAIVGGGYTPSK 180
Cdd:PRK12939  84 --GLDGLVNNAGIT-NSKSATELDIDTWDAVMNVNVRGTFLMLRAALPhLRDSGRGRIVNLASdTALWGAPKLGAYVASK 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 214010158 181 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIE 221
Cdd:PRK12939 161 GAVIGMTRSLARELGGRGITVNAIAPGLTATEATAYVPADE 201
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 26-215 1.69e-21

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: 91.29  E-value: 1.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekG 105
Cdd:cd05341    2 RLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFG--R 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKA-QGRVINVSSVGGRLAIVG-GGYTPSKYAV 183
Cdd:cd05341   80 LDVLVNNAGI-LTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAgGGSIINMSSIEGLVGDPAlAAYNASKGAV 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 214010158 184 EGFNDSLRRDM--KAFGVHVSCIEPGLFKTNLAD 215
Cdd:cd05341  159 RGLTKSAALECatQGYGIRVNSVHPGYIYTPMTD 192
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 30-208 4.57e-21

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 90.31  E-value: 4.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACL-TESGSTALKAE---TSERLRTVLLDVTDPENVKRTAQWVKNQVGekG 105
Cdd:PRK12825   7 RVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEAveaLGRRAQAVQADVTDKAALEAAVAAAVERFG--R 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LWGLINNAGVpgvlapTDW-----LTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTP 178
Cdd:PRK12825  85 IDILVNNAGI------FEDkpladMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRgGRIVNISSVAGLPGWPGrSNYAA 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 214010158 179 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGL 208
Cdd:PRK12825 159 AKAGLVGLTKALARELAEYGITVNMVAPGD 188
PRK08264 PRK08264
SDR family oxidoreductase;
26-215 9.87e-21

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 88.79  E-value: 9.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTAlkaETSERLRTVLLDVTDPENVKRTAQwvknQVGEKG 105
Cdd:PRK08264   3 DIKGKVVLVTGANRGIGRAFVEQLLARGAAKVYAAARDPESVT---DLGPRVVPLQLDVTDPASVAAAAE----AASDVT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LwgLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAI-VGGGYTPSKYAV 183
Cdd:PRK08264  76 I--LVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPvLAANGGGAIVNVLSVLSWVNFpNLGTYSASKAAA 153

                        170       180       190
                 ....*....|....*....|....*....|..
gi 214010158 184 EGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 215
Cdd:PRK08264 154 WSLTQALRAELAPQGTRVLGVHPGPIDTDMAA 185
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 26-213 9.95e-20

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: 86.21  E-value: 9.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSErLRTVLLDVTDPENVKRTAQWVKNQVGEkg 105
Cdd:cd05370    2 KLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN-IHTIVLDVGDAESVEALAEALLSEYPN-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LWGLINNAGVP---GVLAPTDwlTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVggrLAIV----GGGYT 177
Cdd:cd05370   79 LDILINNAGIQrpiDLRDPAS--DLDKADTEIDTNLIGPIRLIKAFLPhLKKQPEATIVNVSSG---LAFVpmaaNPVYC 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 214010158 178 PSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:cd05370  154 ATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTEL 189
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 28-211 1.79e-19

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


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 86.04  E-value: 1.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  28 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE-----RLRTVLLDVTDPENVKRTAQWVKNQVG 102
Cdd:cd05330    2 KDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEiapdaEVLLIKADVSDEAQVEAYVDATVEQFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 EkgLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSK 180
Cdd:cd05330   82 R--IDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGsGMIVNTASVGGIRGVGNqSGYAAAK 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 214010158 181 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT 211
Cdd:cd05330  160 HGVVGLTRNSAVEYGQYGIRINAIAPGAILT 190
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 29-213 1.02e-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: 83.61  E-value: 1.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVI-----AACLTESGSTALKAETSE-RLRTVLLDVTDPENVKRTAQWVKNQVG 102
Cdd:cd05364    3 GKVAIITGSSSGIGAGTAILFARLGARLAltgrdAERLEETRQSCLQAGVSEkKILLVVADLTEEEGQDRIISTTLAKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 EkgLWGLINNAGVPGVLAPTDwLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGG-GYTPSKY 181
Cdd:cd05364   83 R--LDILVNNAGILAKGGGED-QDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGRSFPGVlYYCISKA 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 214010158 182 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:cd05364  160 ALDQFTRCTALELAPKGVRVNSVSPGVIVTGF 191
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
20-215 1.39e-18

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 83.70  E-value: 1.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  20 GKLkiediTDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLR--TVLLDVTDPENVKRTAQWV 97
Cdd:PRK08226   2 GKL-----TGKTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADELCGRGHRctAVVADVRDPASVAAAIKRA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  98 KNQVGEKGLwgLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGG-- 174
Cdd:PRK08226  77 KEKEGRIDI--LVNNAGV-CRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPeMIARKDGRIVMMSSVTGDMVADPGet 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 214010158 175 GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 215
Cdd:PRK08226 154 AYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAE 194
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 29-231 1.64e-18

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: 83.35  E-value: 1.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSER----LRTVLLDVTDPENVKRTAQWVKNQVGEk 104
Cdd:cd08933    9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAgpgsCKFVPCDVTKEEDIKTLISVTVERFGR- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 gLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVggrLAIVG----GGYTPSK 180
Cdd:cd08933   88 -IDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSL---VGSIGqkqaAPYVATK 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 214010158 181 YAVEGFNDSLRRDMKAFGVHVSCIEPGlfktNLADPvkviekklaIWEQLS 231
Cdd:cd08933  164 GAITAMTKALAVDESRYGVRVNCISPG----NIWTP---------LWEELA 201
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 25-223 2.86e-18

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 82.20  E-value: 2.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  25 EDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAAC-LTESGSTALKAETSERLRTVLL---DVTDPENVKRTAQWVKNQ 100
Cdd:PRK05565   1 MKLMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYdINEEAAQELLEEIKEEGGDAIAvkaDVSSEEDVENLVEQIVEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 101 VGekGLWGLINNAGVPGVLAPTDwLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRL-AIVGGGYTP 178
Cdd:PRK05565  81 FG--KIDILVNNAGISNFGLVTD-MTDEEWDRVIDVNLTGVMLLTRYALPyMIKRKSGVIVNISSIWGLIgASCEVLYSA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 214010158 179 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKK 223
Cdd:PRK05565 158 SKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKE 202
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 34-213 3.23e-18

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: 82.35  E-value: 3.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKGFHVIAACLTES--GSTALKA-ETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGLI 110
Cdd:cd05323    5 ITGGASGIGLATAKLLLKKGAKVAILDRNENpgAAAELQAiNPKVKATFVQCDVTSWEQLAAAFKKAIEKFG--RVDILI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 111 NNAgvpGVLAPTDWLTLEDYREPIE----VNLFGLISVTLNMLPLVKKAQ----GRVINVSSVGG----RLAIVgggYTP 178
Cdd:cd05323   83 NNA---GILDEKSYLFAGKLPPPWEktidVNLTGVINTTYLALHYMDKNKggkgGVIVNIGSVAGlypaPQFPV---YSA 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 214010158 179 SKYAVEGFNDSLRRDMKA-FGVHVSCIEPGLFKTNL 213
Cdd:cd05323  157 SKHGVVGFTRSLADLLEYkTGVRVNAICPGFTNTPL 192
PRK07832 PRK07832
SDR family oxidoreductase;
30-219 3.85e-18

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 82.40  E-value: 3.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIaacLTESGSTALkAETSERLR----TVL----LDVTDPENVKRTAQWVKNQV 101
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELF---LTDRDADGL-AQTVADARalggTVPehraLDISDYDAVAAFAADIHAAH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 102 GEKGLwgLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGR-VINVSSVGGRLAIV-GGGYTP 178
Cdd:PRK07832  77 GSMDV--VMNIAGI-SAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPpMVAAGRGGhLVNVSSAAGLVALPwHAAYSA 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 214010158 179 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKV 219
Cdd:PRK07832 154 SKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVNTVEI 194
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 33-228 4.52e-18

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


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 82.20  E-value: 4.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  33 FITGCDSGFGNLAARTFDKKGFHV-IAACLTESGSTALKAETSERLRT--VLLDVTDPENVKRTAQWVKNQVGEKGLwgL 109
Cdd:cd08945    7 LVTGATSGIGLAIARRLGKEGLRVfVCARGEEGLATTVKELREAGVEAdgRTCDVRSVPEIEALVAAAVARYGPIDV--L 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 110 INNAGVPGVLAPTDwLTLEDYREPIEVNLFGLISVTLNMLP---LVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYAVEG 185
Cdd:cd08945   85 VNNAGRSGGGATAE-LADELWLDVVETNLTGVFRVTKEVLKaggMLERGTGRIINIASTGGKQGVVHAApYSASKHGVVG 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 214010158 186 FNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKviEKKLAIWE 228
Cdd:cd08945  164 FTKALGLELARTGITVNAVCPGFVETPMAASVR--EHYADIWE 204
PRK09072 PRK09072
SDR family oxidoreductase;
26-201 4.61e-18

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 82.30  E-value: 4.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETS--ERLRTVLLDVTDPENVKRTAQwVKNQVGe 103
Cdd:PRK09072   2 DLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPypGRHRWVVADLTSEAGREAVLA-RAREMG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 104 kGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSKY 181
Cdd:PRK09072  80 -GINVLINNAGV-NHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPsAMVVNVGSTFGSIGYPGyASYCASKF 157

                        170       180
                 ....*....|....*....|
gi 214010158 182 AVEGFNDSLRRDMKAFGVHV 201
Cdd:PRK09072 158 ALRGFSEALRRELADTGVRV 177
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 28-221 7.27e-18

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: 81.57  E-value: 7.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  28 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTES-GSTALKAEtsERLRTVLLDVTDPENVKRTAQWVKNQVGEkgL 106
Cdd:cd05371    1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSpGETVAKLG--DNCRFVPVDVTSEKDVKAALALAKAKFGR--L 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 107 WGLINNAGVpGVLAPTDWL------TLEDYREPIEVNLFGlisvTLNMLPLVKKAQGR-----------VINVSSVGGRL 169
Cdd:cd05371   77 DIVVNCAGI-AVAAKTYNKkgqqphSLELFQRVINVNLIG----TFNVIRLAAGAMGKnepdqggergvIINTASVAAFE 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 214010158 170 AIVG-GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL--ADPVKVIE 221
Cdd:cd05371  152 GQIGqAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLlaGLPEKVRD 206
PRK07454 PRK07454
SDR family oxidoreductase;
33-215 1.01e-17

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 80.77  E-value: 1.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  33 FITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwgL 109
Cdd:PRK07454  10 LITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRStgvKAAAYSIDLSNPEAIAPGIAELLEQFGCPDV--L 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 110 INNAGVP--GVLAPTDwltLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSKYAVEG 185
Cdd:PRK07454  88 INNAGMAytGPLLEMP---LSDWQWVIQLNLTSVFQCCSAVLPGMRARGgGLIINVSSIAARNAFPQwGAYCVSKAALAA 164

                        170       180       190
                 ....*....|....*....|....*....|
gi 214010158 186 FNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 215
Cdd:PRK07454 165 FTKCLAEEERSHGIRVCTITLGAVNTPLWD 194
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
27-225 1.09e-17

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 80.83  E-value: 1.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  27 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLL----DVTDPENVKRTAQWVKNQVG 102
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRRVKWLEDQKALGFDFIasegNVGDWDSTKAAFDKVKAEVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 EKGLwgLINNAGVPGVLAPTDwLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPSK 180
Cdd:PRK12938  81 EIDV--LVNNAGITRDVVFRK-MTREDWTAVIDTNLTSLFNVTKQVIDgMVERGWGRIINISSVNGQKGQFGqTNYSTAK 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 214010158 181 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVK--VIEKKLA 225
Cdd:PRK12938 158 AGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRpdVLEKIVA 204
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 30-214 1.34e-17

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: 80.10  E-value: 1.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAEtSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGL 109
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS-GGDVEAVPYDARDPEDARALVDALRDRFG--RIDVL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 110 INNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPSKYAVEGFN 187
Cdd:cd08932   78 VHNAGI-GRPTTLREGSDAELEAHFSINVIAPAELTRALLPaLREAGSGRVVFLNSLSGKRVLAGnAGYSASKFALRALA 156

                        170       180
                 ....*....|....*....|....*..
gi 214010158 188 DSLRRDMKAFGVHVSCIEPGLFKTNLA 214
Cdd:cd08932  157 HALRQEGWDHGVRVSAVCPGFVDTPMA 183
PRK08589 PRK08589
SDR family oxidoreductase;
27-215 1.69e-17

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 80.59  E-value: 1.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  27 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKA--ETSERLRTVLLDVTDPENVKRTAQWVKNQVGEK 104
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDKikSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 GLwgLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLA-IVGGGYTPSKYAV 183
Cdd:PRK08589  84 DV--LFNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAAdLYRSGYNAAKGAV 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 214010158 184 EGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 215
Cdd:PRK08589 162 INFTKSIAIEYGRDGIRANAIAPGTIETPLVD 193
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 30-211 2.29e-17

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


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 79.82  E-value: 2.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTEsgsTALK-AETSERLRTVLLDVTDPENVKRTAQwvknqvGEKGLWG 108
Cdd:cd05368    3 KVALITAAAQGIGRAIALAFAREGANVIATDINE---EKLKeLERGPGITTRVLDVTDKEQVAALAK------EEGRIDV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAGV---PGVLAPTDwltlEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGG--GYTPSKYA 182
Cdd:cd05368   74 LFNCAGFvhhGSILDCED----DDWDFAMNLNVRSMYLMIKAVLPkMLARKDGSIINMSSVASSIKGVPNrfVYSTTKAA 149

                        170       180
                 ....*....|....*....|....*....
gi 214010158 183 VEGFNDSLRRDMKAFGVHVSCIEPGLFKT 211
Cdd:cd05368  150 VIGLTKSVAADFAQQGIRCNAICPGTVDT 178
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 26-213 3.79e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 79.32  E-value: 3.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKG 105
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRID 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LwgLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLI----SVTLNMLplvKKAQGRVINVSSVGGRLAIVGG-GYTPSK 180
Cdd:PRK06841  92 I--LVNSAGV-ALLAPAEDVSEEDWDKTIDINLKGSFlmaqAVGRHMI---AAGGGKIVNLASQAGVVALERHvAYCASK 165

                        170       180       190
                 ....*....|....*....|....*....|...
gi 214010158 181 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK06841 166 AGVVGMTKVLALEWGPYGITVNAISPTVVLTEL 198
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 30-211 1.73e-16

