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Conserved domains on  [gi|576796343|ref|NP_001276692|]
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dehydrogenase/reductase SDR family member 9 isoform 2 [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; ...
 90-366 3.36e-160

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: 450.58  E-value: 3.36e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTE--SGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLW 167
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 168 GLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAI-VGGGYTPSKYAVEGF 246
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFpAGGAYCASKAAVEAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 247 NDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEK-KLAIWEQLSPDIKQQYGEGYIEKSLDKLKGNKSYVNMDLSPVV 325
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKqAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 576796343 326 ECMDHALTSLFPKTHYAAGKDAKIFWIPLSHMPAALQDFLL 366
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; ...
 90-366 3.36e-160

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: 450.58  E-value: 3.36e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTE--SGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLW 167
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 168 GLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAI-VGGGYTPSKYAVEGF 246
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFpAGGAYCASKAAVEAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 247 NDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEK-KLAIWEQLSPDIKQQYGEGYIEKSLDKLKGNKSYVNMDLSPVV 325
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKqAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 576796343 326 ECMDHALTSLFPKTHYAAGKDAKIFWIPLSHMPAALQDFLL 366
Cdd:cd09805  241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 88-293 1.80e-52

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: 174.21  E-value: 1.80e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  88 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLW 167
Cdd:COG4221    4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFG--RLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 168 GLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYAVEG 245
Cdd:COG4221   82 VLVNNAGV-ALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPaMRARGSGHIVNISSIAGLRPYPGGAvYAATKAAVRG 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 576796343 246 FNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAI-----WEQLSPD 293
Cdd:COG4221  161 LSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAavyegLEPLTPE 213
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 90-277 9.21e-45

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 152.77  E-value: 9.21e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343   90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE---TSERLRTVLLDVTDPENVKRTAQWVKNQVGekGL 166
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKElgaLGGKALFIQGDVTDRAQVKALVEQAVERLG--RL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  167 WGLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLA-IVGGGYTPSKYAVE 244
Cdd:pfam00106  79 DILVNNAGITGL-GPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPyPGGSAYSASKAAVI 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 576796343  245 GFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPV 277
Cdd:pfam00106 158 GFTRSLALELAPHGIRVNAVAPGGVDTDMTKEL 190
PRK06914 PRK06914
SDR family oxidoreductase;
90-368 6.90e-44

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 153.26  E-value: 6.90e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAET-----SERLRTVLLDVTDPENVKrTAQWVKNQVGEK 164
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQAtqlnlQQNIKVQQLDVTDQNSIH-NFQLVLKEIGRI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 GLwgLINNAG--VPGVLaptDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSK 240
Cdd:PRK06914  83 DL--LVNNAGyaNGGFV---EEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGlSPYVSSK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 241 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNladpvkviekklaIWE------QLSPDIKQQYGEgYIEKSLDKL-KGN 313
Cdd:PRK06914 158 YALEGFSESLRLELKPFGIDVALIEPGSYNTN-------------IWEvgkqlaENQSETTSPYKE-YMKKIQKHInSGS 223

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 576796343 314 KSYVNMDlsPVVECMDHALTSLFPKTHYAAGKDAKIFWIPLSHMPAALQDFLLLK 368
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; ...
 90-366 3.36e-160

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: 450.58  E-value: 3.36e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTE--SGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLW 167
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 168 GLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAI-VGGGYTPSKYAVEGF 246
Cdd:cd09805   81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFpAGGAYCASKAAVEAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 247 NDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEK-KLAIWEQLSPDIKQQYGEGYIEKSLDKLKGNKSYVNMDLSPVV 325
Cdd:cd09805  161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKqAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 576796343 326 ECMDHALTSLFPKTHYAAGKDAKIFWIPLSHMPAALQDFLL 366
Cdd:cd09805  241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 90-348 5.86e-62

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: 5.86e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRtaqwVKNQVGEKG--LW 167
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKA----AVKEVIERFgrID 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 168 GLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYAVEG 245
Cdd:cd05374   77 VLVNNAGY-GLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPlMRKQGSGRIVNVSSVAGLVPTPFLGpYCASKAALEA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 246 FNDSLRRDMKAFGVHVSCIEPGLFKTNLADPvkviekklaiweQLSPDIKQQYGEGY--IEKSLDKLKGNKSYVNMDLSP 323
Cdd:cd05374  156 LSESLRLELAPFGIKVTIIEPGPVRTGFADN------------AAGSALEDPEISPYapERKEIKENAAGVGSNPGDPEK 223

                        250       260
                 ....*....|....*....|....*
gi 576796343 324 VVECMDHALTSLFPKTHYAAGKDAK 348
Cdd:cd05374  224 VADVIVKALTSESPPLRYFLGSDAL 248
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 88-293 1.80e-52

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: 174.21  E-value: 1.80e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  88 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLW 167
Cdd:COG4221    4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFG--RLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 168 GLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYAVEG 245
Cdd:COG4221   82 VLVNNAGV-ALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPaMRARGSGHIVNISSIAGLRPYPGGAvYAATKAAVRG 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 576796343 246 FNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAI-----WEQLSPD 293
Cdd:COG4221  161 LSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAavyegLEPLTPE 213
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
87-365 2.05e-52

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 174.67  E-value: 2.05e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  87 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE---TSERLRTVLLDVTDPENVKRTAQWVKNQVGe 163
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAElraAGARVEVVALDVTDPDAVAALAEAVLARFG- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 164 kGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPSKY 241
Cdd:COG0300   82 -PIDVLVNNAGV-GGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPlMRARGRGRIVNVSSVAGLRGLPGmAAYAASKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 242 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAiweqLSPDIkqqygegyieksldklkgnksyvnmdl 321
Cdd:COG0300  160 ALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPL----LSPEE--------------------------- 208

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 576796343 322 spVVECMDHALTSlfPKTHYAAGKDAKIFWIPLSHMPAALQDFL 365
Cdd:COG0300  209 --VARAILRALER--GRAEVYVGWDARLLARLLRLLPRLFDRLL 248
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 90-277 9.21e-45

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 152.77  E-value: 9.21e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343   90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE---TSERLRTVLLDVTDPENVKRTAQWVKNQVGekGL 166
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKElgaLGGKALFIQGDVTDRAQVKALVEQAVERLG--RL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  167 WGLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLA-IVGGGYTPSKYAVE 244
Cdd:pfam00106  79 DILVNNAGITGL-GPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPyPGGSAYSASKAAVI 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 576796343  245 GFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPV 277
Cdd:pfam00106 158 GFTRSLALELAPHGIRVNAVAPGGVDTDMTKEL 190
PRK06914 PRK06914
SDR family oxidoreductase;
90-368 6.90e-44

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 153.26  E-value: 6.90e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAET-----SERLRTVLLDVTDPENVKrTAQWVKNQVGEK 164
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQAtqlnlQQNIKVQQLDVTDQNSIH-NFQLVLKEIGRI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 GLwgLINNAG--VPGVLaptDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSK 240
Cdd:PRK06914  83 DL--LVNNAGyaNGGFV---EEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGlSPYVSSK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 241 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNladpvkviekklaIWE------QLSPDIKQQYGEgYIEKSLDKL-KGN 313
Cdd:PRK06914 158 YALEGFSESLRLELKPFGIDVALIEPGSYNTN-------------IWEvgkqlaENQSETTSPYKE-YMKKIQKHInSGS 223

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 576796343 314 KSYVNMDlsPVVECMDHALTSLFPKTHYAAGKDAKIFWIPLSHMPAALQDFLLLK 368
Cdd:PRK06914 224 DTFGNPI--DVANLIVEIAESKRPKLRYPIGKGVKLMILAKKILPWRLWEYLVLK 276
PRK05993 PRK05993
SDR family oxidoreductase;
90-369 5.36e-43

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 150.95  E-value: 5.36e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETserLRTVLLDVTDPENVKRTAQWVKNQVGEKgLWGL 169
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEAEG---LEAFQLDYAEPESIAALVAQVLELSGGR-LDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 170 INNA--GVPGVLA--PTDWLtledyREPIEVNLFGLISVTLNMLPLVKK-AQGRVINVSSVGGRLAI-VGGGYTPSKYAV 243
Cdd:PRK05993  81 FNNGayGQPGAVEdlPTEAL-----RAQFEANFFGWHDLTRRVIPVMRKqGQGRIVQCSSILGLVPMkYRGAYNASKFAI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 244 EGFNDSLRRDMKAFGVHVSCIEPGLFKTNL-ADPVKVIEKKLaiweqlspDIKQQ-YGEGYiEKSLDKLKGNKSYVNMDL 321
Cdd:PRK05993 156 EGLSLTLRMELQGSGIHVSLIEPGPIETRFrANALAAFKRWI--------DIENSvHRAAY-QQQMARLEGGGSKSRFKL 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 576796343 322 SP--VVECMDHALTSLFPKTHYAAGKDAKIFWIPLSHMPAALQDFLLLKQ 369
Cdd:PRK05993 227 GPeaVYAVLLHALTAPRPRPHYRVTTPAKQGALLKRLLPARWLYRLLRKA 276
PRK06182 PRK06182
short chain dehydrogenase; Validated
 90-348 2.27e-39

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 141.25  E-value: 2.27e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAAC--------LTESGSTALKaetserlrtvlLDVTDPENVKRTAQWVKNQV 161
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYGAArrvdkmedLASLGVHPLS-----------LDVTDEASIKAAVDTIIAEE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 162 GEKGLwgLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLA-IVGGGYTPS 239
Cdd:PRK06182  73 GRIDV--LVNNAGY-GSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIYtPLGAWYHAT 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 240 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADpvkVIEKKLAIWEQLSPdikqqYGE--GYIEKSLDKLKGNksyv 317
Cdd:PRK06182 150 KFALEGFSDALRLEVAPFGIDVVVIEPGGIKTEWGD---IAADHLLKTSGNGA-----YAEqaQAVAASMRSTYGS---- 217

                        250       260       270
                 ....*....|....*....|....*....|...
gi 576796343 318 NMDLSP--VVECMDHALTSLFPKTHYAAGKDAK 348
Cdd:PRK06182 218 GRLSDPsvIADAISKAVTARRPKTRYAVGFGAK 250
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 90-274 1.46e-37

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 136.58  E-value: 1.46e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGL 169
Cdd:PRK06180   5 KTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFG--PIDVL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 170 INNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPSKYAVEGFN 247
Cdd:PRK06180  83 VNNAGY-GHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPgMRARRRGHIVNITSMGGLITMPGiGYYCGSKFALEGIS 161

                        170       180
                 ....*....|....*....|....*..
gi 576796343 248 DSLRRDMKAFGVHVSCIEPGLFKTNLA 274
Cdd:PRK06180 162 ESLAKEVAPFGIHVTAVEPGSFRTDWA 188
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 92-286 1.63e-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: 135.10  E-value: 1.63e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  92 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESG--STALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGL 169
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEAlaELAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFG--RLDIL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 170 INNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSKYAVEGFN 247
Cdd:cd05233   79 VNNAGI-ARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGgGRIVNISSVAGLRPLPGqAAYAASKAALEGLT 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 576796343 248 DSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAI 286
Cdd:cd05233  158 RSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKEL 196
PRK08017 PRK08017
SDR family oxidoreductase;
90-277 2.66e-37

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 135.21  E-value: 2.66e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLtesgstalKAETSERLRT-----VLLDVTDPENVKRTAQWVKNQVGEK 164
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAACR--------KPDDVARMNSlgftgILLDLDDPESVERAADEVIALTDNR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 gLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPSKYA 242
Cdd:PRK08017  75 -LYGLFNNAGF-GVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPaMLPHGEGRIVMTSSVMGLISTPGrGAYAASKYA 152

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 576796343 243 VEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPV 277
Cdd:PRK08017 153 LEAWSDALRMELRHSGIKVSLIEPGPIRTRFTDNV 187
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 86-292 5.99e-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: 131.45  E-value: 5.99e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVG 162
Cdd:COG1028    3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAaggRALAVAADVTDEAAVEALVAAAVAAFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 ekGLWGLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSK 240
Cdd:COG1028   83 --RLDILVNNAGITPP-GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGgGRIVNISSIAGLRGSPGqAAYAASK 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 576796343 241 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSP 292
Cdd:COG1028  160 AAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAARIP 211
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 87-276 1.47e-32

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: 122.69  E-value: 1.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  87 ITDKYIFITGCDSGFGNLAARTFDKKGFHVI-------------AACLTESGSTALkaetserlrTVLLDVTDPENVKRT 153
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVlsarreerleevkSECLELGAPSPH---------VVPLDMSDLEDAEQV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 154 AQWVKNQVGekGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIV 232
Cdd:cd05332   72 VEEALKLFG--GLDILINNAGI-SMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPhLIERSQGSIVVVSSIAGKIGVP 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 576796343 233 G-GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADP 276
Cdd:cd05332  149 FrTAYAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMN 193
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 90-271 3.95e-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: 3.95e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAAC-----LTESGSTaLKAETSERLRTVLLDVTDPENVKrtAQWVKNQVGEK 164
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLILTGrraerLQELADE-LGAKFPVKVLPLQLDVSDRESIE--AALENLPEEFR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 GLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYA 242
Cdd:cd05346   78 DIDILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPiMIARNQGHIINLGSIAGRYPYAGGNvYCATKAA 157

                        170       180
                 ....*....|....*....|....*....
gi 576796343 243 VEGFNDSLRRDMKAFGVHVSCIEPGLFKT 271
Cdd:cd05346  158 VRQFSLNLRKDLIGTGIRVTNIEPGLVET 186
PRK09291 PRK09291
SDR family oxidoreductase;
88-275 3.09e-30