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: 77.50  E-value: 1.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACL-TESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwg 108
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYrSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDT-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAGVPGVLAP-----TDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKA-QGRVINVSSVGGRLAIVG-GGYTPSKY 181
Cdd:cd05349   79 IVNNALIDFPFDPdqrktFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERgSGRVINIGTNLFQNPVVPyHDYTTAKA 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 214010158 182 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKT 211
Cdd:cd05349  159 ALLGFTRNMAKELGPYGITVNMVSGGLLKV 188
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 29-213 4.77e-16

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 76.06  E-value: 4.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVIaacltesgstaLKAETSERLRTV------------------LLDVTdPENV 90
Cdd:PRK08945  12 DRIILVTGAGDGIGREAALTYARHGATVI-----------LLGRTEEKLEAVydeieaaggpqpaiipldLLTAT-PQNY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  91 KRTAQWVKNQVGEkgLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRL 169
Cdd:PRK08945  80 QQLADTIEEQFGR--LDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPaASLVFTSSSVGRQ 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 214010158 170 AIVG-GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK08945 158 GRANwGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAM 202
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 27-213 4.77e-16

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 76.32  E-value: 4.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  27 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIaacLTESGSTALKAETSE-------RLRTVLLDVTDPENVKRTAQWVKN 99
Cdd:PRK12937   3 LSNKVAIVTGASRGIGAAIARRLAADGFAVA---VNYAGSAAAADELVAeieaaggRAIAVQADVADAAAVTRLFDAAET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 100 QVGekGLWGLINNAGVPGvLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAqGRVINVSSVGGRLAIVGGG-YTP 178
Cdd:PRK12937  80 AFG--RIDVLVNNAGVMP-LGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQG-GRIINLSTSVIALPLPGYGpYAA 155

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 214010158 179 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK12937 156 SKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL 190
PRK07774 PRK07774
SDR family oxidoreductase;
25-211 7.24e-16

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 75.94  E-value: 7.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  25 EDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVL---LDVTDPENVKRTAQWVKNQV 101
Cdd:PRK07774   2 GRFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIavqVDVSDPDSAKAMADATVSAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 102 GekGLWGLINNAGVPGVLAPTDWLT--LEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAivGGGYTP 178
Cdd:PRK07774  82 G--GIDYLVNNAAIYGGMKLDLLITvpWDYYKKFMSVNLDGALVCTRAVYKhMAKRGGGAIVNQSSTAAWLY--SNFYGL 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 214010158 179 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT 211
Cdd:PRK07774 158 AKVGLNGLTQQLARELGGMNIRVNAIAPGPIDT 190
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 29-214 1.41e-15

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 74.80  E-value: 1.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRT-VLLDVTDPENVKRTAQWVKNQVGEkgLW 107
Cdd:cd05326    4 GKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISfVHCDVTVEADVRAAVDTAVARFGR--LD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 108 GLINNAGVPGvlAPTDWL---TLEDYREPIEVNLFGLISVTLN----MLPlvkKAQGRVINVSSVGGrlaIVGGG----Y 176
Cdd:cd05326   82 IMFNNAGVLG--APCYSIletSLEEFERVLDVNVYGAFLGTKHaarvMIP---AKKGSIVSVASVAG---VVGGLgphaY 153

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 214010158 177 TPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLA 214
Cdd:cd05326  154 TASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLL 191
FabG-like PRK07231
SDR family oxidoreductase;
26-242 1.85e-15

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 74.48  E-value: 1.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE--TSERLRTVLLDVTDPENVKRTAQWVKNQVGe 103
Cdd:PRK07231   2 RLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEilAGGRAIAVAADVSDEADVEAAVAAALERFG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 104 kGLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKA-QGRVINVSSVGG-RLAIVGGGYTPSKY 181
Cdd:PRK07231  81 -SVDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEgGGAIVNVASTAGlRPRPGLGWYNASKG 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 214010158 182 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADpvkviekklAIWEQLSPDIKQQYGEGY 242
Cdd:PRK07231 160 AVITLTKALAAELGPDKIRVNAVAPVVVETGLLE---------AFMGEPTPENRAKFLATI 211
PRK08219 PRK08219
SDR family oxidoreductase;
34-207 1.98e-15

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 74.20  E-value: 1.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFdKKGFHVIAAClTESGSTALKAETSERLRTVLLDVTDPENVkrtaQWVKNQVGEkgLWGLINNA 113
Cdd:PRK08219   8 ITGASRGIGAAIAREL-APTHTLLLGG-RPAERLDELAAELPGATPFPVDLTDPEAI----AAAVEQLGR--LDVLVHNA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 114 GVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYAVEGFNDSLRR 192
Cdd:PRK08219  80 GV-ADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRANPGWGsYAASKFALRALADALRE 158

                        170
                 ....*....|....*
gi 214010158 193 DmKAFGVHVSCIEPG 207
Cdd:PRK08219 159 E-EPGNVRVTSVHPG 172
PRK09242 PRK09242
SDR family oxidoreductase;
29-225 2.03e-15

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 74.78  E-value: 2.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVI----AACLTESGSTALKAETSER-LRTVLLDVTDPENVKRTAQWVKNQVGe 103
Cdd:PRK09242   9 GQTALITGASKGIGLAIAREFLGLGADVLivarDADALAQARDELAEEFPEReVHGLAADVSDDEDRRAILDWVEDHWD- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 104 kGLWGLINNAGVPGVLAPTDWlTLEDYREPIEVNLFGLISVTLNMLPLVKK-AQGRVINVSSVGGrLAIVGGG--YTPSK 180
Cdd:PRK09242  88 -GLHILVNNAGGNIRKAAIDY-TEDEWRGIFETNLFSAFELSRYAHPLLKQhASSAIVNIGSVSG-LTHVRSGapYGMTK 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 214010158 181 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLA 225
Cdd:PRK09242 165 AALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDYYE 209
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 20-213 2.10e-15

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 74.43  E-value: 2.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  20 GKLKieditDKYIFITGCDSGFGNLAARTFDKKGFHV-IAACLTESGSTALKAETSErlrTVLLDVTDPENVKRTAQWVK 98
Cdd:PRK06463   3 MRFK-----GKVALITGGTRGIGRAIAEAFLREGAKVaVLYNSAENEAKELREKGVF---TIKCDVGNRDQVKKSKEVVE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  99 NQVGEKGLwgLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGG-RLAIVGGG- 175
Cdd:PRK06463  75 KEFGRVDV--LVNNAGI-MYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKnGAIVNIASNAGiGTAAEGTTf 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 214010158 176 YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK06463 152 YAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDM 189
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 26-215 2.63e-15

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 74.18  E-value: 2.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekG 105
Cdd:PRK12936   3 DLSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEADLE--G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LWGLINNAGVPgvlapTDWLTL----EDYREPIEVNLFGLISVTLNML-PLVKKAQGRVINVSSVGGRLAIVG-GGYTPS 179
Cdd:PRK12936  81 VDILVNNAGIT-----KDGLFVrmsdEDWDSVLEVNLTATFRLTRELThPMMRRRYGRIINITSVVGVTGNPGqANYCAS 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 214010158 180 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 215
Cdd:PRK12936 156 KAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTG 191
PRK07201 PRK07201
SDR family oxidoreductase;
30-188 3.05e-15

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 76.14  E-value: 3.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTaqwVKNQVGEKGl 106
Cdd:PRK07201 372 KVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAkggTAHAYTCDLTDSAAVDHT---VKDILAEHG- 447

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 107 wG---LINNAGVP---GVLAPTDwlTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVG-----GRLAivgg 174
Cdd:PRK07201 448 -HvdyLVNNAGRSirrSVENSTD--RFHDYERTMAVNYFGAVRLILGLLPhMRERRFGHVVNVSSIGvqtnaPRFS---- 520

                        170
                 ....*....|....
gi 214010158 175 GYTPSKYAVEGFND 188
Cdd:PRK07201 521 AYVASKAALDAFSD 534
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 26-218 5.60e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 73.21  E-value: 5.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSErlRTVLLDVTDPEnvkrtaqWVKNQVGEKG 105
Cdd:PRK07060   6 DFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGC--EPLRLDVGDDA-------AIRAALAAAG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LW-GLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ--GRVINVSSVGGRLAIVGG-GYTPSKY 181
Cdd:PRK07060  77 AFdGLVNCAGI-ASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGrgGSIVNVSSQAALVGLPDHlAYCASKA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 214010158 182 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLA-----DPVK 218
Cdd:PRK07060 156 ALDAITRVLCVELGPHGIRVNSVNPTVTLTPMAaeawsDPQK 197
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 26-211 9.43e-15

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 72.52  E-value: 9.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTES-GSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGek 104
Cdd:PRK12828   4 SLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAApLSQTLPGVPADALRIGGIDLVDPQAARRAVDEVNRQFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 GLWGLINNAG--VPGVLAPtdwLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPSK 180
Cdd:PRK12828  82 RLDALVNIAGafVWGTIAD---GDADTWDRMYGVNVKTTLNASKAALPaLTASGGGRIVNIGAGAALKAGPGmGAYAAAK 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 214010158 181 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT 211
Cdd:PRK12828 159 AGVARLTEALAAELLDRGITVNAVLPSIIDT 189
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 30-242 1.22e-14

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: 72.48  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVI------AACLtESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGe 103
Cdd:cd08940    3 KVALVTGSTSGIGLGIARALAAAGANIVlngfgdAAEI-EAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 104 kGLWGLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSKY 181
Cdd:cd08940   81 -GVDILVNNAGIQHV-APIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGwGRIINIASVHGLVASANkSAYVAAKH 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 214010158 182 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLadpvkvIEKKLaiweqlsPDIKQQYGEGY 242
Cdd:cd08940  159 GVVGLTKVVALETAGTGVTCNAICPGWVLTPL------VEKQI-------SALAQKNGVPQ 206
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 27-211 1.36e-14

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


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 71.84  E-value: 1.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  27 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESG----STALKAETSERLRTVLLDVTD--PENVKRTAQWVKNQ 100
Cdd:cd05340    2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKlrqvADHINEEGGRQPQWFILDLLTctSENCQQLAQRIAVN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 101 VGEkgLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKK--AQGRVINVSSVGGRLAIVGGGYTP 178
Cdd:cd05340   82 YPR--LDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKsdAGSLVFTSSSVGRQGRANWGAYAV 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 214010158 179 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT 211
Cdd:cd05340  160 SKFATEGL*QVLADEYQQRNLRVNCINPGGTRT 192
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 33-211 1.73e-14

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: 71.61  E-value: 1.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  33 FITGCDSGFGNLAARTFDKKGFHVIAACL-TESGSTALKAETSERLRTVLL---DVTDPENVKRTAQWVKNQVGekGLWG 108
Cdd:cd05359    2 LVTGGSRGIGKAIALRLAERGADVVINYRkSKDAAAEVAAEIEELGGKAVVvraDVSQPQDVEEMFAAVKERFG--RLDV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAGvPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVggGYTP---SKYAVE 184
Cdd:cd05359   80 LVSNAA-AGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGgGRIVAISSLGSIRALP--NYLAvgtAKAALE 156

                        170       180
                 ....*....|....*....|....*..
gi 214010158 185 GFNDSLRRDMKAFGVHVSCIEPGLFKT 211
Cdd:cd05359  157 ALVRYLAVELGPRGIRVNAVSPGVIDT 183
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 31-212 1.75e-14

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: 71.55  E-value: 1.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  31 YIFITGCDSGFGNLAARTFDKKGFHVIAACLTESgSTALKAETSE-----RLRTVLLDVTDPENVKRTAQWVKNQVGEkg 105
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARS-EEPLQELKEElrpglRVTTVKADLSDAAGVEQLLEAIRKLDGE-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKK--AQGRVINVSSVGGRLAIVG-GGYTPSKYA 182
Cdd:cd05367   78 RDLLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKrgLKKTVVNVSSGAAVNPFKGwGLYCSSKAA 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 214010158 183 VegfnDSLRRDMKA--FGVHVSCIEPGLFKTN 212
Cdd:cd05367  158 R----DMFFRVLAAeePDVRVLSYAPGVVDTD 185
PRK06484 PRK06484
short chain dehydrogenase; Validated
 30-213 2.04e-14

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 73.73  E-value: 2.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwgL 109
Cdd:PRK06484   6 RVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDV--L 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 110 INNAGVPG-VLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVkKAQGR---VINVSSVGGRLAIVG-GGYTPSKYAVE 184
Cdd:PRK06484  84 VNNAGVTDpTMTATLDTTLEEFARLQAINLTGAYLVAREALRLM-IEQGHgaaIVNVASGAGLVALPKrTAYSASKAAVI 162

                        170       180
                 ....*....|....*....|....*....
gi 214010158 185 GFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK06484 163 SLTRSLACEWAAKGIRVNAVLPGYVRTQM 191
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 30-229 2.19e-14

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: 71.37  E-value: 2.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGL 109
Cdd:cd08944    4 KVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFG--GLDLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 110 INNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPSKYAVEGFN 187
Cdd:cd08944   82 VNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPrMIARGGGSIVNLSSIAGQSGDPGyGAYGASKAAIRNLT 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 214010158 188 DSLRRDMKAFGVHVSCIEPGLFKTNLadpvkvIEKKLAIWEQ 229
Cdd:cd08944  162 RTLAAELRHAGIRCNALAPGLIDTPL------LLAKLAGFEG 197
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 30-235 2.85e-14

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: 71.25  E-value: 2.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACL-TESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGekG 105
Cdd:cd05366    3 KVAIITGAAQGIGRAIAERLAADGFNIVLADLnLEEAAKSTIQEISEagyNAVAVGADVTDKDDVEALIDQAVEKFG--S 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ--GRVINVSSVGGRLA-IVGGGYTPSKYA 182
Cdd:cd05366   81 FDVMVNNAGI-APITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhgGKIINASSIAGVQGfPNLGAYSASKFA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 214010158 183 VEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAI------WEQLSPDIK 235
Cdd:cd05366  160 VRGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVGEIAGkpegegFAEFSSSIP 218
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 27-215 3.06e-14

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 71.07  E-value: 3.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  27 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLT-ESGSTALKAETSE--RLRTVLLDVTDPENVKRTAQWVKNQVGe 103
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNdEAAAAAAEALQKAggKAIGVAMDVTDEEAINAGIDYAVETFG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 104 kGLWGLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSKY 181
Cdd:PRK12429  81 -GVDILVNNAGIQHV-APIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGgGRIINMASVHGLVGSAGkAAYVSAKH 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 214010158 182 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 215
Cdd:PRK12429 159 GLIGLTKVVALEGATHGVTVNAICPGYVDTPLVR 192
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 32-215 3.22e-14

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 70.90  E-value: 3.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  32 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLR----TVLLDVTDPENVKRTAQWVKNQVGEKG-L 106
Cdd:PRK12827   9 VLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAVAAGIEaaggKALGLAFDVRDFAATRAALDAGVEEFGrL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 107 WGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ--GRVINVSSVGGRLAIVGG-GYTPSKYAV 183
Cdd:PRK12827  89 DILVNNAGI-ATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARrgGRIVNIASVAGVRGNRGQvNYAASKAGL 167

                        170       180       190
                 ....*....|....*....|....*....|..
gi 214010158 184 EGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 215
Cdd:PRK12827 168 IGLTKTLANELAPRGITVNAVAPGAINTPMAD 199
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 30-213 6.14e-14

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


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 70.00  E-value: 6.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIaacLTESGSTALKAETSERLR-------TVLLDVTDPENVKRTAQWVKNQVG 102
Cdd:cd05362    4 KVALVTGASRGIGRAIAKRLARDGASVV---VNYASSKAAAEEVVAEIEaaggkaiAVQADVSDPSQVARLFDAAEKAFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 ekGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKkAQGRVINVSSVGGRLAIVG-GGYTPSKY 181
Cdd:cd05362   81 --GVDILVNNAGV-MLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLR-DGGRIINISSSLTAAYTPNyGAYAGSKA 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 214010158 182 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:cd05362  157 AVEAFTRVLAKELGGRGITVNAVAPGPVDTDM 188
PRK05855 PRK05855
SDR family oxidoreductase;
29-215 6.43e-14

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 72.32  E-value: 6.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGStalkAETSERLR-------TVLLDVTDPENVKRTAQWVKNQV 101
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAA----ERTAELIRaagavahAYRVDVSDADAMEAFAEWVRAEH 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 102 GEKGLwgLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLIS-VTLNMLPLVKKAQ-GRVINVSSvggrlaivGGGYTPS 179
Cdd:PRK05855 391 GVPDI--VVNNAGI-GMAGGFLDTSAEDWDRVLDVNLWGVIHgCRLFGRQMVERGTgGHIVNVAS--------AAAYAPS 459

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 214010158 180 ---------KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 215
Cdd:PRK05855 460 rslpayatsKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVA 504
PRK06398 PRK06398
aldose dehydrogenase; Validated
 25-232 1.25e-13

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 69.48  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  25 EDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTAlkaetSERLRtvlLDVTDPENVKRTAQWVKNQVGEK 104
Cdd:PRK06398   2 LGLKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYND-----VDYFK---VDVSNKEQVIKGIDYVISKYGRI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 GLwgLINNAGVP--GVLAPTDwltLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIV-GGGYTPSK 180
Cdd:PRK06398  74 DI--LVNNAGIEsyGAIHAVE---EDEWDRIINVNVNGIFLMSKYTIPyMLKQDKGVIINIASVQSFAVTRnAAAYVTSK 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 214010158 181 YAVEGFNDSLRRDMkAFGVHVSCIEPGLFKTNL----------ADPVKvIEKKLAIWEQLSP 232
Cdd:PRK06398 149 HAVLGLTRSIAVDY-APTIRCVAVCPGSIRTPLlewaaelevgKDPEH-VERKIREWGEMHP 208
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 26-232 1.39e-13

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 69.22  E-value: 1.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESG----STALKAETSErLRTVLLDVTDPENVKRTAQWVKNQV 101
Cdd:PRK08217   2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKleeaVAECGALGTE-VRGYAANVTDEEDVEATFAQIAEDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 102 GekGLWGLINNAGV----------PGVLapTDWLTLEDYREPIEVNLFGLI----SVTLNMLPLvkKAQGRVINVSSVgG 167
Cdd:PRK08217  81 G--QLNGLINNAGIlrdgllvkakDGKV--TSKMSLEQFQSVIDVNLTGVFlcgrEAAAKMIES--GSKGVIINISSI-A 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 214010158 168 RLAIVG-GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVK--VIEKklaiWEQLSP 232
Cdd:PRK08217 154 RAGNMGqTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKpeALER----LEKMIP 217
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 29-218 2.15e-13

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: 68.40  E-value: 2.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE----RLRTVLLDVTD-PENVKRTAQWVKN-QVG 102
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEkygvETKTIAADFSAgDDIYERIEKELEGlDIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 EkglwgLINNAGV----PGVLAPTDwltLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGG-----RLAIv 172
Cdd:cd05356   81 I-----LVNNVGIshsiPEYFLETP---EDELQDIINVNVMATLKMTRLILPgMVKRKKGAIVNISSFAGliptpLLAT- 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 214010158 173 gggYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVK 218
Cdd:cd05356  152 ---YSASKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSKIRK 194
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 28-207 2.61e-13

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 68.45  E-value: 2.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  28 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE---TSERLRTVLLDVTDPENVKRTAQWVKNQVGek 104
Cdd:PRK07890   4 KGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEiddLGRRALAVPTDITDEDQCANLVALALERFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 GLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVG-GGYTPSKYAV 183
Cdd:PRK07890  82 RVDALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMINSMVLRHSQPKyGAYKMAKGAL 161

                        170       180
                 ....*....|....*....|....
gi 214010158 184 EGFNDSLRRDMKAFGVHVSCIEPG 207
Cdd:PRK07890 162 LAASQSLATELGPQGIRVNSVAPG 185
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 26-201 3.31e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 68.84  E-value: 3.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE--TSERLRTVLLDVTDPENVKRTAQWVKNQVGe 103
Cdd:PRK05872   6 SLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAElgGDDRVLTVVADVTDLAAMQAAAEEAVERFG- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 104 kGLWGLINNAGV--PGVLAPTDwltLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGGG-YTPSK 180
Cdd:PRK05872  85 -GIDVVVANAGIasGGSVAQVD---PDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSLAAFAAAPGMAaYCASK 160

                        170       180
                 ....*....|....*....|.
gi 214010158 181 YAVEGFNDSLRRDMKAFGVHV 201
Cdd:PRK05872 161 AGVEAFANALRLEVAHHGVTV 181
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 24-214 3.92e-13

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: 67.92  E-value: 3.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  24 IEDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLL----DVTDPENVKRTAQWVKN 99
Cdd:cd05343    1 MERWRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLFpyqcDLSNEEQILSMFSAIRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 100 QVGekGLWGLINNAGvpgvLAPTDWL---TLEDYREPIEVNLFGLISVT---LNMLPLVKKAQGRVINVSSVGGR---LA 170
Cdd:cd05343   81 QHQ--GVDVCINNAG----LARPEPLlsgKTEGWKEMFDVNVLALSICTreaYQSMKERNVDDGHIININSMSGHrvpPV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 214010158 171 IVGGGYTPSKYAVEGFNDSLRRDMKAFGVH--VSCIEPGLFKTNLA 214
Cdd:cd05343  155 SVFHFYAATKHAVTALTEGLRQELREAKTHirATSISPGLVETEFA 200
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 16-223 4.56e-13

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: 67.86  E-value: 4.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  16 WTRKGKLKIeditdkyifITGCDSGFGNLAARTFDKKGFHVIA---------ACLTESGSTALKAETSerlrtvLLDVTD 86
Cdd:cd05329    2 WNLEGKTAL---------VTGGTKGIGYAIVEELAGLGAEVYTcarnqkeldECLTEWREKGFKVEGS------VCDVSS 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  87 PENVKRTAQWVKNQVGEKgLWGLINNAGVPGVLAPTDWlTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSV 165
Cdd:cd05329   67 RSERQELMDTVASHFGGK-LNILVNNAGTNIRKEAKDY-TEEDYSLIMSTNFEAAYHLSRLAHPLLKASGnGNIVFISSV 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 214010158 166 GGRLAI-VGGGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPV--------KVIEKK 223
Cdd:cd05329  145 AGVIAVpSGAPYGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPViqqkenldKVIERT 211
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 29-229 5.60e-13

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: 67.68  E-value: 5.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLL---DVTDPENVKRTAQWVKNQVGekG 105
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAGVLAvvaDLTDPEDIDRLVEKAGDAFG--R 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LWGLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVGGGYTP-SKYAV 183
Cdd:cd05344   79 VDILVNNAGGPPP-GPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLTVKEPEPNLVLSNvARAGL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 214010158 184 EGFNDSLRRDMKAFGVHVSCIEPGLFKTN-LADPVKVIEKKLAIWEQ 229
Cdd:cd05344  158 IGLVKTLSRELAPDGVTVNSVLPGYIDTErVRRLLEARAEKEGISVE 204
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
29-240 6.50e-13

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 67.36  E-value: 6.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWG 108
Cdd:PRK07067   6 GKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFG--GIDI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAGVPGvLAPTDWLTLEDYREPIEVNLFGlisvTLNMLPLVKK---AQGR---VINVSSVGGR----LAIVgggYTP 178
Cdd:PRK07067  84 LFNNAALFD-MAPILDISRDSYDRLFAVNVKG----LFFLMQAVARhmvEQGRggkIINMASQAGRrgeaLVSH---YCA 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 214010158 179 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVkviEKKLAIWEQLSP-DIKQQYGE 240
Cdd:PRK07067 156 TKAAVISYTQSAALALIRHGINVNAIAPGVVDTPMWDQV---DALFARYENRPPgEKKRLVGE 215
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 26-208 6.68e-13

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 67.34  E-value: 6.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGstalkaETSERLRTVLLDVTDPENVKRTAQWVKNQVGEkg 105
Cdd:PRK06171   6 NLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGD------GQHENYQFVPTDVSSAEEVNHTVAEIIEKFGR-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LWGLINNAGV--PGVLA-PTD-----WLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG- 175
Cdd:PRK06171  78 IDGLVNNAGIniPRLLVdEKDpagkyELNEAAFDKMFNINQKGVFLMSQAVARqMVKQHDGVIVNMSSEAGLEGSEGQSc 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 214010158 176 YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGL 208
Cdd:PRK06171 158 YAATKAALNSFTRSWAKELGKHNIRVVGVAPGI 190
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 27-232 8.15e-13

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: 67.02  E-value: 8.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  27 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAAcLTESGSTAlkAETSERLRT-------VLLDVTDPENVKRTAQWVKN 99
Cdd:cd05358    1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVN-YRSKEDAA--EEVVEEIKAvggkaiaVQADVSKEEDVVALFQSAIK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 100 QVGEKGLWglINNAGVPGVLAPTDwLTLEDYREPIEVNLFGLISV---TLNMLpLVKKAQGRVINVSSVGGRLAIVG-GG 175
Cdd:cd05358   78 EFGTLDIL--VNNAGLQGDASSHE-MTLEDWNKVIDVNLTGQFLCareAIKRF-RKSKIKGKIINMSSVHEKIPWPGhVN 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 214010158 176 YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSP 232
Cdd:cd05358  154 YAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDPEQRADLLSLIP 210
PRK06139 PRK06139
SDR family oxidoreductase;
29-211 8.20e-13

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 67.82  E-value: 8.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFH-VIAAclteSGSTALkAETSERLR-------TVLLDVTDPENVKRTAQWVKNQ 100
Cdd:PRK06139   7 GAVVVITGASSGIGQATAEAFARRGARlVLAA----RDEEAL-QAVAEECRalgaevlVVPTDVTDADQVKALATQAASF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 101 VGEKGLWglINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKaQGR--VINVSSVGGRLAI-VGGGYT 177
Cdd:PRK06139  82 GGRIDVW--VNNVGV-GAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKK-QGHgiFINMISLGGFAAQpYAAAYS 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 214010158 178 PSKYAVEGFNDSLRRDMKAF-GVHVSCIEPGLFKT 211
Cdd:PRK06139 158 ASKFGLRGFSEALRGELADHpDIHVCDVYPAFMDT 192
PRK05866 PRK05866
SDR family oxidoreductase;
26-218 9.36e-13

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 67.46  E-value: 9.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSER---LRTVLLDVTDPENVKRTAQWVKNQVG 102
Cdd:PRK05866  37 DLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAggdAMAVPCDLSDLDAVDALVADVEKRIG 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 ekGLWGLINNAG----VPGVLAPTDWltlEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSvGGRLAIVG---G 174
Cdd:PRK05866 117 --GVDILINNAGrsirRPLAESLDRW---HDVERTMVLNYYAPLRLIRGLAPgMLERGDGHIINVAT-WGVLSEASplfS 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 214010158 175 GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVK 218
Cdd:PRK05866 191 VYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPMIAPTK 234
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 26-211 1.07e-12

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 66.65  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACL-TESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGeK 104
Cdd:PRK08642   2 QISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHqSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEHFG-K 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 GLWGLINNAGV-----PGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYT 177
Cdd:PRK08642  81 PITTVVNNALAdfsfdGDARKKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGfGRIINIGTNLFQNPVVPyHDYT 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 214010158 178 PSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT 211
Cdd:PRK08642 161 TAKAALLGLTRNLAAELGPYGITVNMVSGGLLRT 194
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 26-229 1.58e-12

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 66.46  E-value: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE---TSERLRTVLLDVTDPENVKRTAQWVKNQVG 102
Cdd:PRK13394   4 NLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEinkAGGKAIGVAMDVTNEDAVNAGIDKVAERFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 EKGLwgLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ--GRVINVSSVGGRLAIVG-GGYTPS 179
Cdd:PRK13394  84 SVDI--LVSNAGIQIV-NPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHSHEASPLkSAYVTA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 214010158 180 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADP-VKVIEKKLAIWEQ 229
Cdd:PRK13394 161 KHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKqIPEQAKELGISEE 211
PRK06484 PRK06484
short chain dehydrogenase; Validated
 34-211 2.03e-12

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 67.57  E-value: 2.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwgLINNA 113
Cdd:PRK06484 274 ITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRLDV--LVNNA 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 114 GVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAqGRVINVSSVGGRLAIVG-GGYTPSKYAVEGFNDSLRR 192
Cdd:PRK06484 352 GIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG-GVIVNLGSIASLLALPPrNAYCASKAAVTMLSRSLAC 430

                        170
                 ....*....|....*....
gi 214010158 193 DMKAFGVHVSCIEPGLFKT 211
Cdd:PRK06484 431 EWAPAGIRVNTVAPGYIET 449
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 20-213 2.80e-12

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: 65.78  E-value: 2.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  20 GKLKieditDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTA---LKAETSERLRTVLL--DVTDPENVKRTA 94
Cdd:cd05355   22 GKLK-----GKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEDDAeetKKLIEEEGRKCLLIpgDLGDESFCRDLV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  95 QWVKNQVGekGLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAqGRVINVSSVggrLAIVGG 174
Cdd:cd05355   97 KEVVKEFG--KLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKKG-SSIINTTSV---TAYKGS 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 214010158 175 G----YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:cd05355  171 PhlldYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPL 213
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 25-213 2.94e-12