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 116.25  E-value: 3.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  88 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSER---LRTVLLDVTDPENVKRTAQW---Vknqv 161
Cdd:PRK09291   1 MSKTILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRglaLRVEKLDLTDAIDRAQAAEWdvdV---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 162 gekglwgLINNAGV--PGVLAPtdwLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG-YT 237
Cdd:PRK09291  77 -------LLNNAGIgeAGAVVD---IPVELVRELFETNVFGPLELTQGFVRkMVARGKGKVVFTSSMAGLITGPFTGaYC 146

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 576796343 238 PSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 275
Cdd:PRK09291 147 ASKHALEAIAEAMHAELKPFGIQVATVNPGPYLTGFND 184
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 94-369 4.00e-30

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 116.54  E-value: 4.00e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKGFHVIAaclteSGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwgLINNA 173
Cdd:PRK06179   9 VTGASSGIGRATAEKLARAGYRVFG-----TSRNPARAAPIPGVELLELDVTDDASVQAAVDEVIARAGRIDV--LVNNA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 174 GVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKA-QGRVINVSSVGGRL-AIVGGGYTPSKYAVEGFNDSLR 251
Cdd:PRK06179  82 GV-GLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQgSGRIINISSVLGFLpAPYMALYAASKHAVEGYSESLD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 252 RDMKAFGVHVSCIEPGLFKTNLadpvkviekklaiwEQLSPDIKQQYGEGYIEKSLDKLKGNKSYVNMDLSPVV-ECMDH 330
Cdd:PRK06179 161 HEVRQFGIRVSLVEPAYTKTNF--------------DANAPEPDSPLAEYDRERAVVSKAVAKAVKKADAPEVVaDTVVK 226

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 576796343 331 ALTSLFPKTHYAAGKDAKIFWIPLSHMPAALQDFLLLKQ 369
Cdd:PRK06179 227 AALGPWPKMRYTAGGQASLLSKLRRFMPAGAVDKSLRKT 265
PRK05693 PRK05693
SDR family oxidoreductase;
92-274 3.93e-29

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 113.73  E-value: 3.93e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  92 IFITGCDSGFGNLAARTFDKKGFHVIAacltesgsTALKAETSERL-----RTVLLDVTDPENVKRTAQWVKNQVGekGL 166
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWA--------TARKAEDVEALaaagfTAVQLDVNDGAALARLAEELEAEHG--GL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 167 WGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAI-VGGGYTPSKYAVEG 245
Cdd:PRK05693  74 DVLINNAGY-GAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTpFAGAYCASKAAVHA 152

                        170       180
                 ....*....|....*....|....*....
gi 576796343 246 FNDSLRRDMKAFGVHVSCIEPGLFKTNLA 274
Cdd:PRK05693 153 LSDALRLELAPFGVQVMEVQPGAIASQFA 181
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 88-301 6.20e-29

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 113.21  E-value: 6.20e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  88 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEkgLW 167
Cdd:PRK08263   2 MEKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGR--LD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 168 GLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVGGG-YTPSKYAVEG 245
Cdd:PRK08263  80 IVVNNAGY-GLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRsGHIIQISSIGGISAFPMSGiYHASKWALEG 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 576796343 246 FNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSPDIKQQYGEG 301
Cdd:PRK08263 159 MSEALAQEVAEFGIKVTLVEPGGYSTDWAGTSAKRATPLDAYDTLREELAEQWSER 214
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 87-297 9.10e-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: 9.10e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  87 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE-TSE--RLRTVLLDVTDPENVKRTAQWVKNQVGe 163
Cdd:cd08934    1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADElEAEggKALVLELDVTDEQQVDAAVERTVEALG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 164 kGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVK-KAQGRVINVSSVGGRLAIVG-GGYTPSKY 241
Cdd:cd08934   80 -RLDILVNNAGI-MLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLlRNKGTIVNISSVAGRVAVRNsAVYNATKF 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 576796343 242 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSPDIKQQ 297
Cdd:cd08934  158 GVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHITHTITKEAYEERISTIRKLQ 213
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 98-292 1.42e-28

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: 1.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343   98 DSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVL-LDVTDPENVKRTAQWVKNQVGekGLWGLINNAGV- 175
Cdd:pfam13561   5 ESGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAEELGAAVLpCDVTDEEQVEALVAAAVEKFG--RLDILVNNAGFa 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  176 PGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKaQGRVINVSSVGGRLAIVGGG-YTPSKYAVEGFNDSLRRDM 254
Cdd:pfam13561  83 PKLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKE-GGSIVNLSSIGAERVVPNYNaYGAAKAALEALTRYLAVEL 161

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 576796343  255 KAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSP 292
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 ...
 90-274 1.44e-28

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: 111.18  E-value: 1.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFH--VIAACLTESGSTALKAETSERL--RTVLLDVTDPENVKRTAQWVKNQVGekG 165
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPGtvILTARDVERGQAAVEKLRAEGLsvRFHQLDVTDDASIEAAADFVEEKYG--G 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIvggGYTPSKYAVE 244
Cdd:cd05324   79 LDILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPaGRIVNVSSGLGSLTS---AYGVSKAALN 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 576796343 245 GFNDSLRRDMKAFGVHVSCIEPGLFKTNLA 274
Cdd:cd05324  156 ALTRILAKELKETGIKVNACCPGWVKTDMG 185
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 87-274 7.07e-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: 7.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  87 ITDKYIFITGCDSGFGNLAARTFDKKGF-HVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNqvgekg 165
Cdd:cd05354    1 IKDKTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAAQAKD------ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKA-QGRVINVSSVGGRLAIVG-GGYTPSKYAV 243
Cdd:cd05354   75 VDVVINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANgGGAIVNLNSVASLKNFPAmGTYSASKSAA 154

                        170       180       190
                 ....*....|....*....|....*....|.
gi 576796343 244 EGFNDSLRRDMKAFGVHVSCIEPGLFKTNLA 274
Cdd:cd05354  155 YSLTQGLRAELAAQGTLVLSVHPGPIDTRMA 185
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 86-285 1.88e-27

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 108.74  E-value: 1.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTES-GSTALKAETSERLRTVLL---DVTDPENVKRTAQWVKNQV 161
Cdd:PRK05557   2 SLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEaGAEALVAEIGALGGKALAvqgDVSDAESVERAVDEAKAEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 162 GekGLWGLINNAGVpgvlapTDW-----LTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG 235
Cdd:PRK05557  82 G--GVDILVNNAGI------TRDnllmrMKEEDWDRVIDTNLTGVFNLTKAVARpMMKQRSGRIINISSVVGLMGNPGQA 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 576796343 236 -YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT--NLADPVKVIEKKLA 285
Cdd:PRK05557 154 nYAASKAGVIGFTKSLARELASRGITVNAVAPGFIETdmTDALPEDVKEAILA 206
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
88-272 6.27e-26

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 104.47  E-value: 6.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  88 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGek 164
Cdd:PRK05653   4 QGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAaggEARVLVFDVSDEAAVRALIEAAVEAFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 GLWGLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGlisvTLNML-----PLVKKAQGRVINVSSVGGRLAIVGGG-YTP 238
Cdd:PRK05653  82 ALDILVNNAGITRD-ALLPRMSEEDWDRVIDVNLTG----TFNVVraalpPMIKARYGRIVNISSVSGVTGNPGQTnYSA 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 576796343 239 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTN 272
Cdd:PRK05653 157 AKAGVIGFTKALALELASRGITVNAVAPGFIDTD 190
PRK07326 PRK07326
SDR family oxidoreductase;
85-275 1.14e-25

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 103.55  E-value: 1.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  85 EDITDKYIFITGCDSGFGNLAARTFDKKGFHV-IAACLTESGSTALKA-ETSERLRTVLLDVTDPENVKRTAQWVKNQVG 162
Cdd:PRK07326   2 MSLKGKVALITGGSKGIGFAIAEALLAEGYKVaITARDQKELEEAAAElNNKGNVLGLAADVRDEADVQRAVDAIVAAFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 ekGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGG-GYTPSKY 241
Cdd:PRK07326  82 --GLDVLIANAGV-GHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGTNFFAGGaAYNASKF 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 576796343 242 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 275
Cdd:PRK07326 159 GLVGFSEAAMLDLRQYGIKVSTIMPGSVATHFNG 192
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 89-281 1.46e-25

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: 1.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE-------TSERLRTVLLDVTDPENVKRtaqwVKNQV 161
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEieaeanaSGQKVSYISADLSDYEEVEQ----AFAQA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 162 GEKGLWG--LINNAG--VPGVLapTDwLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GG 235
Cdd:cd08939   77 VEKGGPPdlVVNCAGisIPGLF--ED-LTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRpGHIVFVSSQAALVGIYGySA 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 576796343 236 YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT------NLADP--VKVIE 281
Cdd:cd08939  154 YCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTpgfeeeNKTKPeeTKAIE 207
PRK05650 PRK05650
SDR family oxidoreductase;
92-275 1.92e-25

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 103.58  E-value: 1.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  92 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGekGLWG 168
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREaggDGFYQRCDVRDYSQLTALAQACEEKWG--GIDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAGVP--GVLAPtdwLTLEDYREPIEVNLFGLISVTLNMLPLVKKA-QGRVINVSSVGGRLAIVG-GGYTPSKYAVE 244
Cdd:PRK05650  81 IVNNAGVAsgGFFEE---LSLEDWDWQIAINLMGVVKGCKAFLPLFKRQkSGRIVNIASMAGLMQGPAmSSYNVAKAGVV 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 576796343 245 GFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 275
Cdd:PRK05650 158 ALSETLLVELADDEIGVHVVCPSFFQTNLLD 188
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 90-275 2.24e-25

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


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 102.59  E-value: 2.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGL 169
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFG--GLDAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 170 INNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLN-MLPLVKKAQGRVINVSSVGGRLAIVGG-GYTPSKYAVEGFN 247
Cdd:cd08929   79 VNNAGV-GVMKPVEELTPEEWRLVLDTNLTGAFYCIHKaAPALLRRGGGTIVNVGSLAGKNAFKGGaAYNASKFGLLGLS 157

                        170       180
                 ....*....|....*....|....*...
gi 576796343 248 DSLRRDMKAFGVHVSCIEPGLFKTNLAD 275
Cdd:cd08929  158 EAAMLDLREANIRVVNVMPGSVDTGFAG 185
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 92-277 2.31e-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: 102.76  E-value: 2.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  92 IFITGCDSGFGNLAARTF-DKKGFHVIAACLTESGSTALKAETSERLRTVL--LDVTDPenVKRTAQWVKNQVGEKGLWG 168
Cdd:cd05325    1 VLITGASRGIGLELVRQLlARGNNTVIATCRDPSAATELAALGASHSRLHIleLDVTDE--IAESAEAVAERLGDAGLDV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKA-QGRVINVSSVGGRLA-IVGGG---YTPSKYAV 243
Cdd:cd05325   79 LINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGaRAKIINISSRVGSIGdNTSGGwysYRASKAAL 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 576796343 244 EGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPV 277
Cdd:cd05325  159 NMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPF 192
PRK12826 PRK12826
SDR family oxidoreductase;
86-277 2.84e-25

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 102.69  E-value: 2.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALkAETSE----RLRTVLLDVTDPENVKRTAQWVKNQV 161
Cdd:PRK12826   3 DLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAAT-AELVEaaggKARARQVDVRDRAALKAAVAAGVEDF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 162 GekGLWGLINNAGVPGvLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGR-LAIVGG-GYTP 238
Cdd:PRK12826  82 G--RLDILVANAGIFP-LTPFAEMDDEQWERVIDVNLTGTFLLTQAALPaLIRAGGGRIVLTSSVAGPrVGYPGLaHYAA 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 576796343 239 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPV 277
Cdd:PRK12826 159 SKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNL 197
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 92-279 3.81e-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: 102.32  E-value: 3.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  92 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALK---AETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwg 168
Cdd:cd05339    2 VLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETAnnvRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTI-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAGVPGVLAPTDwLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYAVEGF 246
Cdd:cd05339   80 LINNAGVVSGKKLLE-LPDEEIEKTFEVNTLAHFWTTKAFLPdMLERNHGHIVTIASVAGLISPAGLAdYCASKAAAVGF 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 576796343 247 NDSLRRDMKAF---GVHVSCIEPGLFKTNLADPVKV 279
Cdd:cd05339  159 HESLRLELKAYgkpGIKTTLVCPYFINTGMFQGVKT 194
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 90-267 5.23e-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: 5.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFG-NLAARTF--DKKGFHVIAACLTESGSTALKAETSER----LRTVLLDVTDPENVkrtAQWVkNQVG 162
Cdd:cd09806    1 TVVLITGCSSGIGlHLAVRLAsdPSKRFKVYATMRDLKKKGRLWEAAGALaggtLETLQLDVCDSKSV---AAAV-ERVT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 EKGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKK-AQGRVINVSSVGGRLAIVGGG-YTPSK 240
Cdd:cd09806   77 ERHVDVLVCNAGV-GLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRrGSGRILVTSSVGGLQGLPFNDvYCASK 155