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


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 65.56  E-value: 2.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  25 EDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLT-ESGSTALKAETS--ERLRTVLLDVTDPENVKRTAQWVKNQV 101
Cdd:cd08935    1 FSLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNqEKGDKVAKEITAlgGRAIALAADVLDRASLERAREEIVAQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 102 GEKGLwgLINNAG--VPGVLAPTDWLTLEDYREPIEVNLFGLISVT-LNML-----------PLVKKAQGRVINVSSVGG 167
Cdd:cd08935   81 GTVDI--LINGAGgnHPDATTDPEHYEPETEQNFFDLDEEGWEFVFdLNLNgsflpsqvfgkDMLEQKGGSIINISSMNA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 214010158 168 RLAIVG-GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:cd08935  159 FSPLTKvPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQ 205
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
30-213 3.18e-12

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 65.48  E-value: 3.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETS-ERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLWG 108
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKELTKLAEQYnSNLTFHSLDLQDVHELETNFNEILSSIQEDNVSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 --LINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQG--RVINVSSVGGRLAIVG-GGYTPSKYAV 183
Cdd:PRK06924  82 ihLINNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKVdkRVINISSGAAKNPYFGwSAYCSSKAGL 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 214010158 184 EGFNDS--LRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK06924 162 DMFTQTvaTEQEEEEYPVKIVAFSPGVMDTNM 193
PLN02253 PLN02253
xanthoxin dehydrogenase
 30-216 3.94e-12

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 65.61  E-value: 3.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHV-IAACLTESGSTALKA-ETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLw 107
Cdd:PLN02253  19 KVALVTGGATGIGESIVRLFHKHGAKVcIVDLQDDLGQNVCDSlGGEPNVCFFHCDVTVEDDVSRAVDFTVDKFGTLDI- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 108 gLINNAGVPGvlAP-TDW--LTLEDYREPIEVNL----FGLISVTLNMLPLVKkaqGRVINVSSVGGRLAIVG-GGYTPS 179
Cdd:PLN02253  98 -MVNNAGLTG--PPcPDIrnVELSEFEKVFDVNVkgvfLGMKHAARIMIPLKK---GSIVSLCSVASAIGGLGpHAYTGS 171

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 214010158 180 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADP 216
Cdd:PLN02253 172 KHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALA 208
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 26-211 4.21e-12

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 64.97  E-value: 4.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLL---DVTDPENVKRTAQWVKNQVG 102
Cdd:PRK08213   9 DLSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGIDALWiaaDVADEADIERLAEETLERFG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 EKGLwgLINNAGVP-GvlAPTDWLTLEDYREPIEVNLFGLISVT-----LNMLPlvkKAQGRVINVSSVGGrlaiVGG-- 174
Cdd:PRK08213  89 HVDI--LVNNAGATwG--APAEDHPVEAWDKVMNLNVRGLFLLSqavakRSMIP---RGYGRIINVASVAG----LGGnp 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 214010158 175 -------GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT 211
Cdd:PRK08213 158 pevmdtiAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPT 201
PRK07069 PRK07069
short chain dehydrogenase; Validated
 33-225 4.90e-12

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 64.73  E-value: 4.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  33 FITGCDSGFGNLAARTFDKKGFHVIAACL-TESGSTALKAETSERLRT-----VLLDVTDPENVKRTAQWVKNQVGekGL 106
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVFLTDInDAAGLDAFAAEINAAHGEgvafaAVQDVTDEAQWQALLAQAADAMG--GL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 107 WGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGrlAIVGG---GYTPSKYA 182
Cdd:PRK07069  81 SVLVNNAGV-GSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQpASIVNISSVAA--FKAEPdytAYNASKAA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 214010158 183 VEGFNDSLRRDMKAFGVHVSC--IEPGLFKTNLADPV------KVIEKKLA 225
Cdd:PRK07069 158 VASLTKSIALDCARRGLDVRCnsIHPTFIRTGIVDPIfqrlgeEEATRKLA 208
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 30-213 5.12e-12

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: 65.18  E-value: 5.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACL----TESGSTALKAETSERLRTVL-LDVTDPENVKRTAQWVKNQvgEK 104
Cdd:cd09807    2 KTVIITGANTGIGKETARELARRGARVIMACRdmakCEEAAAEIRRDTLNHEVIVRhLDLASLKSIRAFAAEFLAE--ED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 GLWGLINNAGVpgVLAPTdWLTLEDYREPIEVNLFGLISVTLNMLPLVKK-AQGRVINVSSV---GGRLAI--------- 171
Cdd:cd09807   80 RLDVLINNAGV--MRCPY-SKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKsAPSRIVNVSSLahkAGKINFddlnseksy 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 214010158 172 -VGGGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:cd09807  157 nTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTEL 199
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 26-207 5.16e-12

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 64.91  E-value: 5.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGstalkaETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKG 105
Cdd:PRK08220   5 DFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLT------QEDYPFATFVLDVSDAAAVAQVCQRLLAETGPLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LwgLINNAGVPGvLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVK-KAQGRVINVSSVGGRLAIVG-GGYTPSKYAV 183
Cdd:PRK08220  79 V--LVNAAGILR-MGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRrQRSGAIVTVGSNAAHVPRIGmAAYGASKAAL 155

                        170       180
                 ....*....|....*....|....
gi 214010158 184 EGFNDSLRRDMKAFGVHVSCIEPG 207
Cdd:PRK08220 156 TSLAKCVGLELAPYGVRCNVVSPG 179
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 29-236 5.48e-12

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 64.87  E-value: 5.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGekG 105
Cdd:PRK06113  11 GKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQlggQAFACRCDITSEQELSALADFALSKLG--K 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LWGLINNAGVPGVlAPTDwLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVI-NVSSVGG-----RLAivggGYTPS 179
Cdd:PRK06113  89 VDILVNNAGGGGP-KPFD-MPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVIlTITSMAAenkniNMT----SYASS 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 214010158 180 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNladpvkviekklAIWEQLSPDIKQ 236
Cdd:PRK06113 163 KAAASHLVRNMAFDLGEKNIRVNGIAPGAILTD------------ALKSVITPEIEQ 207
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 26-232 5.67e-12

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: 64.66  E-value: 5.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHV----IAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQV 101
Cdd:cd05352    5 SLKGKVAIVTGGSRGIGLAIARALAEAGADVaiiyNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 102 GEkgLWGLINNAGVPGVLAPTDwLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG---GGYT 177
Cdd:cd05352   85 GK--IDILIANAGITVHKPALD-YTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGkGSLIITASMSGTIVNRPqpqAAYN 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 214010158 178 PSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLaiWEQLSP 232
Cdd:cd05352  162 ASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKK--WESYIP 214
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
30-211 6.02e-12

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 64.75  E-value: 6.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETS---ERLRTVLLDVTDPENVKRTAQWVKNQVGekGL 106
Cdd:PRK08643   3 KVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSkdgGKAIAVKADVSDRDQVFAAVRQVVDTFG--DL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 107 WGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ--GRVINVSSVGG-----RLAIvgggYTPS 179
Cdd:PRK08643  81 NVVVNNAGV-APTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGhgGKIINATSQAGvvgnpELAV----YSST 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 214010158 180 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT 211
Cdd:PRK08643 156 KFAVRGLTQTAARDLASEGITVNAYAPGIVKT 187
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 29-227 8.07e-12

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 64.39  E-value: 8.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVIAaclteSGSTALKAETS-ERLR-------TVLLDVTDPENVKRTAQWVKNQ 100
Cdd:PRK08085   9 GKNILITGSAQGIGFLLATGLAEYGAEIII-----NDITAERAELAvAKLRqegikahAAPFNVTHKQEVEAAIEHIEKD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 101 VGEKGLwgLINNAGVPGVLAPTDWlTLEDYREPIEVNLFG--LIS--VTLNMlplVKKAQGRVINVSSVG---GRLAIVg 173
Cdd:PRK08085  84 IGPIDV--LINNAGIQRRHPFTEF-PEQEWNDVIAVNQTAvfLVSqaVARYM---VKRQAGKIINICSMQselGRDTIT- 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 214010158 174 gGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVkVIEKKLAIW 227
Cdd:PRK08085 157 -PYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKAL-VEDEAFTAW 208
PRK06194 PRK06194
hypothetical protein; Provisional
 24-215 8.68e-12

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 64.65  E-value: 8.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  24 IEDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTE----SGSTALKAETSERLrTVLLDVTDPENVKRTAQWVKN 99
Cdd:PRK06194   1 MKDFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQdaldRAVAELRAQGAEVL-GVRTDVSDAAQVEALADAALE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 100 QVGEKGLwgLINNAGVP--GVLaptdWL-TLEDYREPIEVNLFGLIS----VTLNMLPLVKKA---QGRVINVSSVGGRL 169
Cdd:PRK06194  80 RFGAVHL--LFNNAGVGagGLV----WEnSLADWEWVLGVNLWGVIHgvraFTPLMLAAAEKDpayEGHIVNTASMAGLL 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 214010158 170 AIVGGG-YTPSKYAVEGFNDSLRRDMKAFG--VHVSCIEPGLFKTNLAD 215
Cdd:PRK06194 154 APPAMGiYNVSKHAVVSLTETLYQDLSLVTdqVGASVLCPYFVPTGIWQ 202
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 29-240 1.18e-11

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 63.79  E-value: 1.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWG 108
Cdd:cd05363    3 GKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWG--SIDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAGVPGvLAPTDWLTLEDYREPIEVNLFGlisvTLNMLPLVKK---AQGR---VINVSSVGGRL--AIVgGGYTPSK 180
Cdd:cd05363   81 LVNNAALFD-LAPIVDITRESYDRLFAINVSG----TLFMMQAVARamiAQGRggkIINMASQAGRRgeALV-GVYCATK 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 214010158 181 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVkviEKKLAIWEQLS-PDIKQQYGE 240
Cdd:cd05363  155 AAVISLTQSAGLNLIRHGINVNAIAPGVVDGEHWDGV---DAKFARYENRPrGEKKRLVGE 212
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 32-207 1.31e-11

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: 63.64  E-value: 1.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  32 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESgstaLKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGLIN 111
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFV----LLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHG--PIDALVN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 112 NAGVPgVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGG---RLAIvgGGYTPSKYAVEGFN 187
Cdd:cd05331   75 CAGVL-RPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPhMKDRRTGAIVTVASNAAhvpRISM--AAYGASKAALASLS 151

                        170       180
                 ....*....|....*....|
gi 214010158 188 DSLRRDMKAFGVHVSCIEPG 207
Cdd:cd05331  152 KCLGLELAPYGVRCNVVSPG 171
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 28-245 1.33e-11

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 63.52  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  28 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLR-----TVLLDVTDPENVKRTAQWVKNQVG 102
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGegmayGFGADATSEQSVLALSRGVDEIFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 EKGLwgLINNAGVpGVLAPTDWLTLEDYREPIEVNLFG--LISVTLNMLPLVKKAQGRVINVSSVGGRlaiVGG----GY 176
Cdd:PRK12384  81 RVDL--LVYNAGI-AKAAFITDFQLGDFDRSLQVNLVGyfLCAREFSRLMIRDGIQGRIIQINSKSGK---VGSkhnsGY 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 214010158 177 TPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGlfktNLADP---VKVIE---KKLAIweqlSPDIKQQYgegYIEK 245
Cdd:PRK12384 155 SAAKFGGVGLTQSLALDLAEYGITVHSLMLG----NLLKSpmfQSLLPqyaKKLGI----KPDEVEQY---YIDK 218
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 30-225 1.34e-11

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 63.48  E-value: 1.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVI-----AACLTESGSTALKAETSERLrTVLLDVTDPENVKRTAQWVKNQVGEK 104
Cdd:PRK12935   7 KVAIVTGGAKGIGKAITVALAQEGAKVVinynsSKEAAENLVNELGKEGHDVY-AVQADVSKVEDANRLVEEAVNHFGKV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 GLwgLINNAGVPGVLAPTDwLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSKYA 182
Cdd:PRK12935  86 DI--LVNNAGITRDRTFKK-LNREDWERVIDVNLSSVFNTTSAVLPYITEAEeGRIISISSIIGQAGGFGqTNYSAAKAG 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 214010158 183 VEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL--ADPVKVIEKKLA 225
Cdd:PRK12935 163 MLGFTKSLALELAKTNVTVNAICPGFIDTEMvaEVPEEVRQKIVA 207
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 29-206 1.50e-11

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: 63.18  E-value: 1.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWG 108
Cdd:cd05345    5 GKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFG--RLDI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVI-NVSSVGG---RLAIVggGYTPSKYAVE 184
Cdd:cd05345   83 LVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIiNIASTAGlrpRPGLT--WYNASKGWVV 160

                        170       180
                 ....*....|....*....|..
gi 214010158 185 GFNDSLRRDMKAFGVHVSCIEP 206
Cdd:cd05345  161 TATKAMAVELAPRNIRVNCLCP 182
PRK07024 PRK07024
SDR family oxidoreductase;
32-211 2.12e-11

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 63.02  E-value: 2.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  32 IFITGCDSGFGNLAARTFDKKGFHV--IAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwgL 109
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLglVARRTDALQAFAARLPKAARVSVYAADVRDADALAAAAADFIAAHGLPDV--V 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 110 INNAGVP-GVLA--PTDwltLEDYREPIEVNLFGLISvTLN--MLPLVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYAV 183
Cdd:PRK07024  83 IANAGISvGTLTeeRED---LAVFREVMDTNYFGMVA-TFQpfIAPMRAARRGTLVGIASVAGVRGLPGAGaYSASKAAA 158

                        170       180
                 ....*....|....*....|....*...
gi 214010158 184 EGFNDSLRRDMKAFGVHVSCIEPGLFKT 211
Cdd:PRK07024 159 IKYLESLRVELRPAGVRVVTIAPGYIRT 186
PRK07062 PRK07062
SDR family oxidoreductase;
26-165 2.43e-11

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 63.14  E-value: 2.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHViAAC------LTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKN 99
Cdd:PRK07062   5 QLEGRVAVVTGGSSGIGLATVELLLEAGASV-AICgrdeerLASAEARLREKFPGARLLAARCDVLDEADVAAFAAAVEA 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 214010158 100 QVGekGLWGLINNAGvPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKA-QGRVINVSSV 165
Cdd:PRK07062  84 RFG--GVDMLVNNAG-QGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASaAASIVCVNSL 147
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 20-207 3.15e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 62.74  E-value: 3.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  20 GKLKieditDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTalkAETSERL-----RTVLL--DVTDP----E 88
Cdd:PRK06701  42 GKLK-----GKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDA---NETKQRVekegvKCLLIpgDVSDEafckD 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  89 NVKRTAQwvknQVGekGLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAqGRVINVSSVGGr 168
Cdd:PRK06701 114 AVEETVR----ELG--RLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLKQG-SAIINTGSITG- 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 214010158 169 laIVGGG----YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPG 207
Cdd:PRK06701 186 --YEGNEtlidYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPG 226
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 34-211 3.96e-11

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: 62.20  E-value: 3.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGLI 110
Cdd:cd05365    4 VTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQaggQAIGLECNVTSEQDLEAVVKATVSQFG--GITILV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 111 NNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVI-NVSSVGGRL-AIVGGGYTPSKYAVEGFND 188
Cdd:cd05365   82 NNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAIlNISSMSSENkNVRIAAYGSSKAAVNHMTR 161

                        170       180
                 ....*....|....*....|...
gi 214010158 189 SLRRDMKAFGVHVSCIEPGLFKT 211
Cdd:cd05365  162 NLAFDLGPKGIRVNAVAPGAVKT 184
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
26-223 4.45e-11

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 62.06  E-value: 4.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGStALKAETSERLRTVL---LDVTDPENVKRTAQWVKNQVG 102
Cdd:PRK06935  12 SLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWD-ETRRLIEKEGRKVTfvqVDLTKPESAEKVVKEALEEFG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 EKGLwgLINNAGVPGvLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVggrLAIVGG----GYT 177
Cdd:PRK06935  91 KIDI--LVNNAGTIR-RAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKvMAKQGSGKIINIASM---LSFQGGkfvpAYT 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 214010158 178 PSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKK 223
Cdd:PRK06935 165 ASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAPIRADKNR 210
PRK06949 PRK06949
SDR family oxidoreductase;
26-213 5.48e-11

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 61.70  E-value: 5.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSER---LRTVLLDVTDPENVKRTAQWVKNQVG 102
Cdd:PRK06949   6 NLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEggaAHVVSLDVTDYQSIKAAVAHAETEAG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 EKGLwgLINNAGVPGVLAPTDwLTLEDYREPIEVNLFGLI----SVTLNMLPLVK-----KAQGRVINVSSVGGrLAIVG 173
Cdd:PRK06949  86 TIDI--LVNNSGVSTTQKLVD-VTPADFDFVFDTNTRGAFfvaqEVAKRMIARAKgagntKPGGRIINIASVAG-LRVLP 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 214010158 174 --GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK06949 162 qiGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEI 203
PRK06124 PRK06124
SDR family oxidoreductase;
34-211 7.04e-11

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 61.65  E-value: 7.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKGFHVI-----AACLTESGST----ALKAETserlrtVLLDVTDPENVKRTAQWVKNQVGek 104
Cdd:PRK06124  16 VTGSARGLGFEIARALAGAGAHVLvngrnAATLEAAVAAlraaGGAAEA------LAFDIADEEAVAAAFARIDAEHG-- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 GLWGLINNAGVPGvLAPTDWLTLEDYREPIEVNLFGLISVT-LNMLPLVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYA 182
Cdd:PRK06124  88 RLDILVNNVGARD-RRPLAELDDAAIRALLETDLVAPILLSrLAAQRMKRQGYGRIIAITSIAGQVARAGDAvYPAAKQG 166

                        170       180
                 ....*....|....*....|....*....
gi 214010158 183 VEGFNDSLRRDMKAFGVHVSCIEPGLFKT 211
Cdd:PRK06124 167 LTGLMRALAAEFGPHGITSNAIAPGYFAT 195
PRK06138 PRK06138
SDR family oxidoreductase;
26-213 8.90e-11

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 61.32  E-value: 8.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE--TSERLRTVLLDVTDPENVKRTAQWVKNQVGe 103
Cdd:PRK06138   2 RLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAiaAGGRAFARQGDVGSAEAVEALVDFVAARWG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 104 kGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSvggRLAIVGG----GYTP 178
Cdd:PRK06138  81 -RLDVLVNNAGF-GCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGgGSIVNTAS---QLALAGGrgraAYVA 155

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 214010158 179 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK06138 156 SKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPY 190
PRK06101 PRK06101
SDR family oxidoreductase;
32-241 9.24e-11

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 61.04  E-value: 9.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  32 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAeTSERLRTVLLDVTDPENVKRTAQWVKNQvgeKGLWglIN 111
Cdd:PRK06101   4 VLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDELHT-QSANIFTLAFDVTDHPGTKAALSQLPFI---PELW--IF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 112 NAGvpgvlaptDWLTLED-------YREPIEVNLFGLISVTLNMLPLVKKAQgRVINVSSVGGRLAIV-GGGYTPSKYAV 183
Cdd:PRK06101  78 NAG--------DCEYMDDgkvdatlMARVFNVNVLGVANCIEGIQPHLSCGH-RVVIVGSIASELALPrAEAYGASKAAV 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 214010158 184 EGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSPDIKQQYGEG 241
Cdd:PRK06101 149 AYFARTLQLDLRPKGIEVVTVFPGFVATPLTDKNTFAMPMIITVEQASQEIRAQLARG 206
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 29-207 1.00e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 61.10  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE-TSERLRTVLL--DVTDPENVKRTAQWVKNQVGekG 105
Cdd:PRK07478   6 GKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEiRAEGGEAVALagDVRDEAYAKALVALAVERFG--G 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSS-VGGRLAIVG-GGYTPSKYA 182
Cdd:PRK07478  84 LDIAFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPaMLARGGGSLIFTSTfVGHTAGFPGmAAYAASKAG 163

                        170       180
                 ....*....|....*....|....*
gi 214010158 183 VEGFNDSLRRDMKAFGVHVSCIEPG 207
Cdd:PRK07478 164 LIGLTQVLAAEYGAQGIRVNALLPG 188
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 34-213 1.15e-10

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 61.13  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKGFHVIAACLTESG----STALKAETSErLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwgL 109
Cdd:PRK05876  11 ITGGASGIGLATGTEFARRGARVVLGDVDKPGlrqaVNHLRAEGFD-VHGVMCDVRHREEVTHLADEAFRLLGHVDV--V 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 110 INNAGVPgVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP--LVKKAQGRVINVSSVGGRLAIVG-GGYTPSKYAVEGF 186
Cdd:PRK05876  88 FSNAGIV-VGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPrlLEQGTGGHVVFTASFAGLVPNAGlGAYGVAKYGVVGL 166

                        170       180
                 ....*....|....*....|....*..
gi 214010158 187 NDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK05876 167 AETLAREVTADGIGVSVLCPMVVETNL 193
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 32-167 2.03e-10

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: 60.20  E-value: 2.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  32 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTAlkaetserlrtvllDVTDPENVKRTAQWVKNQVGeKGLWGLIN 111
Cdd:cd05328    2 IVITGAASGIGAATAELLEDAGHTVIGIDLREADVIA--------------DLSTPEGRAAAIADVLARCS-GVLDGLVN 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 214010158 112 NAGVPGVlAPTDwLTLedyrepiEVNLFGLISVTLNMLPLVKKA-QGRVINVSSVGG 167
Cdd:cd05328   67 CAGVGGT-TVAG-LVL-------KVNYFGLRALMEALLPRLRKGhGPAAVVVSSIAG 114
PRK06114 PRK06114
SDR family oxidoreductase;
26-232 2.95e-10

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 59.80  E-value: 2.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHViaACLTESGSTALkAETSERLRT-------VLLDVTDPENVKRTAQWVK 98
Cdd:PRK06114   5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADV--ALFDLRTDDGL-AETAEHIEAagrraiqIAADVTSKADLRAAVARTE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  99 NQVGEKGLwgLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGL-ISVTLNMLPLVKKAQGRVINVSSVGGrlAIVGGG-- 175
Cdd:PRK06114  82 AELGALTL--AVNAAGIANA-NPAEEMEEEQWQTVMDINLTGVfLSCQAEARAMLENGGGSIVNIASMSG--IIVNRGll 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 176 ---YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEkKLAIWEQLSP 232
Cdd:PRK06114 157 qahYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTRPEMVH-QTKLFEEQTP 215
PRK08251 PRK08251
SDR family oxidoreductase;
28-218 4.17e-10

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 59.18  E-value: 4.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  28 TDKYIFITGCDSGFGNLAARTFDKKGfHVIAAC------LTEsgstaLKAETSER--LRTVL---LDVTDPENVKRTAQW 96
Cdd:PRK08251   1 TRQKILITGASSGLGAGMAREFAAKG-RDLALCarrtdrLEE-----LKAELLARypGIKVAvaaLDVNDHDQVFEVFAE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  97 VKNQVGekGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLIS---VTLNMLplvkKAQGR--VINVSSVggrLAI 171
Cdd:PRK08251  75 FRDELG--GLDRVIVNAGI-GKGARLGTGKFWANKATAETNFVAALAqceAAMEIF----REQGSghLVLISSV---SAV 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 214010158 172 VG-----GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVK 218
Cdd:PRK08251 145 RGlpgvkAAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNAKAK 196
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 109-230 7.64e-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: 57.53  E-value: 7.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVK-KAQGRVINVSSVGGRLAIVG-GGYTPSKYAVEGF 186
Cdd:cd02266   35 VVHNAAILDD-GRLIDLTGSRIERAIRANVVGTRRLLEAARELMKaKRLGRFILISSVAGLFGAPGlGGYAASKAALDGL 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 214010158 187 NDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQL 230
Cdd:cd02266  114 AQQWASEGWGNGLPATAVACGTWAGSGMAKGPVAPEEILGNRRH 157
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 26-234 1.63e-09

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: 57.36  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEkg 105
Cdd:cd05348    1 WLKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGK-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LWGLINNAGV---PGVLAPTDWLTLED-YREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGrLAIVGGG--YTPS 179
Cdd:cd05348   79 LDCFIGNAGIwdySTSLVDIPEEKLDEaFDELFHINVKGYILGAKAALPALYATEGSVIFTVSNAG-FYPGGGGplYTAS 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 214010158 180 KYAVEGFNDSLRRDMkAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSPDI 234
Cdd:cd05348  158 KHAVVGLVKQLAYEL-APHIRVNGVAPGGMVTDLRGPASLGQGETSISTPPLDDM 211
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 26-209 1.87e-09

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


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 57.11  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAacltesgsTALKAE----TSERLRT------VLLDVTDPENVKRTAQ 95
Cdd:cd08942    3 SVAGKIVLVTGGSRGIGRMIAQGFLEAGARVII--------SARKAEacadAAEELSAygeciaIPADLSSEEGIEALVA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  96 wvknQVGEKG--LWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-----GRVINVSSVGGr 168
Cdd:cd08942   75 ----RVAERSdrLDVLVNNAGA-TWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAAtaenpARVINIGSIAG- 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 214010158 169 laIVGGG-----YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLF 209
Cdd:cd08942  149 --IVVSGlenysYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRF 192
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 34-183 2.49e-09

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: 57.02  E-value: 2.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGS--TALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGLIN 111
Cdd:cd08943    6 VTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAekVAEAAQGGPRALGVQCDVTSEAQVQSAFEQAVLEFG--GLDIVVS 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 214010158 112 NAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKaQGrvinvssVGGRLAIVGggytpSKYAV 183
Cdd:cd08943   84 NAGIATS-SPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKS-QG-------IGGNIVFNA-----SKNAV 141
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
30-164 3.82e-09

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 57.55  E-value: 3.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE--TSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLW 107
Cdd:PRK08324 423 KVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAElgGPDRALGVACDVTDEAAVQAAFEEAALAFG--GVD 500

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 214010158 108 GLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ--GRVINVSS 164
Cdd:PRK08324 501 IVVSNAGIAIS-GPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGlgGSIVFIAS 558
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 26-207 4.56e-09

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 56.17  E-value: 4.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekG 105
Cdd:PRK08265   3 GLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFG--R 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LWGLINNAGV---PGVLAP-TDWLTLEDyrepieVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGGG-YTPSK 180
Cdd:PRK08265  81 VDILVNLACTyldDGLASSrADWLAALD------VNLVSAAMLAQAAHPHLARGGGAIVNFTSISAKFAQTGRWlYPASK 154

                        170       180
                 ....*....|....*....|....*..
gi 214010158 181 YAVEGFNDSLRRDMKAFGVHVSCIEPG 207
Cdd:PRK08265 155 AAIRQLTRSMAMDLAPDGIRVNSVSPG 181
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 26-216 7.61e-09

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 55.54  E-value: 7.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVI-----AACLtESGSTALKAETSErLRTVLLDVTDPENVKRTAQWVKNQ 100
Cdd:PRK07523   7 DLTGRRALVTGSSQGIGYALAEGLAQAGAEVIlngrdPAKL-AAAAESLKGQGLS-AHALAFDVTDHDAVRAAIDAFEAE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 101 VGEKGLwgLINNAGVPgVLAPTDWLTLEDYREPIEVNLFGLISVTLNML-PLVKKAQGRVINVSSVGGRLAIVG-GGYTP 178
Cdd:PRK07523  85 IGPIDI--LVNNAGMQ-FRTPLEDFPADAFERLLRTNISSVFYVGQAVArHMIARGAGKIINIASVQSALARPGiAPYTA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 214010158 179 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL-----ADP 216
Cdd:PRK07523 162 TKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLnaalvADP 204
PRK08628 PRK08628
SDR family oxidoreductase;
26-206 7.98e-09

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 55.35  E-value: 7.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGfhVIAACLTESgstALKAETSERLR-------TVLLDVTDPENVKRTaqwVK 98
Cdd:PRK08628   4 NLKDKVVIVTGGASGIGAAISLRLAEEG--AIPVIFGRS---APDDEFAEELRalqpraeFVQVDLTDDAQCRDA---VE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  99 NQVGEKG-LWGLINNAGVpgvlapTDWLTLE----DYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSvggRLAIVG 173
Cdd:PRK08628  76 QTVAKFGrIDGLVNNAGV------NDGVGLEagreAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISS---KTALTG 146

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 214010158 174 ----GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEP 206
Cdd:PRK08628 147 qggtSGYAAAKGAQLALTREWAVALAKDGVRVNAVIP 183
PRK12746 PRK12746
SDR family oxidoreductase;
24-213 9.29e-09

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 55.43  E-value: 9.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  24 IEDITDKYIFITGCDSGFGNLAARTFDKKGFHVI---AACLTESGSTALKAETSE-RLRTVLLDVTDPENVKRTAQWVKN 99
Cdd:PRK12746   1 MKNLDGKVALVTGASRGIGRAIAMRLANDGALVAihyGRNKQAADETIREIESNGgKAFLIEADLNSIDGVKKLVEQLKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 100 Q----VGEKGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKkAQGRVINVSSVGGRLAIVGG- 174
Cdd:PRK12746  81 ElqirVGTSEIDILVNNAGI-GTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLR-AEGRVINISSAEVRLGFTGSi 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 214010158 175 GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK12746 159 AYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDI 197
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 34-238 1.09e-08