                        170       180
                 ....*....|....*....|....*..
gi 576796343 241 YAVEGFNDSLRRDMKAFGVHVSCIEPG 267
Cdd:cd09806  156 FALEGLCESLAVQLLPFNVHLSLIECG 182
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 92-271 7.82e-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: 7.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  92 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGEKGLWg 168
Cdd:cd05360    3 VVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRElggEAIAVVADVADAAQVERAADTAVERFGRIDTW- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 lINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIV-GGGYTPSKYAVEGF 246
Cdd:cd05360   82 -VNNAGV-AVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGgGALINVGSLLGYRSAPlQAAYSASKHAVRGF 159

                        170       180
                 ....*....|....*....|....*..
gi 576796343 247 NDSLRRDMKAFG--VHVSCIEPGLFKT 271
Cdd:cd05360  160 TESLRAELAHDGapISVTLVQPTAMNT 186
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 86-274 1.98e-24

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 101.17  E-value: 1.98e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTEsgstALKAETSERLRTVL---LDVTDPENVKRTAQWVKNQVG 162
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDE----ALAKETAAELGLVVggpLDVTDPASFAAFLDAVEADLG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 EKGLwgLINNAGV-P--GVLAPTDWLTledyREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG-YT 237
Cdd:PRK07825  78 PIDV--LVNNAGVmPvgPFLDEPDAVT----RRILDVNVYGVILGSKLAAPrMVPRGRGHVVNVASLAGKIPVPGMAtYC 151

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 576796343 238 PSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLA 274
Cdd:PRK07825 152 ASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELI 188
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
94-300 1.99e-24

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 100.23  E-value: 1.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGST----ALKAETSERLRTVLLDVTDPENVKRTaqwVKNQVGEKGLWG- 168
Cdd:PRK12824   7 VTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAkdwfEEYGFTEDQVRLKELDVTDTEECAEA---LAEIEEEEGPVDi 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAGVP--GVLAPtdwLTLEDYREPIEVNLFGLISVTLNMLPLVK-KAQGRVINVSSVGGRLAIVGG-GYTPSKYAVE 244
Cdd:PRK12824  84 LVNNAGITrdSVFKR---MSHQEWNDVINTNLNSVFNVTQPLFAAMCeQGYGRIINISSVNGLKGQFGQtNYSAAKAGMI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 576796343 245 GFNDSLRRDMKAFGVHVSCIEPGLFKTNLAdpvkviekklaiwEQLSPDIKQQYGE 300
Cdd:PRK12824 161 GFTKALASEGARYGITVNCIAPGYIATPMV-------------EQMGPEVLQSIVN 203
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 90-278 2.12e-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: 99.83  E-value: 2.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAET-SERLRTVLLDVTDPENVKRT-AQWVKNQVGekGLW 167
Cdd:cd08931    1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELgAENVVAGALDVTDRAAWAAAlADFAAATGG--RLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 168 GLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQG-RVINVSSVGG-----RLAIvgggYTPSKY 241
Cdd:cd08931   79 ALFNNAGV-GRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGaRVINTASSSAiygqpDLAV----YSATKF 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 576796343 242 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVK 278
Cdd:cd08931  154 AVRGLTEALDVEWARHGIRVADVWPWFVDTPILTKGE 190
PRK06482 PRK06482
SDR family oxidoreductase;
93-274 2.54e-24

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 100.96  E-value: 2.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  93 FITGCDSGFGNLAARTFDKKGfHVIAACLTESGSTA-LKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwgLIN 171
Cdd:PRK06482   6 FITGASSGFGRGMTERLLARG-DRVAATVRRPDALDdLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAALGRIDV--VVS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 172 NAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYAVEGFNDS 249
Cdd:PRK06482  83 NAGY-GLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPhLRRQGGGRIVQVSSEGGQIAYPGFSlYHATKWGIEGFVEA 161

                        170       180
                 ....*....|....*....|....*
gi 576796343 250 LRRDMKAFGVHVSCIEPGLFKTNLA 274
Cdd:PRK06482 162 VAQEVAPFGIEFTIVEPGPARTNFG 186
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 85-287 4.55e-23

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 96.19  E-value: 4.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  85 EDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTEsgstalKAETSERLRTVLLDVTDPenVKRTAQWVKnQVGEk 164
Cdd:PRK06550   1 QEFMTKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQD------KPDLSGNFHFLQLDLSDD--LEPLFDWVP-SVDI- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 glwgLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAivGGG---YTPSK 240
Cdd:PRK06550  71 ----LCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPqMLERKSGIIINMCSIASFVA--GGGgaaYTASK 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 576796343 241 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT--NLADpvkVIEKKLAIW 287
Cdd:PRK06550 145 HALAGFTKQLALDYAKDGIQVFGIAPGAVKTpmTAAD---FEPGGLADW 190
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 86-336 5.41e-23

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 96.67  E-value: 5.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKG--FHVIAACLTESGSTALKAETSERLRTVLlDVTDPENVKRTAQWVKNQVGe 163
Cdd:PRK12829   8 PLDGLRVLVTGGASGIGRAIAEAFAEAGarVHVCDVSEAALAATAARLPGAKVTATVA-DVADPAQVERVFDTAVERFG- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 164 kGLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVK--KAQGRVINVSSVGGRLAIVGG-GYTPSK 240
Cdd:PRK12829  86 -GLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKasGHGGVIIALSSVAGRLGYPGRtPYAASK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 241 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVkviekklaiweqlSPDIKQQYGEGYIEKSLDKLKGnksyvnMD 320
Cdd:PRK12829 165 WAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRV-------------IEARAQQLGIGLDEMEQEYLEK------IS 225

                        250
                 ....*....|....*.
gi 576796343 321 LSPVVECMDHALTSLF 336
Cdd:PRK12829 226 LGRMVEPEDIAATALF 241
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 92-278 7.85e-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: 95.86  E-value: 7.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  92 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGekGLWG 168
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNpnpSVEVEILDVTDEERNQLVIAELEAELG--GLDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGG-GYTPSKYAVEGF 246
Cdd:cd05350   79 VIINAGV-GKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPqFRAKGRGHLVLISSVAALRGLPGAaAYSASKAALSSL 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 576796343 247 NDSLRRDMKAFGVHVSCIEPGLFKTNLADPVK 278
Cdd:cd05350  158 AESLRYDVKKRGIRVTVINPGFIDTPLTANMF 189
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 85-274 9.16e-23

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 95.53  E-value: 9.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  85 EDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQV 161
Cdd:PRK07666   3 QSLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAygvKVVIATADVSDYEEVTAAIEQLKNEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 162 GEKGLwgLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGG-RLAIVGGGYTPS 239
Cdd:PRK07666  83 GSIDI--LINNAGI-SKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPsMIERQSGDIINISSTAGqKGAAVTSAYSAS 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 576796343 240 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLA 274
Cdd:PRK07666 160 KFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMA 194
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 86-273 9.51e-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: 9.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGnLA-ARTFDKKGFHVIAACLTESGSTALKAETsERLRTVLLDVTDPENVKRTAQWVKNQVGEk 164
Cdd:COG3967    2 KLTGNTILITGGTSGIG-LAlAKRLHARGNTVIITGRREEKLEEAAAAN-PGLHTIVLDVADPASIAALAEQVTAEFPD- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 gLWGLINNAgvpGVLAPTDWL----TLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVggrLAIVGGGYTP- 238
Cdd:COG3967   79 -LNVLINNA---GIMRAEDLLdeaeDLADAEREITTNLLGPIRLTAAFLPhLKAQPEAAIVNVSSG---LAFVPLAVTPt 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 576796343 239 ---SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:COG3967  152 ysaTKAALHSYTQSLRHQLKDTSVKVIELAPPAVDTDL 189
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 92-268 1.18e-22

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 95.59  E-value: 1.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  92 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRT-----AQWVKNQVgekgl 166
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMlaslpAEWRNIDV----- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 167 wgLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYAVE 244
Cdd:PRK10538  78 --LVNNAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPgMVERNHGHIINIGSTAGSWPYAGGNvYGATKAFVR 155

                        170       180
                 ....*....|....*....|....
gi 576796343 245 GFNDSLRRDMKAFGVHVSCIEPGL 268
Cdd:PRK10538 156 QFSLNLRTDLHGTAVRVTDIEPGL 179
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 90-285 1.82e-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: 94.92  E-value: 1.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE---TSERLRTVLLDVTDPENVKRTAQWVKNQVGekGL 166
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEikaLGGNAAALEADVSDREAVEALVEKVEAEFG--PV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 167 WGLINNAGVpgvlapT-DWL----TLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPS 239
Cdd:cd05333   79 DILVNNAGI------TrDNLlmrmSEEDWDAVINVNLTGVFNVTQAVIRaMIKRRSGRIINISSVVGLIGNPGqANYAAS 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 576796343 240 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD--PVKVIEKKLA 285
Cdd:cd05333  153 KAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDalPEKVKEKILK 200
PRK06181 PRK06181
SDR family oxidoreductase;
89-273 2.27e-22

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 95.05  E-value: 2.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVL---LDVTDPENVKRTAQWVKNQVGekG 165
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALvvpTDVSDAEACERLIEAAVARFG--G 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LWGLINNAGVpGVLAPTDWLT-LEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVG-GGYTPSKYAV 243
Cdd:PRK06181  79 IDILVNNAGI-TMWSRFDELTdLSVFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTrSGYAASKHAL 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 576796343 244 EGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:PRK06181 158 HGFFDSLRIELADDGVAVTVVCPGFVATDI 187
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 89-273 2.40e-22

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: 94.98  E-value: 2.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE-----TSERLRTVLLDVTDPENVKRTAQWVKNQVGE 163
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEikketGNAKVEVIQLDLSSLASVRQFAEEFLARFPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 164 kgLWGLINNAgvpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKK-AQGRVINVSSVGGRLAIVGG-----GYT 237
Cdd:cd05327   81 --LDILINNA---GIMAPPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKAsAPSRIVNVSSIAHRAGPIDFndldlENN 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 576796343 238 PSKYAVEGFNDS----------LRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:cd05327  156 KEYSPYKAYGQSklanilftreLARRLEGTGVTVNALHPGVVRTEL 201
PRK08267 PRK08267
SDR family oxidoreductase;
90-361 2.44e-22

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 95.00  E-value: 2.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE-TSERLRTVLLDVTDPenvkrtAQWvKNQVGEKGLWG 168
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAElGAGNAWTGALDVTDR------AAW-DAALADFAAAT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 ------LINNAGVP--GVLAPTDwltLEDYREPIEVNLFGLISVTLNMLPLVKKAQG-RVINVSSVGG-----RLAIvgg 234
Cdd:PRK08267  75 ggrldvLFNNAGILrgGPFEDIP---LEAHDRVIDINVKGVLNGAHAALPYLKATPGaRVINTSSASAiygqpGLAV--- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 235 gYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADpvkviekklaiweqlspdikqQYGEGYIEKSLDKLkgnk 314
Cdd:PRK08267 149 -YSATKFAVRGLTEALDLEWRRHGIRVADVMPLFVDTAMLD---------------------GTSNEVDAGSTKRL---- 202

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 576796343 315 syvNMDLSP------VVECMDHAltslfPKTHYAAGKDAKIFWIPLSHMPAAL 361
Cdd:PRK08267 203 ---GVRLTPedvaeaVWAAVQHP-----TRLHWPVGKQAKLLAFLARLSPGFV 247
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 87-271 5.78e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 95.37  E-value: 5.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  87 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGE 163
Cdd:PRK07109   6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAaggEALAVVADVADAEAVQAAADRAEEELGP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 164 KGLWglINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAI-VGGGYTPSKY 241
Cdd:PRK07109  86 IDTW--VNNAMV-TVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRhMRPRDRGAIIQVGSALAYRSIpLQSAYCAAKH 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 576796343 242 AVEGFNDSLRRDMKAFG--VHVSCIEPGLFKT 271
Cdd:PRK07109 163 AIRGFTDSLRCELLHDGspVSVTMVQPPAVNT 194
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 86-277 1.07e-21

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: 92.81  E-value: 1.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLT-ESGSTALKAETSE--RLRTVLLDVTDPENVKRTAQWVKNQVG 162
Cdd:cd05347    2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNeEKAEEAQQLIEKEgvEATAFTCDVSDEEAIKAAVEAIEEDFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 EKGLwgLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVggrLAIVGG----GYT 237
Cdd:cd05347   82 KIDI--LVNNAGI-IRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARhMIKQGHGKIINICSL---LSELGGppvpAYA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 576796343 238 PSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPV 277
Cdd:cd05347  156 ASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTEAV 195
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 86-275 2.64e-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: 91.68  E-value: 2.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekG 165
Cdd:cd05341    2 RLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFG--R 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKA-QGRVINVSSVGGRLAIVG-GGYTPSKYAV 243
Cdd:cd05341   80 LDVLVNNAGI-LTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAgGGSIINMSSIEGLVGDPAlAAYNASKGAV 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 576796343 244 EGFNDSLRRDM--KAFGVHVSCIEPGLFKTNLAD 275
Cdd:cd05341  159 RGLTKSAALECatQGYGIRVNSVHPGYIYTPMTD 192
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 90-281 2.64e-21

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 91.96  E-value: 2.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAAclteSGSTALKAETSERLR-------TVLLDVTDPENVKRTAQWVKNQVG 162
Cdd:PRK12939   8 KRALVTGAARGLGAAFAEALAEAGATVAFN----DGLAAEARELAAALEaaggrahAIAADLADPASVQRFFDAAAAALG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 ekGLWGLINNAGVPgVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSS-VGGRLAIVGGGYTPSK 240
Cdd:PRK12939  84 --GLDGLVNNAGIT-NSKSATELDIDTWDAVMNVNVRGTFLMLRAALPhLRDSGRGRIVNLASdTALWGAPKLGAYVASK 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 576796343 241 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIE 281
Cdd:PRK12939 161 GAVIGMTRSLARELGGRGITVNAIAPGLTATEATAYVPADE 201
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 90-268 1.03e-20

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 90.31  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACL-TESGSTALKAE---TSERLRTVLLDVTDPENVKRTAQWVKNQVGekG 165
Cdd:PRK12825   7 RVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEAveaLGRRAQAVQADVTDKAALEAAVAAAVERFG--R 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LWGLINNAGVpgvlapTDW-----LTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTP 238
Cdd:PRK12825  85 IDILVNNAGI------FEDkpladMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRgGRIVNISSVAGLPGWPGrSNYAA 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 576796343 239 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGL 268
Cdd:PRK12825 159 AKAGLVGLTKALARELAEYGITVNMVAPGD 188
PRK08264 PRK08264
SDR family oxidoreductase;
86-275 2.18e-20

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 88.79  E-value: 2.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTAlkaETSERLRTVLLDVTDPENVKRTAQwvknQVGEKG 165
Cdd:PRK08264   3 DIKGKVVLVTGANRGIGRAFVEQLLARGAAKVYAAARDPESVT---DLGPRVVPLQLDVTDPASVAAAAE----AASDVT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LwgLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAI-VGGGYTPSKYAV 243
Cdd:PRK08264  76 I--LVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPvLAANGGGAIVNVLSVLSWVNFpNLGTYSASKAAA 153

                        170       180       190
                 ....*....|....*....|....*....|..
gi 576796343 244 EGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 275
Cdd:PRK08264 154 WSLTQALRAELAPQGTRVLGVHPGPIDTDMAA 185
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 86-273 1.36e-19

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: 86.59  E-value: 1.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSErLRTVLLDVTDPENVKRTAQWVKNQVGEkg 165
Cdd:cd05370    2 KLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN-IHTIVLDVGDAESVEALAEALLSEYPN-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LWGLINNAGVP---GVLAPTDwlTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVggrLAIV----GGGYT 237
Cdd:cd05370   79 LDILINNAGIQrpiDLRDPAS--DLDKADTEIDTNLIGPIRLIKAFLPhLKKQPEATIVNVSSG---LAFVpmaaNPVYC 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 576796343 238 PSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:cd05370  154 ATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTEL 189
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 88-303 3.10e-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: 3.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  88 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE-----RLRTVLLDVTDPENVKRTAQWVKNQVG 162
Cdd:cd05330    2 KDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEiapdaEVLLIKADVSDEAQVEAYVDATVEQFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 EkgLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSK 240
Cdd:cd05330   82 R--IDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGsGMIVNTASVGGIRGVGNqSGYAAAK 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 576796343 241 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLadpvkvIEKKLaiwEQLSPDIKQQYGEGYI 303
Cdd:cd05330  160 HGVVGLTRNSAVEYGQYGIRINAIAPGAILTPM------VEGSL---KQLGPENPEEAGEEFV 213
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 85-283 1.47e-18

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 84.12  E-value: 1.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  85 EDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAAC-LTESGSTALKAETSERLRTVLL---DVTDPENVKRTAQWVKNQ 160
Cdd:PRK05565   1 MKLMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYdINEEAAQELLEEIKEEGGDAIAvkaDVSSEEDVENLVEQIVEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 161 VGekGLWGLINNAGVPGVLAPTDwLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRL-AIVGGGYTP 238
Cdd:PRK05565  81 FG--KIDILVNNAGISNFGLVTD-MTDEEWDRVIDVNLTGVMLLTRYALPyMIKRKSGVIVNISSIWGLIgASCEVLYSA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 576796343 239 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKK 283
Cdd:PRK05565 158 SKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKE 202
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 89-273 2.07e-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: 2.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVI-----AACLTESGSTALKAETSE-RLRTVLLDVTDPENVKRTAQWVKNQVG 162
Cdd:cd05364    3 GKVAIITGSSSGIGAGTAILFARLGARLAltgrdAERLEETRQSCLQAGVSEkKILLVVADLTEEEGQDRIISTTLAKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 EkgLWGLINNAGVPGVLAPTDwLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGG-GYTPSKY 241
Cdd:cd05364   83 R--LDILVNNAGILAKGGGED-QDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGRSFPGVlYYCISKA 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 576796343 242 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:cd05364  160 ALDQFTRCTALELAPKGVRVNSVSPGVIVTGF 191
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 94-273 2.44e-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: 83.50  E-value: 2.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKGFHVIAACLTES--GSTALKA-ETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGLI 170
Cdd:cd05323    5 ITGGASGIGLATAKLLLKKGAKVAILDRNENpgAAAELQAiNPKVKATFVQCDVTSWEQLAAAFKKAIEKFG--RVDILI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 171 NNAgvpGVLAPTDWLTLEDYREPIE----VNLFGLISVTLNMLPLVKKAQ----GRVINVSSVGG----RLAIVgggYTP 238
Cdd:cd05323   83 NNA---GILDEKSYLFAGKLPPPWEktidVNLTGVINTTYLALHYMDKNKggkgGVIVNIGSVAGlypaPQFPV---YSA 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 576796343 239 SKYAVEGFNDSLRRDMKA-FGVHVSCIEPGLFKTNL 273
Cdd:cd05323  157 SKHGVVGFTRSLADLLEYkTGVRVNAICPGFTNTPL 192
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
80-275 2.67e-18

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 83.70  E-value: 2.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  80 GKLkiediTDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLR--TVLLDVTDPENVKRTAQWV 157
Cdd:PRK08226   2 GKL-----TGKTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADELCGRGHRctAVVADVRDPASVAAAIKRA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 158 KNQVGEKGLwgLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGG-- 234
Cdd:PRK08226  77 KEKEGRIDI--LVNNAGV-CRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPeMIARKDGRIVMMSSVTGDMVADPGet 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 576796343 235 GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 275
Cdd:PRK08226 154 AYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAE 194
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 89-291 3.30e-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: 3.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSER----LRTVLLDVTDPENVKRTAQWVKNQVGEk 164
Cdd:cd08933    9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAgpgsCKFVPCDVTKEEDIKTLISVTVERFGR- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 gLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVggrLAIVG----GGYTPSK 240
Cdd:cd08933   88 -IDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSL---VGSIGqkqaAPYVATK 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 576796343 241 YAVEGFNDSLRRDMKAFGVHVSCIEPGlfktNLADPvkviekklaIWEQLS 291
Cdd:cd08933  164 GAITAMTKALAVDESRYGVRVNCISPG----NIWTP---------LWEELA 201
PRK07832 PRK07832
SDR family oxidoreductase;
90-279 7.68e-18

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 82.40  E-value: 7.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIaacLTESGSTALkAETSERLR----TVL----LDVTDPENVKRTAQWVKNQV 161
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELF---LTDRDADGL-AQTVADARalggTVPehraLDISDYDAVAAFAADIHAAH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 162 GEKGLwgLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGR-VINVSSVGGRLAIV-GGGYTP 238
Cdd:PRK07832  77 GSMDV--VMNIAGI-SAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPpMVAAGRGGhLVNVSSAAGLVALPwHAAYSA 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 576796343 239 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKV 279
Cdd:PRK07832 154 SKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVNTVEI 194
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 93-288 8.91e-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: 8.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  93 FITGCDSGFGNLAARTFDKKGFHV-IAACLTESGSTALKAETSERLRT--VLLDVTDPENVKRTAQWVKNQVGEKGLwgL 169
Cdd:cd08945    7 LVTGATSGIGLAIARRLGKEGLRVfVCARGEEGLATTVKELREAGVEAdgRTCDVRSVPEIEALVAAAVARYGPIDV--L 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 170 INNAGVPGVLAPTDwLTLEDYREPIEVNLFGLISVTLNMLP---LVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYAVEG 245
Cdd:cd08945   85 VNNAGRSGGGATAE-LADELWLDVVETNLTGVFRVTKEVLKaggMLERGTGRIINIASTGGKQGVVHAApYSASKHGVVG 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 576796343 246 FNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKviEKKLAIWE 288
Cdd:cd08945  164 FTKALGLELARTGITVNAVCPGFVETPMAASVR--EHYADIWE 204
PRK09072 PRK09072
SDR family oxidoreductase;
86-261 9.15e-18

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 82.30  E-value: 9.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETS--ERLRTVLLDVTDPENVKRTAQwVKNQVGe 163
Cdd:PRK09072   2 DLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPypGRHRWVVADLTSEAGREAVLA-RAREMG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 164 kGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSKY 241
Cdd:PRK09072  80 -GINVLINNAGV-NHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPsAMVVNVGSTFGSIGYPGyASYCASKF 157

                        170       180
                 ....*....|....*....|
gi 576796343 242 AVEGFNDSLRRDMKAFGVHV 261
Cdd:PRK09072 158 ALRGFSEALRRELADTGVRV 177
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 88-281 1.42e-17

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: 1.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  88 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTES-GSTALKAEtsERLRTVLLDVTDPENVKRTAQWVKNQVGEkgL 166
Cdd:cd05371    1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSpGETVAKLG--DNCRFVPVDVTSEKDVKAALALAKAKFGR--L 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 167 WGLINNAGVpGVLAPTDWL------TLEDYREPIEVNLFGlisvTLNMLPLVKKAQGR-----------VINVSSVGGRL 229
Cdd:cd05371   77 DIVVNCAGI-AVAAKTYNKkgqqphSLELFQRVINVNLIG----TFNVIRLAAGAMGKnepdqggergvIINTASVAAFE 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 576796343 230 AIVG-GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL--ADPVKVIE 281
Cdd:cd05371  152 GQIGqAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLlaGLPEKVRD 206
PRK07454 PRK07454
SDR family oxidoreductase;
93-275 1.62e-17

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 81.16  E-value: 1.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  93 FITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwgL 169
Cdd:PRK07454  10 LITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRStgvKAAAYSIDLSNPEAIAPGIAELLEQFGCPDV--L 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 170 INNAGVP--GVLAPTDwltLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSKYAVEG 245
Cdd:PRK07454  88 INNAGMAytGPLLEMP---LSDWQWVIQLNLTSVFQCCSAVLPGMRARGgGLIINVSSIAARNAFPQwGAYCVSKAALAA 164

                        170       180       190
                 ....*....|....*....|....*....|
gi 576796343 246 FNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 275
Cdd:PRK07454 165 FTKCLAEEERSHGIRVCTITLGAVNTPLWD 194
PRK08589 PRK08589
SDR family oxidoreductase;
87-275 1.83e-17

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 81.36  E-value: 1.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  87 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKA--ETSERLRTVLLDVTDPENVKRTAQWVKNQVGEK 164
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDKikSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 GLwgLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLA-IVGGGYTPSKYAV 243
Cdd:PRK08589  84 DV--LFNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAAdLYRSGYNAAKGAV 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 576796343 244 EGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 275
Cdd:PRK08589 162 INFTKSIAIEYGRDGIRANAIAPGTIETPLVD 193
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
87-285 2.10e-17

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 80.83  E-value: 2.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  87 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLL----DVTDPENVKRTAQWVKNQVG 162
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRRVKWLEDQKALGFDFIasegNVGDWDSTKAAFDKVKAEVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 EKGLwgLINNAGVPGVLAPTDwLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPSK 240
Cdd:PRK12938  81 EIDV--LVNNAGITRDVVFRK-MTREDWTAVIDTNLTSLFNVTKQVIDgMVERGWGRIINISSVNGQKGQFGqTNYSTAK 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 576796343 241 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVK--VIEKKLA 285
Cdd:PRK12938 158 AGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRpdVLEKIVA 204
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 90-274 2.54e-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: 2.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAEtSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGL 169
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS-GGDVEAVPYDARDPEDARALVDALRDRFG--RIDVL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 170 INNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPSKYAVEGFN 247
Cdd:cd08932   78 VHNAGI-GRPTTLREGSDAELEAHFSINVIAPAELTRALLPaLREAGSGRVVFLNSLSGKRVLAGnAGYSASKFALRALA 156

                        170       180
                 ....*....|....*....|....*..
gi 576796343 248 DSLRRDMKAFGVHVSCIEPGLFKTNLA 274
Cdd:cd08932  157 HALRQEGWDHGVRVSAVCPGFVDTPMA 183
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 86-273 3.52e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 80.47  E-value: 3.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKG 165
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRID 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LwgLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLI----SVTLNMLplvKKAQGRVINVSSVGGRLAIVGG-GYTPSK 240
Cdd:PRK06841  92 I--LVNSAGV-ALLAPAEDVSEEDWDKTIDINLKGSFlmaqAVGRHMI---AAGGGKIVNLASQAGVVALERHvAYCASK 165

                        170       180       190
                 ....*....|....*....|....*....|...
gi 576796343 241 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:PRK06841 166 AGVVGMTKVLALEWGPYGITVNAISPTVVLTEL 198
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 90-271 3.92e-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: 3.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTEsgsTALK-AETSERLRTVLLDVTDPENVKRTAQwvknqvGEKGLWG 168
Cdd:cd05368    3 KVALITAAAQGIGRAIALAFAREGANVIATDINE---EKLKeLERGPGITTRVLDVTDKEQVAALAK------EEGRIDV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAGV---PGVLAPTDwltlEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGG--GYTPSKYA 242
Cdd:cd05368   74 LFNCAGFvhhGSILDCED----DDWDFAMNLNVRSMYLMIKAVLPkMLARKDGSIINMSSVASSIKGVPNrfVYSTTKAA 149