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


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 54.70  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRT----VLLDVTDPENVKRTAQWVKNQVGEKGLwgL 109
Cdd:cd05373    4 VVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGsakaVPTDARDEDEVIALFDLIEEEIGPLEV--L 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 110 INNAG--VPGVLAPTdwlTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVI---NVSSVGGR--LAivggGYTPSKY 181
Cdd:cd05373   82 VYNAGanVWFPILET---TPRVFEKVWEMAAFGGFLAAREAAKrMLARGRGTIIftgATASLRGRagFA----AFAGAKF 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 214010158 182 AVEGFNDSLRRDMKAFGVHV------SCIEPGLFKTNLADPVKVIEKKlaiwEQLSPD-IKQQY 238
Cdd:cd05373  155 ALRALAQSMARELGPKGIHVahviidGGIDTDFIRERFPKRDERKEED----GILDPDaIAEAY 214
PRK07985 PRK07985
SDR family oxidoreductase;
16-213 1.10e-08

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 55.39  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  16 WTRKGKLKieditDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTA--LKAETSERLRTVLL---DVTDPENV 90
Cdd:PRK07985  41 YVGSGRLK-----DRKALVTGGDSGIGRAAAIAYAREGADVAISYLPVEEEDAqdVKKIIEECGRKAVLlpgDLSDEKFA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  91 KRTAQWVKNQVGEKGLWGLInnAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAqGRVINVSSVggrla 170
Cdd:PRK07985 116 RSLVHEAHKALGGLDIMALV--AGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPKG-ASIITTSSI----- 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 214010158 171 ivgGGYTPS---------KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK07985 188 ---QAYQPSphlldyaatKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTAL 236
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
22-212 1.18e-08

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 54.91  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  22 LKIEDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE-TSERLRTVLLDVTDPENVKRTAQWVKNQ 100
Cdd:PRK12481   1 MQLFDLNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEAPETQAQVEaLGRKFHFITADLIQQKDIDSIVSQAVEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 101 VGEKGLwgLINNAGVpgvLAPTDWLTL--EDYREPIEVNLFGLISVTLNMLPLVKKAQ--GRVINVSSVggrLAIVGG-- 174
Cdd:PRK12481  81 MGHIDI--LINNAGI---IRRQDLLEFgnKDWDDVININQKTVFFLSQAVAKQFVKQGngGKIINIASM---LSFQGGir 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 214010158 175 --GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTN 212
Cdd:PRK12481 153 vpSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATD 192
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 26-218 1.37e-08

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 54.73  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLT-ESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQV 101
Cdd:PRK08936   4 DLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSdEEEANDVAEEIKKaggEAIAVKGDVTVESDVVNLIQTAVKEF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 102 GEKGLWglINNAGVPgVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKK--AQGRVINVSSVGGRLAI-VGGGYTP 178
Cdd:PRK08936  84 GTLDVM--INNAGIE-NAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEhdIKGNIINMSSVHEQIPWpLFVHYAA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 214010158 179 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT-----NLADPVK 218
Cdd:PRK08936 161 SKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTpinaeKFADPKQ 205
PRK07074 PRK07074
SDR family oxidoreductase;
28-211 1.43e-08

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 54.78  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  28 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETS-ERLRTVLLDVTDPENVKRTaqwVKNQVGEKGL 106
Cdd:PRK07074   1 TKRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGdARFVPVACDLTDAASLAAA---LANAAAERGP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 107 WG-LINNAGVPGVLAPTDwLTLEDYREPIEVNLFG-LISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGGGYTPSKYAVE 184
Cdd:PRK07074  78 VDvLVANAGAARAASLHD-TTPASWRADNALNLEAaYLCVEAVLEGMLKRSRGAVVNIGSVNGMAALGHPAYSAAKAGLI 156

                        170       180
                 ....*....|....*....|....*..
gi 214010158 185 GFNDSLRRDMKAFGVHVSCIEPGLFKT 211
Cdd:PRK07074 157 HYTKLLAVEYGRFGIRANAVAPGTVKT 183
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 22-212 2.48e-08

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 54.09  E-value: 2.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  22 LKIeDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESG----STALKAETSERLRTVLLDVTDPENVKRTAQWV 97
Cdd:PRK08339   2 LKI-DLSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENlkkaREKIKSESNVDVSYIVADLTKREDLERTVKEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  98 KNqVGEKGLWGLINNAGVPGVLAPtdwLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGGY 176
Cdd:PRK08339  81 KN-IGEPDIFFFSTGGPKPGYFME---MSMEDWEGAVKLLLYPAVYLTRALVPaMERKGFGRIIYSTSVAIKEPIPNIAL 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 214010158 177 TP-SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTN 212
Cdd:PRK08339 157 SNvVRISMAGLVRTLAKELGPKGITVNGIMPGIIRTD 193
PRK06947 PRK06947
SDR family oxidoreductase;
30-213 3.11e-08

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 53.66  E-value: 3.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHViaaCLTESGSTALKAETSE-------RLRTVLLDVTDPENVKRTAQWVKNQVG 102
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSV---GINYARDAAAAEETADavraaggRACVVAGDVANEADVIAMFDAVQSAFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 ekGLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ----GRVINVSSVGGRLaivgGG--- 175
Cdd:PRK06947  80 --RLDALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRggrgGAIVNVSSIASRL----GSpne 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 214010158 176 ---YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK06947 154 yvdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEI 194
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
28-212 3.45e-08

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 53.57  E-value: 3.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  28 TDKYIFITGCDSGFGNLAARTFDKKGFHvIAACLTESGSTALkaETSERLR-------TVLLDVTDPENVKRTAQWVKNQ 100
Cdd:PRK08063   3 SGKVALVTGSSRGIGKAIALRLAEEGYD-IAVNYARSRKAAE--ETAEEIEalgrkalAVKANVGDVEKIKEMFAQIDEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 101 VGekGLWGLINNAGvPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIvgGGYTP- 178
Cdd:PRK08063  80 FG--RLDVFVNNAA-SGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGgGKIISLSSLGSIRYL--ENYTTv 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 214010158 179 --SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTN 212
Cdd:PRK08063 155 gvSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTD 190
PRK12743 PRK12743
SDR family oxidoreductase;
34-215 3.52e-08

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 53.50  E-value: 3.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKGFHV-IAACLTESGSTALKAETSERLR---TVLLDVTDPEnvkRTAQWVKNQVGEKG-LWG 108
Cdd:PRK12743   7 VTASDSGIGKACALLLAQQGFDIgITWHSDEEGAKETAEEVRSHGVraeIRQLDLSDLP---EGAQALDKLIQRLGrIDV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAGVpGVLAPTDWLTLEDYREPIEVNLFGlisVTL-------NMlplVKKAQ-GRVINVSSVGGRLAIVGGG-YTPS 179
Cdd:PRK12743  84 LVNNAGA-MTKAPFLDMDFDEWRKIFTVDVDG---AFLcsqiaarHM---VKQGQgGRIINITSVHEHTPLPGASaYTAA 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 214010158 180 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 215
Cdd:PRK12743 157 KHALGGLTKAMALELVEHGILVNAVAPGAIATPMNG 192
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 26-218 4.97e-08

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: 52.86  E-value: 4.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSErLRTVLLDVTDPENVKRTaqwvknqVGEKG 105
Cdd:cd05351    4 DFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPG-IEPVCVDLSDWDATEEA-------LGSVG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LW-GLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ--GRVINVSSVGGRLAIVG-GGYTPSKY 181
Cdd:cd05351   76 PVdLLVNNAAV-AILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvpGSIVNVSSQASQRALTNhTVYCSTKA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 214010158 182 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKT-----NLADPVK 218
Cdd:cd05351  155 ALDMLTKVMALELGPHKIRVNSVNPTVVMTdmgrdNWSDPEK 196
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
32-209 8.33e-08

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 52.67  E-value: 8.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  32 IFITGCdSGF-GNLAARTFDKKGFHVIAACLTESGSTALKAetSERLRTVLLDVTDPENVKRTAQWVKnqvgekglwGLI 110
Cdd:COG0451    2 ILVTGG-AGFiGSHLARRLLARGHEVVGLDRSPPGAANLAA--LPGVEFVRGDLRDPEALAAALAGVD---------AVV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 111 NNAGVPGVlaptdwlTLEDYREPIEVNLFGlisvTLNMLPLVKKAQ-GRVINVSSVggrlAIVGGGYTP----------- 178
Cdd:COG0451   70 HLAAPAGV-------GEEDPDETLEVNVEG----TLNLLEAARAAGvKRFVYASSS----SVYGDGEGPidedtplrpvs 134

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 214010158 179 ----SKYAVEGFndsLRRDMKAFGVHVSCIEPGLF 209
Cdd:COG0451  135 pygaSKLAAELL---ARAYARRYGLPVTILRPGNV 166
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 30-213 9.30e-08

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: 52.49  E-value: 9.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVkNQVGEkgLWGL 109
Cdd:cd08951    8 KRIFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSSLAETRKLADQV-NAIGR--FDAV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 110 INNAGV---PGVLAPTdwltlEDYREPIEVNLFGLISVTlnmlPLVKKAQgRVINVSS--------------VGGRLAIV 172
Cdd:cd08951   85 IHNAGIlsgPNRKTPD-----TGIPAMVAVNVLAPYVLT----ALIRRPK-RLIYLSSgmhrggnaslddidWFNRGEND 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 214010158 173 GGGYTPSKYAVEGFNDSLRRDMKafGVHVSCIEPGLFKTNL 213
Cdd:cd08951  155 SPAYSDSKLHVLTLAAAVARRWK--DVSSNAVHPGWVPTKM 193
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 29-252 1.09e-07

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: 52.14  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGStALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKG-LW 107
Cdd:cd08937    4 GKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVH-EVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGrVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 108 GLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRlAIVGGGYTPSKYAVEGF 186
Cdd:cd08937   83 VLINNVGGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPhMLERQQGVIVNVSSIATR-GIYRIPYSAAKGGVNAL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 214010158 187 NDSLRRDMKAFGVHVSCIEPGLFKTnladPVKVIEKKLAIWEQLSPDIKQQYGEGYIEKSLDKLKG 252
Cdd:cd08937  162 TASLAFEHARDGIRVNAVAPGGTEA----PPRKIPRNAAPMSEQEKVWYQRIVDQTLDSSLMGRYG 223
PRK07775 PRK07775
SDR family oxidoreductase;
34-227 1.26e-07

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 52.06  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKGFHV------------IAACLTESGSTALkaetserlrTVLLDVTDPENVKRTAQWVKNQV 101
Cdd:PRK07775  15 VAGASSGIGAATAIELAAAGFPValgarrvekceeLVDKIRADGGEAV---------AFPLDVTDPDSVKSFVAQAEEAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 102 GEKGLwgLINNAG--VPGVLAPTDwltLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSS-VGGRLAIVGGGYT 177
Cdd:PRK07775  86 GEIEV--LVSGAGdtYFGKLHEIS---TEQFESQVQIHLVGANRLATAVLPgMIERRRGDLIFVGSdVALRQRPHMGAYG 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 214010158 178 PSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLA--DPVKVIEKKLAIW 227
Cdd:PRK07775 161 AAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGMGwsLPAEVIGPMLEDW 212
PRK07023 PRK07023
SDR family oxidoreductase;
34-213 1.75e-07

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 51.17  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKGFHVIaaCLTESGSTALKAETSERLRTVLLDVTDPEnvkRTAQWVKNQVGEKGLWG----- 108
Cdd:PRK07023   6 VTGHSRGLGAALAEQLLQPGIAVL--GVARSRHPSLAAAAGERLAEVELDLSDAA---AAAAWLAGDLLAAFVDGasrvl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKK-AQGRVINVSSVGGRLAIVG-GGYTPSKYAVEGF 186
Cdd:PRK07023  81 LINNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDaAERRILHISSGAARNAYAGwSVYCATKAALDHH 160

                        170       180
                 ....*....|....*....|....*..
gi 214010158 187 NDSLRRDMKAfGVHVSCIEPGLFKTNL 213
Cdd:PRK07023 161 ARAVALDANR-ALRIVSLAPGVVDTGM 186
PRK06953 PRK06953
SDR family oxidoreductase;
30-213 2.60e-07

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 50.46  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSErlrTVLLDVTDPENVKRTAqWvknQVGEKGLWGL 109
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQALGAE---ALALDVADPASVAGLA-W---KLDGEALDAA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 110 INNAGVPGV-LAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGGG----YTPSKYAVe 184
Cdd:PRK06953  75 VYVAGVYGPrTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSRMGSIGDATGTtgwlYRASKAAL- 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 214010158 185 gfNDSLR---RDMKafgvHVSCI--EPGLFKTNL 213
Cdd:PRK06953 154 --NDALRaasLQAR----HATCIalHPGWVRTDM 181
PRK07035 PRK07035
SDR family oxidoreductase;
26-214 2.63e-07

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 50.78  E-value: 2.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVG 102
Cdd:PRK07035   5 DLTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAaggKAEALACHIGEMEQIDALFAHIRERHG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 EkgLWGLINNAGV-P--GVLAPTDwltLEDYREPIEVNLFGLISVTLNMLPLVKK-AQGRVINVSSVGG-RLAIVGGGYT 177
Cdd:PRK07035  85 R--LDILVNNAAAnPyfGHILDTD---LGAFQKTVDVNIRGYFFMSVEAGKLMKEqGGGSIVNVASVNGvSPGDFQGIYS 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 214010158 178 PSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLA 214
Cdd:PRK07035 160 ITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFA 196
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 34-245 4.58e-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: 50.16  E-value: 4.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALK----AETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwgL 109
Cdd:cd05322    7 VIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVAdeinAEYGEKAYGFGADATNEQSVIALSKGVDEIFKRVDL--L 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 110 INNAGVpGVLAPTDWLTLEDYREPIEVNLFG--LISVTLNMLPLVKKAQGRVINVSSVGGRlaiVGG----GYTPSKYAV 183
Cdd:cd05322   85 VYSAGI-AKSAKITDFELGDFDRSLQVNLVGyfLCAREFSKLMIRDGIQGRIIQINSKSGK---VGSkhnsGYSAAKFGG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 214010158 184 EGFNDSLRRDMKAFGVHVSCIEPG-LFKTNLADP-VKVIEKKLAIweqlSPDIKQQYgegYIEK 245
Cdd:cd05322  161 VGLTQSLALDLAEHGITVNSLMLGnLLKSPMFQSlLPQYAKKLGI----KESEVEQY---YIDK 217
PRK07577 PRK07577
SDR family oxidoreductase;
28-213 5.16e-07