                        170       180
                 ....*....|....*....|....*....
gi 576796343 243 VEGFNDSLRRDMKAFGVHVSCIEPGLFKT 271
Cdd:cd05368  150 VIGLTKSVAADFAQQGIRCNAICPGTVDT 178
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 90-271 3.14e-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: 3.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACL-TESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwg 168
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYrSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDT-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAGVPGVLAP-----TDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKA-QGRVINVSSVGGRLAIVG-GGYTPSKY 241
Cdd:cd05349   79 IVNNALIDFPFDPdqrktFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERgSGRVINIGTNLFQNPVVPyHDYTTAKA 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 576796343 242 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKT 271
Cdd:cd05349  159 ALLGFTRNMAKELGPYGITVNMVSGGLLKV 188
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 87-273 8.50e-16

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 76.32  E-value: 8.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  87 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIaacLTESGSTALKAETSE-------RLRTVLLDVTDPENVKRTAQWVKN 159
Cdd:PRK12937   3 LSNKVAIVTGASRGIGAAIARRLAADGFAVA---VNYAGSAAAADELVAeieaaggRAIAVQADVADAAAVTRLFDAAET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 160 QVGekGLWGLINNAGVPGvLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAqGRVINVSSVGGRLAIVGGG-YTP 238
Cdd:PRK12937  80 AFG--RIDVLVNNAGVMP-LGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQG-GRIINLSTSVIALPLPGYGpYAA 155

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 576796343 239 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:PRK12937 156 SKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL 190
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 89-273 8.54e-16

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 76.06  E-value: 8.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVIaacltesgstaLKAETSERLRTV------------------LLDVTdPENV 150
Cdd:PRK08945  12 DRIILVTGAGDGIGREAALTYARHGATVI-----------LLGRTEEKLEAVydeieaaggpqpaiipldLLTAT-PQNY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 151 KRTAQWVKNQVGEkgLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRL 229
Cdd:PRK08945  80 QQLADTIEEQFGR--LDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPaASLVFTSSSVGRQ 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 576796343 230 AIVG-GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:PRK08945 158 GRANwGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAM 202
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 80-273 1.03e-15

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 75.98  E-value: 1.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  80 GKLKieditDKYIFITGCDSGFGNLAARTFDKKGFHV-IAACLTESGSTALKAETSErlrTVLLDVTDPENVKRTAQWVK 158
Cdd:PRK06463   3 MRFK-----GKVALITGGTRGIGRAIAEAFLREGAKVaVLYNSAENEAKELREKGVF---TIKCDVGNRDQVKKSKEVVE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 159 NQVGEKGLwgLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGG-RLAIVGGG- 235
Cdd:PRK06463  75 KEFGRVDV--LVNNAGI-MYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKnGAIVNIASNAGiGTAAEGTTf 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 576796343 236 YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:PRK06463 152 YAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDM 189
PRK07774 PRK07774
SDR family oxidoreductase;
85-271 1.28e-15

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 75.94  E-value: 1.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  85 EDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVL---LDVTDPENVKRTAQWVKNQV 161
Cdd:PRK07774   2 GRFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIavqVDVSDPDSAKAMADATVSAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 162 GekGLWGLINNAGVPGVLAPTDWLT--LEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAivGGGYTP 238
Cdd:PRK07774  82 G--GIDYLVNNAAIYGGMKLDLLITvpWDYYKKFMSVNLDGALVCTRAVYKhMAKRGGGAIVNQSSTAAWLY--SNFYGL 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 576796343 239 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT 271
Cdd:PRK07774 158 AKVGLNGLTQQLARELGGMNIRVNAIAPGPIDT 190
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 89-274 2.47e-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: 2.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRT-VLLDVTDPENVKRTAQWVKNQVGEkgLW 167
Cdd:cd05326    4 GKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISfVHCDVTVEADVRAAVDTAVARFGR--LD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 168 GLINNAGVPGvlAPTDWL---TLEDYREPIEVNLFGLISVTLN----MLPlvkKAQGRVINVSSVGGrlaIVGGG----Y 236
Cdd:cd05326   82 IMFNNAGVLG--APCYSIletSLEEFERVLDVNVYGAFLGTKHaarvMIP---AKKGSIVSVASVAG---VVGGLgphaY 153

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 576796343 237 TPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLA 274
Cdd:cd05326  154 TASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLL 191
FabG-like PRK07231
SDR family oxidoreductase;
86-302 3.15e-15

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 74.48  E-value: 3.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE--TSERLRTVLLDVTDPENVKRTAQWVKNQVGe 163
Cdd:PRK07231   2 RLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEilAGGRAIAVAADVSDEADVEAAVAAALERFG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 164 kGLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKA-QGRVINVSSVGG-RLAIVGGGYTPSKY 241
Cdd:PRK07231  81 -SVDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEgGGAIVNVASTAGlRPRPGLGWYNASKG 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 576796343 242 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADpvkviekklAIWEQLSPDIKQQYGEGY 302
Cdd:PRK07231 160 AVITLTKALAAELGPDKIRVNAVAPVVVETGLLE---------AFMGEPTPENRAKFLATI 211
PRK09242 PRK09242
SDR family oxidoreductase;
89-285 3.37e-15

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 74.78  E-value: 3.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVI----AACLTESGSTALKAETSER-LRTVLLDVTDPENVKRTAQWVKNQVGe 163
Cdd:PRK09242   9 GQTALITGASKGIGLAIAREFLGLGADVLivarDADALAQARDELAEEFPEReVHGLAADVSDDEDRRAILDWVEDHWD- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 164 kGLWGLINNAGVPGVLAPTDWlTLEDYREPIEVNLFGLISVTLNMLPLVKK-AQGRVINVSSVGGrLAIVGGG--YTPSK 240
Cdd:PRK09242  88 -GLHILVNNAGGNIRKAAIDY-TEDEWRGIFETNLFSAFELSRYAHPLLKQhASSAIVNIGSVSG-LTHVRSGapYGMTK 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 576796343 241 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLA 285
Cdd:PRK09242 165 AALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDYYE 209
PRK08219 PRK08219
SDR family oxidoreductase;
94-267 3.41e-15

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 74.20  E-value: 3.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFdKKGFHVIAAClTESGSTALKAETSERLRTVLLDVTDPENVkrtaQWVKNQVGEkgLWGLINNA 173
Cdd:PRK08219   8 ITGASRGIGAAIAREL-APTHTLLLGG-RPAERLDELAAELPGATPFPVDLTDPEAI----AAAVEQLGR--LDVLVHNA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 174 GVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYAVEGFNDSLRR 252
Cdd:PRK08219  80 GV-ADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRANPGWGsYAASKFALRALADALRE 158

                        170
                 ....*....|....*
gi 576796343 253 DmKAFGVHVSCIEPG 267
Cdd:PRK08219 159 E-EPGNVRVTSVHPG 172
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 86-275 4.52e-15

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 74.18  E-value: 4.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekG 165
Cdd:PRK12936   3 DLSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEADLE--G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LWGLINNAGVPgvlapTDWLTL----EDYREPIEVNLFGLISVTLNML-PLVKKAQGRVINVSSVGGRLAIVG-GGYTPS 239
Cdd:PRK12936  81 VDILVNNAGIT-----KDGLFVrmsdEDWDSVLEVNLTATFRLTRELThPMMRRRYGRIINITSVVGVTGNPGqANYCAS 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 576796343 240 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 275
Cdd:PRK12936 156 KAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTG 191
PRK07201 PRK07201
SDR family oxidoreductase;
90-248 6.36e-15

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 76.14  E-value: 6.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTaqwVKNQVGEKGl 166
Cdd:PRK07201 372 KVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAkggTAHAYTCDLTDSAAVDHT---VKDILAEHG- 447

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 167 wG---LINNAGVP---GVLAPTDwlTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVG-----GRLAivgg 234
Cdd:PRK07201 448 -HvdyLVNNAGRSirrSVENSTD--RFHDYERTMAVNYFGAVRLILGLLPhMRERRFGHVVNVSSIGvqtnaPRFS---- 520

                        170
                 ....*....|....
gi 576796343 235 GYTPSKYAVEGFND 248
Cdd:PRK07201 521 AYVASKAALDAFSD 534
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 86-278 9.51e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 73.21  E-value: 9.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSErlRTVLLDVTDPEnvkrtaqWVKNQVGEKG 165
Cdd:PRK07060   6 DFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGC--EPLRLDVGDDA-------AIRAALAAAG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LW-GLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ--GRVINVSSVGGRLAIVGG-GYTPSKY 241
Cdd:PRK07060  77 AFdGLVNCAGI-ASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGrgGSIVNVSSQAALVGLPDHlAYCASKA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 576796343 242 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLA-----DPVK 278
Cdd:PRK07060 156 ALDAITRVLCVELGPHGIRVNSVNPTVTLTPMAaeawsDPQK 197
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 86-271 1.61e-14

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 72.52  E-value: 1.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTES-GSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGek 164
Cdd:PRK12828   4 SLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAApLSQTLPGVPADALRIGGIDLVDPQAARRAVDEVNRQFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 GLWGLINNAG--VPGVLAPtdwLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPSK 240
Cdd:PRK12828  82 RLDALVNIAGafVWGTIAD---GDADTWDRMYGVNVKTTLNASKAALPaLTASGGGRIVNIGAGAALKAGPGmGAYAAAK 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 576796343 241 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT 271
Cdd:PRK12828 159 AGVARLTEALAAELLDRGITVNAVLPSIIDT 189
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 90-302 2.05e-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: 2.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVI------AACLtESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGe 163
Cdd:cd08940    3 KVALVTGSTSGIGLGIARALAAAGANIVlngfgdAAEI-EAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 164 kGLWGLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSKY 241
Cdd:cd08940   81 -GVDILVNNAGIQHV-APIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGwGRIINIASVHGLVASANkSAYVAAKH 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 576796343 242 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLadpvkvIEKKLaiweqlsPDIKQQYGEGY 302
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 ...
 87-271 2.25e-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: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  87 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESG----STALKAETSERLRTVLLDVTD--PENVKRTAQWVKNQ 160
Cdd:cd05340    2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKlrqvADHINEEGGRQPQWFILDLLTctSENCQQLAQRIAVN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 161 VGEkgLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKK--AQGRVINVSSVGGRLAIVGGGYTP 238
Cdd:cd05340   82 YPR--LDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKsdAGSLVFTSSSVGRQGRANWGAYAV 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 576796343 239 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT 271
Cdd:cd05340  160 SKFATEGL*QVLADEYQQRNLRVNCINPGGTRT 192
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 87-275 2.47e-14

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 72.23  E-value: 2.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  87 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLT-ESGSTALKAETSE--RLRTVLLDVTDPENVKRTAQWVKNQVGe 163
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNdEAAAAAAEALQKAggKAIGVAMDVTDEEAINAGIDYAVETFG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 164 kGLWGLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSKY 241
Cdd:PRK12429  81 -GVDILVNNAGIQHV-APIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGgGRIINMASVHGLVGSAGkAAYVSAKH 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 576796343 242 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 275
Cdd:PRK12429 159 GLIGLTKVVALEGATHGVTVNAICPGYVDTPLVR 192
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 91-272 2.83e-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: 2.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  91 YIFITGCDSGFGNLAARTFDKKGFHVIAACLTESgSTALKAETSE-----RLRTVLLDVTDPENVKRTAQWVKNQVGEkg 165
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARS-EEPLQELKEElrpglRVTTVKADLSDAAGVEQLLEAIRKLDGE-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKK--AQGRVINVSSVGGRLAIVG-GGYTPSKYA 242
Cdd:cd05367   78 RDLLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKrgLKKTVVNVSSGAAVNPFKGwGLYCSSKAA 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 576796343 243 VegfnDSLRRDMKA--FGVHVSCIEPGLFKTN 272
Cdd:cd05367  158 R----DMFFRVLAAeePDVRVLSYAPGVVDTD 185
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 93-271 2.87e-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: 2.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  93 FITGCDSGFGNLAARTFDKKGFHVIAACL-TESGSTALKAETSERLRTVLL---DVTDPENVKRTAQWVKNQVGekGLWG 168
Cdd:cd05359    2 LVTGGSRGIGKAIALRLAERGADVVINYRkSKDAAAEVAAEIEELGGKAVVvraDVSQPQDVEEMFAAVKERFG--RLDV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAGvPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVggGYTP---SKYAVE 244
Cdd:cd05359   80 LVSNAA-AGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGgGRIVAISSLGSIRALP--NYLAvgtAKAALE 156

                        170       180
                 ....*....|....*....|....*..
gi 576796343 245 GFNDSLRRDMKAFGVHVSCIEPGLFKT 271
Cdd:cd05359  157 ALVRYLAVELGPRGIRVNAVSPGVIDT 183
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 90-295 3.36e-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: 71.64  E-value: 3.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACL-TESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGekG 165
Cdd:cd05366    3 KVAIITGAAQGIGRAIAERLAADGFNIVLADLnLEEAAKSTIQEISEagyNAVAVGADVTDKDDVEALIDQAVEKFG--S 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ--GRVINVSSVGGRLA-IVGGGYTPSKYA 242
Cdd:cd05366   81 FDVMVNNAGI-APITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhgGKIINASSIAGVQGfPNLGAYSASKFA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 576796343 243 VEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAI------WEQLSPDIK 295
Cdd:cd05366  160 VRGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVGEIAGkpegegFAEFSSSIP 218
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 90-289 3.62e-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: 3.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGL 169
Cdd:cd08944    4 KVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFG--GLDLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 170 INNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPSKYAVEGFN 247
Cdd:cd08944   82 VNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPrMIARGGGSIVNLSSIAGQSGDPGyGAYGASKAAIRNLT 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 576796343 248 DSLRRDMKAFGVHVSCIEPGLFKTNLadpvkvIEKKLAIWEQ 289
Cdd:cd08944  162 RTLAAELRHAGIRCNALAPGLIDTPL------LLAKLAGFEG 197
PRK06484 PRK06484
short chain dehydrogenase; Validated
 90-273 3.94e-14