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 49.73  E-value: 5.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  28 TDKYIFITGCDSGFGNLAARTFDKKGFHVIaacltesgstALKAETSERLRTVLL--DVTDPEnvkRTAQWVKNQVGEKG 105
Cdd:PRK07577   2 SSRTVLVTGATKGIGLALSLRLANLGHQVI----------GIARSAIDDFPGELFacDLADIE---QTAATLAQINEIHP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LWGLINNAGV--PGVLAPTDWLTLEDYrepIEVNLFGLISVTLNMLPLVKKA-QGRVINVSSvggrLAIVGG----GYTP 178
Cdd:PRK07577  69 VDAIVNNVGIalPQPLGKIDLAALQDV---YDLNVRAAVQVTQAFLEGMKLReQGRIVNICS----RAIFGAldrtSYSA 141

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 214010158 179 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK07577 142 AKSALVGCTRTWALELAEYGITVNAVAPGPIETEL 176
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 33-217 5.21e-07

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


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 49.44  E-value: 5.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  33 FITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVllDVTDPENVKRTAQwvknQVGEKGLWGLINN 112
Cdd:cd11730    2 LILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALARPA--DVAAELEVWALAQ----ELGPLDLLVYAAG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 113 AGVPGVLAPTdwlTLEDYREPIEVNLFGLISVTLNMLPLVkKAQGRVINVSSVGGRLAIVG-GGYTPSKYAVEGFNDSLR 191
Cdd:cd11730   76 AILGKPLART---KPAAWRRILDANLTGAALVLKHALALL-AAGARLVFLGAYPELVMLPGlSAYAAAKAALEAYVEVAR 151

                        170       180
                 ....*....|....*....|....*.
gi 214010158 192 RDMKafGVHVSCIEPGLFKTNLADPV 217
Cdd:cd11730  152 KEVR--GLRLTLVRPPAVDTGLWAPP 175
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 34-169 5.65e-07

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 49.90  E-value: 5.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAET-----SERLRTVLLDVTDPenvKRTAQWVKNQVGE-KGLW 107
Cdd:cd09808    6 ITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIetesgNQNIFLHIVDMSDP---KQVWEFVEEFKEEgKKLH 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 214010158 108 GLINNAgvpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQG-RVINVSSvGGRL 169
Cdd:cd09808   83 VLINNA---GCMVNKRELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDpRVITVSS-GGML 141
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
26-212 6.07e-07

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 49.87  E-value: 6.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERlrtVLLDVT-DPENVKRTAQWVKNQVGEK 104
Cdd:PRK08993   7 SLEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEPTETIEQVTALGR---RFLSLTaDLRKIDGIPALLERAVAEF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 GLWG-LINNAGVPGVLAPTDWlTLEDYREPIEVNlfglISVTLNMLPLVKK---AQG---RVINVSSVggrLAIVGG--- 174
Cdd:PRK08993  84 GHIDiLVNNAGLIRREDAIEF-SEKDWDDVMNLN----IKSVFFMSQAAAKhfiAQGnggKIINIASM---LSFQGGirv 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 214010158 175 -GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTN 212
Cdd:PRK08993 156 pSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATN 194
PRK05867 PRK05867
SDR family oxidoreductase;
22-232 6.89e-07

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 49.65  E-value: 6.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  22 LKIEDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAAClteSGSTALKAETSE------RLRTVLLDVTDPENVKRTAQ 95
Cdd:PRK05867   2 LDLFDLHGKRALITGASTGIGKRVALAYVEAGAQVAIAA---RHLDALEKLADEigtsggKVVPVCCDVSQHQQVTSMLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  96 WVKNQVGekGLWGLINNAGVPGVLAPTDwLTLEDYREPIEVNLFGL-ISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG 173
Cdd:PRK05867  79 QVTAELG--GIDIAVCNAGIITVTPMLD-MPLEEFQRLQNTNVTGVfLTAQAAAKAMVKQGQgGVIINTASMSGHIINVP 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 214010158 174 ---GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPvkvIEKKLAIWEQLSP 232
Cdd:PRK05867 156 qqvSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEP---YTEYQPLWEPKIP 214
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 29-217 6.92e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 49.80  E-value: 6.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHV---------IAACLTEsgSTALKAETSerLRTVLLDVTDPENVKRTAQWVKN 99
Cdd:PRK05875   7 DRTYLVTGGGSGIGKGVAAGLVAAGAAVmivgrnpdkLAAAAEE--IEALKGAGA--VRYEPADVTDEDQVARAVDAATA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 100 QVGekGLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNML-PLVKKAQGRVINVSSVGG----RLAivgG 174
Cdd:PRK05875  83 WHG--RLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAArELVRGGGGSFVGISSIAAsnthRWF---G 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 214010158 175 GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPV 217
Cdd:PRK05875 158 AYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPI 200
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 23-212 7.18e-07

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 49.90  E-value: 7.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  23 KIEDITDKYIFITGCDSGFGNLAARTFDKKGFHV------------IAACLTESGSTALKAETserlrtvllDVTDPENV 90
Cdd:PRK08277   4 NLFSLKGKVAVITGGGGVLGGAMAKELARAGAKVaildrnqekaeaVVAEIKAAGGEALAVKA---------DVLDKESL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  91 KRTAQWVKNQVGEKGLwgLINNAG--VPGvlAPTDW--------------LTLEDYREPIEVNLFGlisvtlNMLP---- 150
Cdd:PRK08277  75 EQARQQILEDFGPCDI--LINGAGgnHPK--ATTDNefhelieptktffdLDEEGFEFVFDLNLLG------TLLPtqvf 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 151 ---LVKKAQGRVINVSSVGG-----RLAivggGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTN 212
Cdd:PRK08277 145 akdMVGRKGGNIINISSMNAftpltKVP----AYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTE 210
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 27-214 1.11e-06

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


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 49.08  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  27 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTES----GSTALKAETSERLRTVLlDVTDPENVKRTAQWVKNQVG 102
Cdd:cd08936    8 LANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQnvdrAVATLQGEGLSVTGTVC-HVGKAEDRERLVATAVNLHG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 103 ekGLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPSK 180
Cdd:cd08936   87 --GVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPeMEKRGGGSVVIVSSVAAFHPFPGlGPYNVSK 164

                        170       180       190
                 ....*....|....*....|....*....|....
gi 214010158 181 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLA 214
Cdd:cd08936  165 TALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFS 198
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 34-225 1.18e-06

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: 49.00  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERL----RTVLLDVTDPENVKRTAQWVKNQVGekGLWGL 109
Cdd:cd05337    6 VTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAgrraIYFQADIGELSDHEALLDQAWEDFG--RLDCL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 110 INNAGVpGVLAPTDWL--TLEDYREPIEVNLFGLI----SVTLNMLPLVKKAQG---RVINVSSVGGRLAIVG-GGYTPS 179
Cdd:cd05337   84 VNNAGI-AVRPRGDLLdlTEDSFDRLIAINLRGPFfltqAVARRMVEQPDRFDGphrSIIFVTSINAYLVSPNrGEYCIS 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 214010158 180 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVK-VIEKKLA 225
Cdd:cd05337  163 KAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKeKYDELIA 209
PRK07814 PRK07814
SDR family oxidoreductase;
27-207 1.45e-06

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 48.62  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  27 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLR---TVLLDVTDPENvkrTAQWVKNQVGE 103
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRrahVVAADLAHPEA---TAGLAGQAVEA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 104 KG-LWGLINNAG--VPGVLAPTdwlTLEDYREPIEVNLFGLISVTLNMLPLVKK--AQGRVINVSSVGGRLAIVG-GGYT 177
Cdd:PRK07814  85 FGrLDIVVNNVGgtMPNPLLST---STKDLADAFTFNVATAHALTVAAVPLMLEhsGGGSVINISSTMGRLAGRGfAAYG 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 214010158 178 PSKYAVEGFNDSLRRDMkAFGVHVSCIEPG 207
Cdd:PRK07814 162 TAKAALAHYTRLAALDL-CPRIRVNAIAPG 190
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 30-232 2.22e-06

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 47.96  E-value: 2.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGC--DSGFGNLAARTFDKKGFHVIAACLTESGS---TALKAETSERLRTVLLDVTDPENVKRTAqwvkNQVGEK 104
Cdd:cd05372    2 KRILITGIanDRSIAWGIAKALHEAGAELAFTYQPEALRkrvEKLAERLGESALVLPCDVSNDEEIKELF----AEVKKD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 glWGLINnagvpGVL-----APTDWL-------TLEDYREPIEVNLFGLISVTLNMLPLVKKaQGRVINVSSVGGRLAIV 172
Cdd:cd05372   78 --WGKLD-----GLVhsiafAPKVQLkgpfldtSRKGFLKALDISAYSLVSLAKAALPIMNP-GGSIVTLSYLGSERVVP 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 214010158 173 G-GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSP 232
Cdd:cd05372  150 GyNVMGVAKAALESSVRYLAYELGRKGIRVNAISAGPIKTLAASGITGFDKMLEYSEQRAP 210
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 24-214 2.26e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 48.48  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  24 IEDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACL-TESGSTALKAETSER----LRTVLLDVTDPENVKRTAQWVK 98
Cdd:PRK06197  11 IPDQSGRVAVVTGANTGLGYETAAALAAKGAHVVLAVRnLDKGKAAAARITAATpgadVTLQELDLTSLASVRAAADALR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  99 NQVGEKGLwgLINNAgvpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQG-RVINVSSVGGRL--AI---- 171
Cdd:PRK06197  91 AAYPRIDL--LINNA---GVMYTPKQTTADGFELQFGTNHLGHFALTGLLLDRLLPVPGsRVVTVSSGGHRIraAIhfdd 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 214010158 172 --------VGGGYTPSKYAVEGFNDSLRRDMKAFGVHVSCI--EPGLFKTNLA 214
Cdd:PRK06197 166 lqwerrynRVAAYGQSKLANLLFTYELQRRLAAAGATTIAVaaHPGVSNTELA 218
PRK06196 PRK06196
oxidoreductase; Provisional
 26-227 2.82e-06

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 48.14  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVI-AACLTESGSTALKAetSERLRTVLLDVTDPENVKRTAqwvkNQVGEK 104
Cdd:PRK06196  23 DLSGKTAIVTGGYSGLGLETTRALAQAGAHVIvPARRPDVAREALAG--IDGVEVVMLDLADLESVRAFA----ERFLDS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 105 G--LWGLINNAgvpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQG-RVINVSSVGGRLAIV-------GG 174
Cdd:PRK06196  97 GrrIDILINNA---GVMACPETRVGDGWEAQFATNHLGHFALVNLLWPALAAGAGaRVVALSSAGHRRSPIrwddphfTR 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 214010158 175 GYTP------SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIW 227
Cdd:PRK06196 174 GYDKwlaygqSKTANALFAVHLDKLGKDQGVRAFSVHPGGILTPLQRHLPREEQVALGW 232
PRK06123 PRK06123
SDR family oxidoreductase;
29-213 3.11e-06

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 47.47  E-value: 3.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHV-------------IAACLTESGSTALkaetserlrTVLLDVTDPENVKRTAQ 95
Cdd:PRK06123   2 RKVMIITGASRGIGAATALLAAERGYAVclnylrnrdaaeaVVQAIRRQGGEAL---------AVAADVADEADVLRLFE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  96 WVKNQVGEkgLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLI----SVTLNMLPLVKKAQGRVINVSSVGGRLAI 171
Cdd:PRK06123  73 AVDRELGR--LDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSFlcarEAVKRMSTRHGGRGGAIVNVSSMAARLGS 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 214010158 172 VGG--GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK06123 151 PGEyiDYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEI 194
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 29-207 3.86e-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: 47.59  E-value: 3.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTA-----LKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGE 103
Cdd:cd09809    1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAavsriLEEWHKARVEAMTLDLASLRSVQRFAEAFKAKNSP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 104 kgLWGLINNAGVPGVlaptDW-LTLEDYREPIEVNLFGLISVTLNMLPLVKK-AQGRVINVSS----------VGGRLAI 171
Cdd:cd09809   81 --LHVLVCNAAVFAL----PWtLTEDGLETTFQVNHLGHFYLVQLLEDVLRRsAPARVIVVSSeshrftdlpdSCGNLDF 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 214010158 172 VGGGYTPSKY-AVEGFNDS----------LRRDMKAFGVHVSCIEPG 207
Cdd:cd09809  155 SLLSPPKKKYwSMLAYNRAklcnilfsneLHRRLSPRGITSNSLHPG 201
PRK09730 PRK09730
SDR family oxidoreductase;
34-213 4.33e-06

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 47.15  E-value: 4.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKGFHV-------IAAC------LTESG--STALKAetserlrtvllDVTDPENVKRTAQWVK 98
Cdd:PRK09730   6 VTGGSRGIGRATALLLAQEGYTVavnyqqnLHAAqevvnlITQAGgkAFVLQA-----------DISDENQVVAMFTAID 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  99 NQVGEkgLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLIsvtLNMLPLVKKAQ-------GRVINVSSVGGRLAI 171
Cdd:PRK09730  75 QHDEP--LAALVNNAGILFTQCTVENLTAERINRVLSTNVTGYF---LCCREAVKRMAlkhggsgGAIVNVSSAASRLGA 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 214010158 172 VGG--GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK09730 150 PGEyvDYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEM 193
PRK12742 PRK12742
SDR family oxidoreductase;
26-213 5.48e-06

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 46.67  E-value: 5.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVI----------AACLTESGSTALKAETSERLRTV-LLDVTDPENVkrta 94
Cdd:PRK12742   3 AFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRftyagskdaaERLAQETGATAVQTDSADRDAVIdVVRKSGALDI---- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  95 qwvknqvgekglwgLINNAGVpgvLAPTDWLTL--EDYREPIEVNL----FGLISVTLNMlplvkKAQGRVINVSSVGG- 167
Cdd:PRK12742  79 --------------LVVNAGI---AVFGDALELdaDDIDRLFKINIhapyHASVEAARQM-----PEGGRIIIIGSVNGd 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 214010158 168 RLAIVGG-GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK12742 137 RMPVAGMaAYAASKSALQGMARGLARDFGPRGITINVVQPGPIDTDA 183
PRK06128 PRK06128
SDR family oxidoreductase;
34-213 5.58e-06

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 47.16  E-value: 5.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKA----ETSERLRTVLL-DVTDPENVKRTAQWVKNQVGekGLWG 108
Cdd:PRK06128  60 ITGADSGIGRATAIAFAREGADIALNYLPEEEQDAAEVvqliQAEGRKAVALPgDLKDEAFCRQLVERAVKELG--GLDI 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVkKAQGRVINVSSVggrlaivgGGYTPS--------- 179
Cdd:PRK06128 138 LVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHL-PPGASIINTGSI--------QSYQPSptlldyast 208

                        170       180       190
                 ....*....|....*....|....*....|....
gi 214010158 180 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK06128 209 KAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPL 242
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 34-186 6.27e-06