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 73.73  E-value: 3.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwgL 169
Cdd:PRK06484   6 RVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDV--L 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 170 INNAGVPG-VLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVkKAQGR---VINVSSVGGRLAIVG-GGYTPSKYAVE 244
Cdd:PRK06484  84 VNNAGVTDpTMTATLDTTLEEFARLQAINLTGAYLVAREALRLM-IEQGHgaaIVNVASGAGLVALPKrTAYSASKAAVI 162

                        170       180
                 ....*....|....*....|....*....
gi 576796343 245 GFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:PRK06484 163 SLTRSLACEWAAKGIRVNAVLPGYVRTQM 191
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 92-275 5.30e-14

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 70.90  E-value: 5.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  92 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLR----TVLLDVTDPENVKRTAQWVKNQVGEKG-L 166
Cdd:PRK12827   9 VLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAVAAGIEaaggKALGLAFDVRDFAATRAALDAGVEEFGrL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 167 WGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ--GRVINVSSVGGRLAIVGG-GYTPSKYAV 243
Cdd:PRK12827  89 DILVNNAGI-ATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARrgGRIVNIASVAGVRGNRGQvNYAASKAGL 167

                        170       180       190
                 ....*....|....*....|....*....|..
gi 576796343 244 EGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 275
Cdd:PRK12827 168 IGLTKTLANELAPRGITVNAVAPGAINTPMAD 199
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 90-273 5.31e-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: 70.77  E-value: 5.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIaacLTESGSTALKAETSERLR-------TVLLDVTDPENVKRTAQWVKNQVG 162
Cdd:cd05362    4 KVALVTGASRGIGRAIAKRLARDGASVV---VNYASSKAAAEEVVAEIEaaggkaiAVQADVSDPSQVARLFDAAEKAFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 ekGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKkAQGRVINVSSVGGRLAIVG-GGYTPSKY 241
Cdd:cd05362   81 --GVDILVNNAGV-MLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLR-DGGRIINISSSLTAAYTPNyGAYAGSKA 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 576796343 242 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:cd05362  157 AVEAFTRVLAKELGGRGITVNAVAPGPVDTDM 188
PRK05855 PRK05855
SDR family oxidoreductase;
89-275 1.24e-13

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 72.32  E-value: 1.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGStalkAETSERLR-------TVLLDVTDPENVKRTAQWVKNQV 161
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAA----ERTAELIRaagavahAYRVDVSDADAMEAFAEWVRAEH 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 162 GEKGLwgLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLIS-VTLNMLPLVKKAQ-GRVINVSSvggrlaivGGGYTPS 239
Cdd:PRK05855 391 GVPDI--VVNNAGI-GMAGGFLDTSAEDWDRVLDVNLWGVIHgCRLFGRQMVERGTgGHIVNVAS--------AAAYAPS 459

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 576796343 240 ---------KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 275
Cdd:PRK05855 460 rslpayatsKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVA 504
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 86-292 1.53e-13

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 69.60  E-value: 1.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESG----STALKAETSErLRTVLLDVTDPENVKRTAQWVKNQV 161
Cdd:PRK08217   2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKleeaVAECGALGTE-VRGYAANVTDEEDVEATFAQIAEDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 162 GekGLWGLINNAGV----------PGVLapTDWLTLEDYREPIEVNLFGLI----SVTLNMLPLvkKAQGRVINVSSVgG 227
Cdd:PRK08217  81 G--QLNGLINNAGIlrdgllvkakDGKV--TSKMSLEQFQSVIDVNLTGVFlcgrEAAAKMIES--GSKGVIINISSI-A 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 576796343 228 RLAIVG-GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVK--VIEKklaiWEQLSP 292
Cdd:PRK08217 154 RAGNMGqTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKpeALER----LEKMIP 217
PRK06398 PRK06398
aldose dehydrogenase; Validated
 85-292 2.02e-13

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 69.48  E-value: 2.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  85 EDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTAlkaetSERLRtvlLDVTDPENVKRTAQWVKNQVGEK 164
Cdd:PRK06398   2 LGLKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYND-----VDYFK---VDVSNKEQVIKGIDYVISKYGRI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 GLwgLINNAGVP--GVLAPTDwltLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIV-GGGYTPSK 240
Cdd:PRK06398  74 DI--LVNNAGIEsyGAIHAVE---EDEWDRIINVNVNGIFLMSKYTIPyMLKQDKGVIINIASVQSFAVTRnAAAYVTSK 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 576796343 241 YAVEGFNDSLRRDMkAFGVHVSCIEPGLFKTNL----------ADPVKvIEKKLAIWEQLSP 292
Cdd:PRK06398 149 HAVLGLTRSIAVDY-APTIRCVAVCPGSIRTPLlewaaelevgKDPEH-VERKIREWGEMHP 208
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 89-278 3.05e-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: 68.78  E-value: 3.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE----RLRTVLLDVTD-PENVKRTAQWVKN-QVG 162
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEkygvETKTIAADFSAgDDIYERIEKELEGlDIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 EkglwgLINNAGV----PGVLAPTDwltLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGG-----RLAIv 232
Cdd:cd05356   81 I-----LVNNVGIshsiPEYFLETP---EDELQDIINVNVMATLKMTRLILPgMVKRKKGAIVNISSFAGliptpLLAT- 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 576796343 233 gggYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVK 278
Cdd:cd05356  152 ---YSASKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSKIRK 194
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 88-267 4.18e-13

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 68.45  E-value: 4.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  88 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE---TSERLRTVLLDVTDPENVKRTAQWVKNQVGek 164
Cdd:PRK07890   4 KGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEiddLGRRALAVPTDITDEDQCANLVALALERFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 GLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVG-GGYTPSKYAV 243
Cdd:PRK07890  82 RVDALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMINSMVLRHSQPKyGAYKMAKGAL 161

                        170       180
                 ....*....|....*....|....
gi 576796343 244 EGFNDSLRRDMKAFGVHVSCIEPG 267
Cdd:PRK07890 162 LAASQSLATELGPQGIRVNSVAPG 185
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 89-289 4.54e-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: 68.45  E-value: 4.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLL---DVTDPENVKRTAQWVKNQVGekG 165
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAGVLAvvaDLTDPEDIDRLVEKAGDAFG--R 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LWGLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVGGGYTP-SKYAV 243
Cdd:cd05344   79 VDILVNNAGGPPP-GPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLTVKEPEPNLVLSNvARAGL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 576796343 244 EGFNDSLRRDMKAFGVHVSCIEPGLFKTN-LADPVKVIEKKLAIWEQ 289
Cdd:cd05344  158 IGLVKTLSRELAPDGVTVNSVLPGYIDTErVRRLLEARAEKEGISVE 204
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 86-261 5.40e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 68.84  E-value: 5.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE--TSERLRTVLLDVTDPENVKRTAQWVKNQVGe 163
Cdd:PRK05872   6 SLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAElgGDDRVLTVVADVTDLAAMQAAAEEAVERFG- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 164 kGLWGLINNAGV--PGVLAPTDwltLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGGG-YTPSK 240
Cdd:PRK05872  85 -GIDVVVANAGIasGGSVAQVD---PDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSLAAFAAAPGMAaYCASK 160

                        170       180
                 ....*....|....*....|.
gi 576796343 241 YAVEGFNDSLRRDMKAFGVHV 261
Cdd:PRK05872 161 AGVEAFANALRLEVAHHGVTV 181
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 84-274 6.17e-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: 6.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  84 IEDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLL----DVTDPENVKRTAQWVKN 159
Cdd:cd05343    1 MERWRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLFpyqcDLSNEEQILSMFSAIRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 160 QVGekGLWGLINNAGvpgvLAPTDWL---TLEDYREPIEVNLFGLISVT---LNMLPLVKKAQGRVINVSSVGGR---LA 230
Cdd:cd05343   81 QHQ--GVDVCINNAG----LARPEPLlsgKTEGWKEMFDVNVLALSICTreaYQSMKERNVDDGHIININSMSGHrvpPV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 576796343 231 IVGGGYTPSKYAVEGFNDSLRRDMKAFGVH--VSCIEPGLFKTNLA 274
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 ...
 76-283 7.18e-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: 7.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  76 WTRKGKLKIeditdkyifITGCDSGFGNLAARTFDKKGFHVIA---------ACLTESGSTALKAETSerlrtvLLDVTD 146
Cdd:cd05329    2 WNLEGKTAL---------VTGGTKGIGYAIVEELAGLGAEVYTcarnqkeldECLTEWREKGFKVEGS------VCDVSS 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 147 PENVKRTAQWVKNQVGEKgLWGLINNAGVPGVLAPTDWlTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSV 225
Cdd:cd05329   67 RSERQELMDTVASHFGGK-LNILVNNAGTNIRKEAKDY-TEEDYSLIMSTNFEAAYHLSRLAHPLLKASGnGNIVFISSV 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 576796343 226 GGRLAI-VGGGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPV--------KVIEKK 283
Cdd:cd05329  145 AGVIAVpSGAPYGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPViqqkenldKVIERT 211
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 86-268 1.02e-12

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 67.73  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGstalkaETSERLRTVLLDVTDPENVKRTAQWVKNQVGEkg 165
Cdd:PRK06171   6 NLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGD------GQHENYQFVPTDVSSAEEVNHTVAEIIEKFGR-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LWGLINNAGV--PGVLA-PTD-----WLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGG- 235
Cdd:PRK06171  78 IDGLVNNAGIniPRLLVdEKDpagkyELNEAAFDKMFNINQKGVFLMSQAVARqMVKQHDGVIVNMSSEAGLEGSEGQSc 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 576796343 236 YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGL 268
Cdd:PRK06171 158 YAATKAALNSFTRSWAKELGKHNIRVVGVAPGI 190
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
89-300 1.02e-12

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 67.36  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWG 168
Cdd:PRK07067   6 GKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFG--GIDI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAGVPGvLAPTDWLTLEDYREPIEVNLFGlisvTLNMLPLVKK---AQGR---VINVSSVGGR----LAIVgggYTP 238
Cdd:PRK07067  84 LFNNAALFD-MAPILDISRDSYDRLFAVNVKG----LFFLMQAVARhmvEQGRggkIINMASQAGRrgeaLVSH---YCA 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 576796343 239 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVkviEKKLAIWEQLSP-DIKQQYGE 300
Cdd:PRK07067 156 TKAAVISYTQSAALALIRHGINVNAIAPGVVDTPMWDQV---DALFARYENRPPgEKKRLVGE 215
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 87-292 1.20e-12

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: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  87 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAAcLTESGSTAlkAETSERLRT-------VLLDVTDPENVKRTAQWVKN 159
Cdd:cd05358    1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVN-YRSKEDAA--EEVVEEIKAvggkaiaVQADVSKEEDVVALFQSAIK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 160 QVGEKGLWglINNAGVPGVLAPTDwLTLEDYREPIEVNLFGLISV---TLNMLpLVKKAQGRVINVSSVGGRLAIVG-GG 235
Cdd:cd05358   78 EFGTLDIL--VNNAGLQGDASSHE-MTLEDWNKVIDVNLTGQFLCareAIKRF-RKSKIKGKIINMSSVHEKIPWPGhVN 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 576796343 236 YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSP 292
Cdd:cd05358  154 YAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDPEQRADLLSLIP 210
PRK06139 PRK06139
SDR family oxidoreductase;
89-271 1.35e-12

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 67.82  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFH-VIAAclteSGSTALkAETSERLR-------TVLLDVTDPENVKRTAQWVKNQ 160
Cdd:PRK06139   7 GAVVVITGASSGIGQATAEAFARRGARlVLAA----RDEEAL-QAVAEECRalgaevlVVPTDVTDADQVKALATQAASF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 161 VGEKGLWglINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKaQGR--VINVSSVGGRLAI-VGGGYT 237
Cdd:PRK06139  82 GGRIDVW--VNNVGV-GAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKK-QGHgiFINMISLGGFAAQpYAAAYS 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 576796343 238 PSKYAVEGFNDSLRRDMKAF-GVHVSCIEPGLFKT 271
Cdd:PRK06139 158 ASKFGLRGFSEALRGELADHpDIHVCDVYPAFMDT 192
PRK05866 PRK05866
SDR family oxidoreductase;
86-278 1.50e-12

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 67.46  E-value: 1.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSER---LRTVLLDVTDPENVKRTAQWVKNQVG 162
Cdd:PRK05866  37 DLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAggdAMAVPCDLSDLDAVDALVADVEKRIG 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 ekGLWGLINNAG----VPGVLAPTDWltlEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSvGGRLAIVG---G 234
Cdd:PRK05866 117 --GVDILINNAGrsirRPLAESLDRW---HDVERTMVLNYYAPLRLIRGLAPgMLERGDGHIINVAT-WGVLSEASplfS 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 576796343 235 GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVK 278
Cdd:PRK05866 191 VYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPMIAPTK 234
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 86-271 1.66e-12