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 47.13  E-value: 6.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKG-FHVIAACLTESGSTALKAET---SERLRTVLLDVTDPENVKrtaQWVKN-QVGEKGLWG 108
Cdd:cd09810    6 ITGASSGLGLAAAKALARRGeWHVVMACRDFLKAEQAAQEVgmpKDSYSVLHCDLASLDSVR---QFVDNfRRTGRPLDA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAGVPGVLAPTDWLTLEDYREPIEVNLFG---LISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGGGyTPSKY---A 182
Cdd:cd09810   83 LVCNAAVYLPTAKEPRFTADGFELTVGVNHLGhflLTNLLLEDLQRSENASPRIVIVGSITHNPNTLAGN-VPPRAtlgD 161


                 ....
gi 214010158 183 VEGF 186
Cdd:cd09810  162 LEGL 165
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 27-216 6.57e-06

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 46.87  E-value: 6.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  27 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGL 106
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAFG--KL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 107 WGLINNAGVPGVLAP---TDWLTLED-YREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAivGGG---YTPS 179
Cdd:PRK06200  82 DCFVGNAGIWDYNTSlvdIPAETLDTaFDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLSNSSFYP--GGGgplYTAS 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 214010158 180 KYAVEGFNDSLRRDMkAFGVHVSCIEPGLFKTNLADP 216
Cdd:PRK06200 160 KHAVVGLVRQLAYEL-APKIRVNGVAPGGTVTDLRGP 195
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-211 2.47e-05

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 45.60  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGsTALkAETSERLR--TVLLDVTDPENVKRTAQWVKNQVGekGLWGLIN 111
Cdd:PRK08261 215 VTGAARGIGAAIAEVLARDGAHVVCLDVPAAG-EAL-AAVANRVGgtALALDITAPDAPARIAEHLAERHG--GLDIVVH 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 112 NAGVP--GVLAPTDwltlEDY-REPIEVNLFGLISVTLNML-PLVKKAQGRVINVSSVGGrlaIVGG----GYTPSKYAV 183
Cdd:PRK08261 291 NAGITrdKTLANMD----EARwDSVLAVNLLAPLRITEALLaAGALGDGGRIVGVSSISG---IAGNrgqtNYAASKAGV 363

                        170       180
                 ....*....|....*....|....*...
gi 214010158 184 EGFNDSLRRDMKAFGVHVSCIEPGLFKT 211
Cdd:PRK08261 364 IGLVQALAPLLAERGITINAVAPGFIET 391
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 30-207 3.20e-05

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 44.67  E-value: 3.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGEkgL 106
Cdd:PRK07677   2 KVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQfpgQVLTVQMDVRNPEDVQKMVEQIDEKFGR--I 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 107 WGLINNAGvPGVLAPTDWLTLEDYREPIEVNLFG--LISVTLNMLPLVKKAQGRVINVSSVGGRLAivGGGYTPSKYAVE 184
Cdd:PRK07677  80 DALINNAA-GNFICPAEDLSVNGWNSVIDIVLNGtfYCSQAVGKYWIEKGIKGNIINMVATYAWDA--GPGVIHSAAAKA 156

                        170       180
                 ....*....|....*....|....*...
gi 214010158 185 GFNdSLRRDM-----KAFGVHVSCIEPG 207
Cdd:PRK07677 157 GVL-AMTRTLavewgRKYGIRVNAIAPG 183
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 33-218 3.84e-05

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 44.18  E-value: 3.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  33 FITGCDSGFGNLAARTFDKKGFHVIaacLTESGSTALKAETSERLRT-------VLLDVTDPENVKRTAQWVKNQVGekG 105
Cdd:PRK12745   6 LVTGGRRGIGLGIARALAAAGFDLA---INDRPDDEELAATQQELRAlgvevifFPADVADLSAHEAMLDAAQAAWG--R 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 106 LWGLINNAGVpGVLAPTDWL--TLEDYREPIEVNLFGLI----SVTLNMLPLVKKAQGR---VINVSSV-GGRLAIVGGG 175
Cdd:PRK12745  81 IDCLVNNAGV-GVKVRGDLLdlTPESFDRVLAINLRGPFfltqAVAKRMLAQPEPEELPhrsIVFVSSVnAIMVSPNRGE 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 214010158 176 YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVK 218
Cdd:PRK12745 160 YCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPVT 202
PLN00015 PLN00015
protochlorophyllide reductase
 34-178 4.02e-05

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 44.70  E-value: 4.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  34 ITGCDSGFGNLAARTFDKKG-FHVIAACLT-ESGSTALK-AETSERLRTVL-LDVTDPENVKrtaQWVKN-QVGEKGLWG 108
Cdd:PLN00015   2 ITGASSGLGLATAKALAETGkWHVVMACRDfLKAERAAKsAGMPKDSYTVMhLDLASLDSVR---QFVDNfRRSGRPLDV 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 214010158 109 LINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKA---QGRVINVSSVGGRLAIVGGGYTP 178
Cdd:PLN00015  79 LVCNAAVYLPTAKEPTFTADGFELSVGTNHLGHFLLSRLLLDDLKKSdypSKRLIIVGSITGNTNTLAGNVPP 151
PRK06500 PRK06500
SDR family oxidoreductase;
29-237 5.06e-05

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 43.79  E-value: 5.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  29 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEkgLWG 108
Cdd:PRK06500   6 GKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAAQKALAQALAEAFGR--LDA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAGVpgvlapTDWLTLEDYREP-----IEVNLFGLISVTLNMLPLVKKAQGRVINvSSVGGRLAIVGGG-YTPSKYA 182
Cdd:PRK06500  84 VFINAGV------AKFAPLEDWDEAmfdrsFNTNVKGPYFLIQALLPLLANPASIVLN-GSINAHIGMPNSSvYAASKAA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 214010158 183 VEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLaiwEQLSPDIKQQ 237
Cdd:PRK06500 157 LLSLAKTLSGELLPRGIRVNAVSPGPVQTPLYGKLGLPEATL---DAVAAQIQAL 208
PRK08177 PRK08177
SDR family oxidoreductase;
30-213 5.45e-05

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 43.48  E-value: 5.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTvlLDVTDPENVKRTAQWVKNQVGEKglwgL 109
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIEK--LDMNDPASLDQLLQRLQGQRFDL----L 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 110 INNAGVPGVLA-PTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGGG----YTPSKYAVE 184
Cdd:PRK08177  76 FVNAGISGPAHqSAADATAAEIGQLFLTNAIAPIRLARRLLGQVRPGQGVLAFMSSQLGSVELPDGGemplYKASKAALN 155

                        170       180
                 ....*....|....*....|....*....
gi 214010158 185 GFNDSLRRDMKAFGVHVSCIEPGLFKTNL 213
Cdd:PRK08177 156 SMTRSFVAELGEPTLTVLSMHPGWVKTDM 184
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 97-217 9.12e-05

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 43.14  E-value: 9.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  97 VKNQVGEKGLWGLINNAGV-PGvlAPTDWLTLEDYREPIEVNL---FGLISVTLNMLplvkKAQGRVINVSSVGGRLAIV 172
Cdd:PRK12747  80 LQNRTGSTKFDILINNAGIgPG--AFIEETTEQFFDRMVSVNAkapFFIIQQALSRL----RDNSRIINISSAATRISLP 153

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 214010158 173 GG-GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTN-----LADPV 217
Cdd:PRK12747 154 DFiAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDmnaelLSDPM 204
PRK09186 PRK09186
flagellin modification protein A; Provisional
 27-207 1.56e-04

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 42.67  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  27 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE-----TSERLRTVLLDVTDPENVKRTAQWVKNQV 101
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESlgkefKSKKLSLVELDITDQESLEEFLSKSAEKY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 102 GEkgLWGLINNAgVPgvlAPTDW------LTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLA---- 170
Cdd:PRK09186  82 GK--IDGAVNCA-YP---RNKDYgkkffdVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGgGNLVNISSIYGVVApkfe 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 214010158 171 ---------------IVGGGYTPSKYAVEGFNDSlrrdmkafGVHVSCIEPG 207
Cdd:PRK09186 156 iyegtsmtspveyaaIKAGIIHLTKYLAKYFKDS--------NIRVNCVSPG 199
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 109-207 2.18e-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: 41.92  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAGV--PGVLAPTdwlTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSKYAVE 184
Cdd:cd05353   92 LVNNAGIlrDRSFAKM---SEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKfGRIINTSSAAGLYGNFGqANYSAAKLGLL 168

                         90       100
                 ....*....|....*....|...
gi 214010158 185 GFNDSLRRDMKAFGVHVSCIEPG 207
Cdd:cd05353  169 GLSNTLAIEGAKYNITCNTIAPA 191
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
32-171 2.32e-04

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


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 42.29  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  32 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSER---LRTVLLDVTDPENVKRTAqwvkNQVGEKG--L 106
Cdd:COG5748    9 VIITGASSGVGLYAAKALADRGWHVIMACRDLEKAEAAAQELGIPpdsYTIIHIDLASLESVRRFV----ADFRALGrpL 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 214010158 107 WGLINNAGV--PGVLAPTdwLTLEDYREPIEVNLFGLISVTLNMLPLVKK---AQGRVINVSSV-------GGRLAI 171
Cdd:COG5748   85 DALVCNAAVyyPLLKEPL--RSPDGYELSVATNHLGHFLLCNLLLEDLKKspaSDPRLVILGTVtanpkelGGKIPI 159
PRK07831 PRK07831
SDR family oxidoreductase;
39-208 2.58e-04

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 41.94  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  39 SGFGNLAARTFDKKGFHVI-----AACLTESgSTALKAETSE-RLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGLINN 112
Cdd:PRK07831  28 TGIGSATARRALEEGARVVisdihERRLGET-ADELAAELGLgRVEAVVCDVTSEAQVDALIDAAVERLG--RLDVLVNN 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 113 AGVPGVLAPTDwLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ--GRVINVSSVGGRLAIVGGG-YTPSKYAVEGFNDS 189
Cdd:PRK07831 105 AGLGGQTPVVD-MTDDEWSRVLDVTLTGTFRATRAALRYMRARGhgGVIVNNASVLGWRAQHGQAhYAAAKAGVMALTRC 183

                        170
                 ....*....|....*....
gi 214010158 190 LRRDMKAFGVHVSCIEPGL 208
Cdd:PRK07831 184 SALEAAEYGVRINAVAPSI 202
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
 32-164 5.39e-04

CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that catalyzes the conversion of CDP-D-paratose to CDP-D-tyvelose, the last step in tyvelose biosynthesis. This subgroup is a member of the extended SDR subfamily, with a characteristic active site tetrad and NAD-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187568 [Multi-domain]  Cd Length: 337  Bit Score: 41.12  E-value: 5.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  32 IFITGcDSGF-GNLAARTFDKKGFHVIAA-CLTESGSTA----LKA-ETSERLRTVLLDV---TDPENVKRTAQWVknqv 101
Cdd:cd05258    3 VLITG-GAGFiGSNLARFFLKQGWEVIGFdNLMRRGSFGnlawLKAnREDGGVRFVHGDIrnrNDLEDLFEDIDLI---- 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 214010158 102 gekglwglINNAGVPGVLAptdwlTLEDYREPIEVNLFGlisvTLNMLPLVKKA--QGRVINVSS 164
Cdd:cd05258   78 --------IHTAAQPSVTT-----SASSPRLDFETNALG----TLNVLEAARQHapNAPFIFTST 125
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 32-213 8.28e-04

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: 39.87  E-value: 8.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  32 IFITGCDSGFGNLAARTFDKKGFHVIAAcltesGSTAlkaetserlRTVLLDVTDPENVKRTAQwvknQVGEkgLWGLIN 111
Cdd:cd11731    1 IIVIGATGTIGLAVAQLLSAHGHEVITA-----GRSS---------GDYQVDITDEASIKALFE----KVGH--FDAIVS 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 112 NAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKaqGRVINVSS---------VGGRLAIVGGgytpskyA 182
Cdd:cd11731   61 TAGD-AEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYLND--GGSITLTSgilaqrpipGGAAAATVNG-------A 130

                        170       180       190
                 ....*....|....*....|....*....|.
gi 214010158 183 VEGFNDSLRRDMKAfGVHVSCIEPGLFKTNL 213
Cdd:cd11731  131 LEGFVRAAAIELPR-GIRINAVSPGVVEESL 160
PRK05854 PRK05854
SDR family oxidoreductase;
109-213 8.55e-04

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 40.43  E-value: 8.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 109 LINNAgvpGVLAPTDWLTLEDYRE-PIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIV-------------GG 174
Cdd:PRK05854  97 LINNA---GVMTPPERQTTADGFElQFGTNHLGHFALTAHLLPLLRAGRARVTSQSSIAARRGAInwddlnwersyagMR 173

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 214010158 175 GYTPSKYAVEGFNDSLRRDMKA--FGVHVSCIEPGLFKTNL 213
Cdd:PRK05854 174 AYSQSKIAVGLFALELDRRSRAagWGITSNLAHPGVAPTNL 214
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 30-164 8.87e-04

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: 40.26  E-value: 8.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  30 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGL 109
Cdd:cd09761    2 KVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLG--RIDVL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 214010158 110 INNAGV--PGVLAPtdwLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSS 164
Cdd:cd09761   80 VNNAARgsKGILSS---LLLEEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIAS 133
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 26-215 1.03e-03

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 40.09  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  26 DITDKYIFITGCDSGFGNLAARTFDKKGFHVI--AACLTESGSTALK--AETSERLRTVLLDVTDPENVKRTAQWVKNQV 101
Cdd:PRK06077   3 SLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVvnAKKRAEEMNETLKmvKENGGEGIGVLADVSTREGCETLAKATIDRY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 102 GekGLWGLINNAGVpGVLAPtdWLTLED--YREPIEVNLFGLISVTlNMLPLVKKAQGRVINVSSVGGRLAIVG-GGYTP 178
Cdd:PRK06077  83 G--VADILVNNAGL-GLFSP--FLNVDDklIDKHISTDFKSVIYCS-QELAKEMREGGAIVNIASVAGIRPAYGlSIYGA 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 214010158 179 SKYAVEGFNDSLRRDMkAFGVHVSCIEPGLFKTNLAD 215
Cdd:PRK06077 157 MKAAVINLTKYLALEL-APKIRVNAIAPGFVKTKLGE 192
PRK08703 PRK08703
SDR family oxidoreductase;
27-183 3.66e-03

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 38.37  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158  27 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE-------RLRTVLLDVTDPENVKRTAQWVKN 99
Cdd:PRK08703   4 LSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEaghpepfAIRFDLMSAEEKEFEQFAATIAEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010158 100 QVGEkgLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKA-QGRVINV-SSVGGRLAIVGGGYT 177
Cdd:PRK08703  84 TQGK--LDGIVHCAGYFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSpDASVIFVgESHGETPKAYWGGFG 161


                 ....*.
gi 214010158 178 PSKYAV 183
Cdd:PRK08703 162 ASKAAL 167
 
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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