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 66.65  E-value: 1.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACL-TESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGeK 164
Cdd:PRK08642   2 QISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHqSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEHFG-K 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 GLWGLINNAGV-----PGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYT 237
Cdd:PRK08642  81 PITTVVNNALAdfsfdGDARKKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGfGRIINIGTNLFQNPVVPyHDYT 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 576796343 238 PSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT 271
Cdd:PRK08642 161 TAKAALLGLTRNLAAELGPYGITVNMVSGGLLRT 194
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 86-289 2.44e-12

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 66.46  E-value: 2.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE---TSERLRTVLLDVTDPENVKRTAQWVKNQVG 162
Cdd:PRK13394   4 NLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEinkAGGKAIGVAMDVTNEDAVNAGIDKVAERFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 EKGLwgLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ--GRVINVSSVGGRLAIVG-GGYTPS 239
Cdd:PRK13394  84 SVDI--LVSNAGIQIV-NPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHSHEASPLkSAYVTA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 576796343 240 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADP-VKVIEKKLAIWEQ 289
Cdd:PRK13394 161 KHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKqIPEQAKELGISEE 211
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 86-271 3.43e-12

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 65.74  E-value: 3.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLL---DVTDPENVKRTAQWVKNQVG 162
Cdd:PRK08213   9 DLSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGIDALWiaaDVADEADIERLAEETLERFG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 EKGLwgLINNAGVP-GvlAPTDWLTLEDYREPIEVNLFGLISVT-----LNMLPlvkKAQGRVINVSSVGGrlaiVGG-- 234
Cdd:PRK08213  89 HVDI--LVNNAGATwG--APAEDHPVEAWDKVMNLNVRGLFLLSqavakRSMIP---RGYGRIINVASVAG----LGGnp 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 576796343 235 -------GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT 271
Cdd:PRK08213 158 pevmdtiAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPT 201
PRK06484 PRK06484
short chain dehydrogenase; Validated
 94-271 3.61e-12

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 67.57  E-value: 3.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwgLINNA 173
Cdd:PRK06484 274 ITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRLDV--LVNNA 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 174 GVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAqGRVINVSSVGGRLAIVG-GGYTPSKYAVEGFNDSLRR 252
Cdd:PRK06484 352 GIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG-GVIVNLGSIASLLALPPrNAYCASKAAVTMLSRSLAC 430

                        170
                 ....*....|....*....
gi 576796343 253 DMKAFGVHVSCIEPGLFKT 271
Cdd:PRK06484 431 EWAPAGIRVNTVAPGYIET 449
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 85-273 4.30e-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: 65.94  E-value: 4.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  85 EDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLT-ESGSTALKAETS--ERLRTVLLDVTDPENVKRTAQWVKNQV 161
Cdd:cd08935    1 FSLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNqEKGDKVAKEITAlgGRAIALAADVLDRASLERAREEIVAQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 162 GEKGLwgLINNAG--VPGVLAPTDWLTLEDYREPIEVNLFGLISVT-LNML-----------PLVKKAQGRVINVSSVGG 227
Cdd:cd08935   81 GTVDI--LINGAGgnHPDATTDPEHYEPETEQNFFDLDEEGWEFVFdLNLNgsflpsqvfgkDMLEQKGGSIINISSMNA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 576796343 228 RLAIVG-GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:cd08935  159 FSPLTKvPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQ 205
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 80-273 4.35e-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: 4.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  80 GKLKieditDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTA---LKAETSERLRTVLL--DVTDPENVKRTA 154
Cdd:cd05355   22 GKLK-----GKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEDDAeetKKLIEEEGRKCLLIpgDLGDESFCRDLV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 155 QWVKNQVGekGLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAqGRVINVSSVggrLAIVGG 234
Cdd:cd05355   97 KEVVKEFG--KLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKKG-SSIINTTSV---TAYKGS 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 576796343 235 G----YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:cd05355  171 PhlldYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPL 213
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
90-273 4.85e-12

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 65.48  E-value: 4.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETS-ERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLWG 168
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKELTKLAEQYnSNLTFHSLDLQDVHELETNFNEILSSIQEDNVSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 --LINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQG--RVINVSSVGGRLAIVG-GGYTPSKYAV 243
Cdd:PRK06924  82 ihLINNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKVdkRVINISSGAAKNPYFGwSAYCSSKAGL 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 576796343 244 EGFNDS--LRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:PRK06924 162 DMFTQTvaTEQEEEEYPVKIVAFSPGVMDTNM 193
PLN02253 PLN02253
xanthoxin dehydrogenase
 90-276 6.10e-12

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 65.61  E-value: 6.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHV-IAACLTESGSTALKA-ETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLw 167
Cdd:PLN02253  19 KVALVTGGATGIGESIVRLFHKHGAKVcIVDLQDDLGQNVCDSlGGEPNVCFFHCDVTVEDDVSRAVDFTVDKFGTLDI- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 168 gLINNAGVPGvlAP-TDW--LTLEDYREPIEVNL----FGLISVTLNMLPLVKkaqGRVINVSSVGGRLAIVG-GGYTPS 239
Cdd:PLN02253  98 -MVNNAGLTG--PPcPDIrnVELSEFEKVFDVNVkgvfLGMKHAARIMIPLKK---GSIVSLCSVASAIGGLGpHAYTGS 171

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 576796343 240 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADP 276
Cdd:PLN02253 172 KHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALA 208
PRK07069 PRK07069
short chain dehydrogenase; Validated
 93-285 7.41e-12

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 64.73  E-value: 7.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  93 FITGCDSGFGNLAARTFDKKGFHVIAACL-TESGSTALKAETSERLRT-----VLLDVTDPENVKRTAQWVKNQVGekGL 166
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVFLTDInDAAGLDAFAAEINAAHGEgvafaAVQDVTDEAQWQALLAQAADAMG--GL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 167 WGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGrlAIVGG---GYTPSKYA 242
Cdd:PRK07069  81 SVLVNNAGV-GSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQpASIVNISSVAA--FKAEPdytAYNASKAA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 576796343 243 VEGFNDSLRRDMKAFGVHVSC--IEPGLFKTNLADPV------KVIEKKLA 285
Cdd:PRK07069 158 VASLTKSIALDCARRGLDVRCnsIHPTFIRTGIVDPIfqrlgeEEATRKLA 208
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 86-267 7.83e-12

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 64.91  E-value: 7.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGstalkaETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKG 165
Cdd:PRK08220   5 DFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLT------QEDYPFATFVLDVSDAAAVAQVCQRLLAETGPLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LwgLINNAGVPGvLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVK-KAQGRVINVSSVGGRLAIVG-GGYTPSKYAV 243
Cdd:PRK08220  79 V--LVNAAGILR-MGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRrQRSGAIVTVGSNAAHVPRIGmAAYGASKAAL 155

                        170       180
                 ....*....|....*....|....
gi 576796343 244 EGFNDSLRRDMKAFGVHVSCIEPG 267
Cdd:PRK08220 156 TSLAKCVGLELAPYGVRCNVVSPG 179
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 89-296 8.29e-12

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 64.87  E-value: 8.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGekG 165
Cdd:PRK06113  11 GKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQlggQAFACRCDITSEQELSALADFALSKLG--K 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LWGLINNAGVPGVlAPTDwLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVI-NVSSVGG-----RLAivggGYTPS 239
Cdd:PRK06113  89 VDILVNNAGGGGP-KPFD-MPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVIlTITSMAAenkniNMT----SYASS 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 576796343 240 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNladpvkviekklAIWEQLSPDIKQ 296
Cdd:PRK06113 163 KAAASHLVRNMAFDLGEKNIRVNGIAPGAILTD------------ALKSVITPEIEQ 207
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 86-292 8.58e-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: 8.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHV----IAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQV 161
Cdd:cd05352    5 SLKGKVAIVTGGSRGIGLAIARALAEAGADVaiiyNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 162 GEkgLWGLINNAGVPGVLAPTDwLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG---GGYT 237
Cdd:cd05352   85 GK--IDILIANAGITVHKPALD-YTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGkGSLIITASMSGTIVNRPqpqAAYN 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 576796343 238 PSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLaiWEQLSP 292
Cdd:cd05352  162 ASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKK--WESYIP 214
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
90-271 9.12e-12

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 64.75  E-value: 9.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETS---ERLRTVLLDVTDPENVKRTAQWVKNQVGekGL 166
Cdd:PRK08643   3 KVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSkdgGKAIAVKADVSDRDQVFAAVRQVVDTFG--DL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 167 WGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ--GRVINVSSVGG-----RLAIvgggYTPS 239
Cdd:PRK08643  81 NVVVNNAGV-APTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGhgGKIINATSQAGvvgnpELAV----YSST 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 576796343 240 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT 271
Cdd:PRK08643 156 KFAVRGLTQTAARDLASEGITVNAYAPGIVKT 187
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 90-273 1.05e-11

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: 64.80  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACL----TESGSTALKAETSERLRTVL-LDVTDPENVKRTAQWVKNQvgEK 164
Cdd:cd09807    2 KTVIITGANTGIGKETARELARRGARVIMACRdmakCEEAAAEIRRDTLNHEVIVRhLDLASLKSIRAFAAEFLAE--ED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 GLWGLINNAGVpgVLAPTdWLTLEDYREPIEVNLFGLISVTLNMLPLVKK-AQGRVINVSSV---GGRLAI--------- 231
Cdd:cd09807   80 RLDVLINNAGV--MRCPY-SKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKsAPSRIVNVSSLahkAGKINFddlnseksy 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 576796343 232 -VGGGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:cd09807  157 nTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTEL 199
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 88-305 1.07e-11

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 64.29  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  88 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLR-----TVLLDVTDPENVKRTAQWVKNQVG 162
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGegmayGFGADATSEQSVLALSRGVDEIFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 EKGLwgLINNAGVpGVLAPTDWLTLEDYREPIEVNLFG--LISVTLNMLPLVKKAQGRVINVSSVGGRlaiVGG----GY 236
Cdd:PRK12384  81 RVDL--LVYNAGI-AKAAFITDFQLGDFDRSLQVNLVGyfLCAREFSRLMIRDGIQGRIIQINSKSGK---VGSkhnsGY 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 576796343 237 TPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGlfktNLADP---VKVIE---KKLAIweqlSPDIKQQYgegYIEK 305
Cdd:PRK12384 155 SAAKFGGVGLTQSLALDLAEYGITVHSLMLG----NLLKSpmfQSLLPqyaKKLGI----KPDEVEQY---YIDK 218
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 89-287 1.21e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 64.39  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVIAaclteSGSTALKAETS-ERLR-------TVLLDVTDPENVKRTAQWVKNQ 160
Cdd:PRK08085   9 GKNILITGSAQGIGFLLATGLAEYGAEIII-----NDITAERAELAvAKLRqegikahAAPFNVTHKQEVEAAIEHIEKD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 161 VGEKGLwgLINNAGVPGVLAPTDWlTLEDYREPIEVNLFG--LIS--VTLNMlplVKKAQGRVINVSSVG---GRLAIVg 233
Cdd:PRK08085  84 IGPIDV--LINNAGIQRRHPFTEF-PEQEWNDVIAVNQTAvfLVSqaVARYM---VKRQAGKIINICSMQselGRDTIT- 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 576796343 234 gGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVkVIEKKLAIW 287
Cdd:PRK08085 157 -PYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKAL-VEDEAFTAW 208
PRK06194 PRK06194
hypothetical protein; Provisional
 84-275 1.34e-11

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 64.65  E-value: 1.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  84 IEDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTE----SGSTALKAETSERLrTVLLDVTDPENVKRTAQWVKN 159
Cdd:PRK06194   1 MKDFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQdaldRAVAELRAQGAEVL-GVRTDVSDAAQVEALADAALE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 160 QVGEKGLwgLINNAGVP--GVLaptdWL-TLEDYREPIEVNLFGLIS----VTLNMLPLVKKA---QGRVINVSSVGGRL 229
Cdd:PRK06194  80 RFGAVHL--LFNNAGVGagGLV----WEnSLADWEWVLGVNLWGVIHgvraFTPLMLAAAEKDpayEGHIVNTASMAGLL 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 576796343 230 AIVGGG-YTPSKYAVEGFNDSLRRDMKAFG--VHVSCIEPGLFKTNLAD 275
Cdd:PRK06194 154 APPAMGiYNVSKHAVVSLTETLYQDLSLVTdqVGASVLCPYFVPTGIWQ 202
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 89-300 1.76e-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: 1.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWG 168
Cdd:cd05363    3 GKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWG--SIDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAGVPGvLAPTDWLTLEDYREPIEVNLFGlisvTLNMLPLVKK---AQGR---VINVSSVGGRL--AIVgGGYTPSK 240
Cdd:cd05363   81 LVNNAALFD-LAPIVDITRESYDRLFAINVSG----TLFMMQAVARamiAQGRggkIINMASQAGRRgeALV-GVYCATK 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 576796343 241 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVkviEKKLAIWEQLS-PDIKQQYGE 300
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 ...
 92-267 1.94e-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: 1.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  92 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESgstaLKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGLIN 171
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFV----LLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHG--PIDALVN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 172 NAGVPgVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGG---RLAIvgGGYTPSKYAVEGFN 247
Cdd:cd05331   75 CAGVL-RPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPhMKDRRTGAIVTVASNAAhvpRISM--AAYGASKAALASLS 151

                        170       180
                 ....*....|....*....|
gi 576796343 248 DSLRRDMKAFGVHVSCIEPG 267
Cdd:cd05331  152 KCLGLELAPYGVRCNVVSPG 171
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 90-285 1.99e-11

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 63.48  E-value: 1.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVI-----AACLTESGSTALKAETSERLrTVLLDVTDPENVKRTAQWVKNQVGEK 164
Cdd:PRK12935   7 KVAIVTGGAKGIGKAITVALAQEGAKVVinynsSKEAAENLVNELGKEGHDVY-AVQADVSKVEDANRLVEEAVNHFGKV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 GLwgLINNAGVPGVLAPTDwLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSKYA 242
Cdd:PRK12935  86 DI--LVNNAGITRDRTFKK-LNREDWERVIDVNLSSVFNTTSAVLPYITEAEeGRIISISSIIGQAGGFGqTNYSAAKAG 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 576796343 243 VEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL--ADPVKVIEKKLA 285
Cdd:PRK12935 163 MLGFTKSLALELAKTNVTVNAICPGFIDTEMvaEVPEEVRQKIVA 207
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 89-266 2.23e-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: 2.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWG 168
Cdd:cd05345    5 GKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFG--RLDI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVI-NVSSVGG---RLAIVggGYTPSKYAVE 244
Cdd:cd05345   83 LVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIiNIASTAGlrpRPGLT--WYNASKGWVV 160

                        170       180
                 ....*....|....*....|..
gi 576796343 245 GFNDSLRRDMKAFGVHVSCIEP 266
Cdd:cd05345  161 TATKAMAVELAPRNIRVNCLCP 182
PRK07024 PRK07024
SDR family oxidoreductase;
92-271 3.16e-11

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 63.02  E-value: 3.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  92 IFITGCDSGFGNLAARTFDKKGFHV--IAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwgL 169
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLglVARRTDALQAFAARLPKAARVSVYAADVRDADALAAAAADFIAAHGLPDV--V 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 170 INNAGVP-GVLA--PTDwltLEDYREPIEVNLFGLISvTLN--MLPLVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYAV 243
Cdd:PRK07024  83 IANAGISvGTLTeeRED---LAVFREVMDTNYFGMVA-TFQpfIAPMRAARRGTLVGIASVAGVRGLPGAGaYSASKAAA 158

                        170       180
                 ....*....|....*....|....*...
gi 576796343 244 EGFNDSLRRDMKAFGVHVSCIEPGLFKT 271
Cdd:PRK07024 159 IKYLESLRVELRPAGVRVVTIAPGYIRT 186
PRK07062 PRK07062
SDR family oxidoreductase;
86-225 3.63e-11

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 63.14  E-value: 3.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHViAAC------LTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKN 159
Cdd:PRK07062   5 QLEGRVAVVTGGSSGIGLATVELLLEAGASV-AICgrdeerLASAEARLREKFPGARLLAARCDVLDEADVAAFAAAVEA 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 576796343 160 QVGekGLWGLINNAGvPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKA-QGRVINVSSV 225
Cdd:PRK07062  84 RFG--GVDMLVNNAG-QGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASaAASIVCVNSL 147
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 80-267 4.78e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 62.74  E-value: 4.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  80 GKLKieditDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTalkAETSERL-----RTVLL--DVTDP----E 148
Cdd:PRK06701  42 GKLK-----GKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDA---NETKQRVekegvKCLLIpgDVSDEafckD 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 149 NVKRTAQwvknQVGekGLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAqGRVINVSSVGGr 228
Cdd:PRK06701 114 AVEETVR----ELG--RLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLKQG-SAIINTGSITG- 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 576796343 229 laIVGGG----YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPG 267
Cdd:PRK06701 186 --YEGNEtlidYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPG 226
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 94-271 5.77e-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: 5.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGLI 170
Cdd:cd05365    4 VTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQaggQAIGLECNVTSEQDLEAVVKATVSQFG--GITILV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 171 NNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVI-NVSSVGGRL-AIVGGGYTPSKYAVEGFND 248
Cdd:cd05365   82 NNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAIlNISSMSSENkNVRIAAYGSSKAAVNHMTR 161

                        170       180
                 ....*....|....*....|...
gi 576796343 249 SLRRDMKAFGVHVSCIEPGLFKT 271
Cdd:cd05365  162 NLAFDLGPKGIRVNAVAPGAVKT 184
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
86-283 6.56e-11

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 62.06  E-value: 6.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGStALKAETSERLRTVL---LDVTDPENVKRTAQWVKNQVG 162
Cdd:PRK06935  12 SLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWD-ETRRLIEKEGRKVTfvqVDLTKPESAEKVVKEALEEFG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 EKGLwgLINNAGVPGvLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVggrLAIVGG----GYT 237
Cdd:PRK06935  91 KIDI--LVNNAGTIR-RAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKvMAKQGSGKIINIASM---LSFQGGkfvpAYT 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 576796343 238 PSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKK 283
Cdd:PRK06935 165 ASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAPIRADKNR 210
PRK06949 PRK06949
SDR family oxidoreductase;
86-273 8.05e-11

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 61.70  E-value: 8.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSER---LRTVLLDVTDPENVKRTAQWVKNQVG 162
Cdd:PRK06949   6 NLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEggaAHVVSLDVTDYQSIKAAVAHAETEAG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 EKGLwgLINNAGVPGVLAPTDwLTLEDYREPIEVNLFGLI----SVTLNMLPLVK-----KAQGRVINVSSVGGrLAIVG 233
Cdd:PRK06949  86 TIDI--LVNNSGVSTTQKLVD-VTPADFDFVFDTNTRGAFfvaqEVAKRMIARAKgagntKPGGRIINIASVAG-LRVLP 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 576796343 234 --GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:PRK06949 162 qiGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEI 203
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 89-267 8.81e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 61.48  E-value: 8.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE-TSERLRTVLL--DVTDPENVKRTAQWVKNQVGekG 165
Cdd:PRK07478   6 GKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEiRAEGGEAVALagDVRDEAYAKALVALAVERFG--G 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSS-VGGRLAIVG-GGYTPSKYA 242
Cdd:PRK07478  84 LDIAFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPaMLARGGGSLIFTSTfVGHTAGFPGmAAYAASKAG 163

                        170       180
                 ....*....|....*....|....*
gi 576796343 243 VEGFNDSLRRDMKAFGVHVSCIEPG 267
Cdd:PRK07478 164 LIGLTQVLAAEYGAQGIRVNALLPG 188
PRK06124 PRK06124
SDR family oxidoreductase;
94-271 1.03e-10

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 61.65  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKGFHVI-----AACLTESGST----ALKAETserlrtVLLDVTDPENVKRTAQWVKNQVGek 164
Cdd:PRK06124  16 VTGSARGLGFEIARALAGAGAHVLvngrnAATLEAAVAAlraaGGAAEA------LAFDIADEEAVAAAFARIDAEHG-- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 GLWGLINNAGVPGvLAPTDWLTLEDYREPIEVNLFGLISVT-LNMLPLVKKAQGRVINVSSVGGRLAIVGGG-YTPSKYA 242
Cdd:PRK06124  88 RLDILVNNVGARD-RRPLAELDDAAIRALLETDLVAPILLSrLAAQRMKRQGYGRIIAITSIAGQVARAGDAvYPAAKQG 166

                        170       180
                 ....*....|....*....|....*....
gi 576796343 243 VEGFNDSLRRDMKAFGVHVSCIEPGLFKT 271
Cdd:PRK06124 167 LTGLMRALAAEFGPHGITSNAIAPGYFAT 195
PRK06138 PRK06138
SDR family oxidoreductase;
86-273 1.29e-10

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 61.32  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE--TSERLRTVLLDVTDPENVKRTAQWVKNQVGe 163
Cdd:PRK06138   2 RLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAiaAGGRAFARQGDVGSAEAVEALVDFVAARWG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 164 kGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSvggRLAIVGG----GYTP 238
Cdd:PRK06138  81 -RLDVLVNNAGF-GCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGgGSIVNTAS---QLALAGGrgraAYVA 155

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 576796343 239 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:PRK06138 156 SKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPY 190
PRK06101 PRK06101
SDR family oxidoreductase;
92-301 1.33e-10

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 61.04  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  92 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAeTSERLRTVLLDVTDPENVKRTAQWVKNQvgeKGLWglIN 171
Cdd:PRK06101   4 VLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDELHT-QSANIFTLAFDVTDHPGTKAALSQLPFI---PELW--IF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 172 NAGvpgvlaptDWLTLED-------YREPIEVNLFGLISVTLNMLPLVKKAQgRVINVSSVGGRLAIV-GGGYTPSKYAV 243
Cdd:PRK06101  78 NAG--------DCEYMDDgkvdatlMARVFNVNVLGVANCIEGIQPHLSCGH-RVVIVGSIASELALPrAEAYGASKAAV 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 576796343 244 EGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSPDIKQQYGEG 301
Cdd:PRK06101 149 AYFARTLQLDLRPKGIEVVTVFPGFVATPLTDKNTFAMPMIITVEQASQEIRAQLARG 206
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 94-273 1.70e-10

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 61.13  E-value: 1.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKGFHVIAACLTESG----STALKAETSErLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwgL 169
Cdd:PRK05876  11 ITGGASGIGLATGTEFARRGARVVLGDVDKPGlrqaVNHLRAEGFD-VHGVMCDVRHREEVTHLADEAFRLLGHVDV--V 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 170 INNAGVPgVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP--LVKKAQGRVINVSSVGGRLAIVG-GGYTPSKYAVEGF 246
Cdd:PRK05876  88 FSNAGIV-VGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPrlLEQGTGGHVVFTASFAGLVPNAGlGAYGVAKYGVVGL 166

                        170       180
                 ....*....|....*....|....*..
gi 576796343 247 NDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:PRK05876 167 AETLAREVTADGIGVSVLCPMVVETNL 193
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 92-227 2.92e-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: 2.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  92 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTAlkaetserlrtvllDVTDPENVKRTAQWVKNQVGeKGLWGLIN 171
Cdd:cd05328    2 IVITGAASGIGAATAELLEDAGHTVIGIDLREADVIA--------------DLSTPEGRAAAIADVLARCS-GVLDGLVN 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 576796343 172 NAGVPGVlAPTDwLTLedyrepiEVNLFGLISVTLNMLPLVKKA-QGRVINVSSVGG 227
Cdd:cd05328   67 CAGVGGT-TVAG-LVL-------KVNYFGLRALMEALLPRLRKGhGPAAVVVSSIAG 114
PRK08251 PRK08251
SDR family oxidoreductase;
88-278 3.80e-10

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 59.56  E-value: 3.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  88 TDKYIFITGCDSGFGNLAARTFDKKGfHVIAAC------LTEsgstaLKAETSER--LRTVL---LDVTDPENVKRTAQW 156
Cdd:PRK08251   1 TRQKILITGASSGLGAGMAREFAAKG-RDLALCarrtdrLEE-----LKAELLARypGIKVAvaaLDVNDHDQVFEVFAE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 157 VKNQVGekGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLIS---VTLNMLplvkKAQGR--VINVSSVggrLAI 231
Cdd:PRK08251  75 FRDELG--GLDRVIVNAGI-GKGARLGTGKFWANKATAETNFVAALAqceAAMEIF----REQGSghLVLISSV---SAV 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 576796343 232 VG-----GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVK 278
Cdd:PRK08251 145 RGlpgvkAAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNAKAK 196
PRK06114 PRK06114
SDR family oxidoreductase;
86-292 4.24e-10

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 59.80  E-value: 4.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHViaACLTESGSTALkAETSERLRT-------VLLDVTDPENVKRTAQWVK 158
Cdd:PRK06114   5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADV--ALFDLRTDDGL-AETAEHIEAagrraiqIAADVTSKADLRAAVARTE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 159 NQVGEKGLwgLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGL-ISVTLNMLPLVKKAQGRVINVSSVGGrlAIVGGG-- 235
Cdd:PRK06114  82 AELGALTL--AVNAAGIANA-NPAEEMEEEQWQTVMDINLTGVfLSCQAEARAMLENGGGSIVNIASMSG--IIVNRGll 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 236 ---YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEkKLAIWEQLSP 292
Cdd:PRK06114 157 qahYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTRPEMVH-QTKLFEEQTP 215
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 169-290 8.70e-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: 8.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVK-KAQGRVINVSSVGGRLAIVG-GGYTPSKYAVEGF 246
Cdd:cd02266   35 VVHNAAILDD-GRLIDLTGSRIERAIRANVVGTRRLLEAARELMKaKRLGRFILISSVAGLFGAPGlGGYAASKAALDGL 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 576796343 247 NDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQL 290
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, ...
 86-294 1.50e-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: 58.13  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEkg 165
Cdd:cd05348    1 WLKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGK-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LWGLINNAGV---PGVLAPTDWLTLED-YREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGrLAIVGGG--YTPS 239
Cdd:cd05348   79 LDCFIGNAGIwdySTSLVDIPEEKLDEaFDELFHINVKGYILGAKAALPALYATEGSVIFTVSNAG-FYPGGGGplYTAS 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 576796343 240 KYAVEGFNDSLRRDMkAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSPDI 294
Cdd:cd05348  158 KHAVVGLVKQLAYEL-APHIRVNGVAPGGMVTDLRGPASLGQGETSISTPPLDDM 211
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 94-243 2.41e-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: 57.40  E-value: 2.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGS--TALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGLIN 171
Cdd:cd08943    6 VTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAekVAEAAQGGPRALGVQCDVTSEAQVQSAFEQAVLEFG--GLDIVVS 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 576796343 172 NAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKaQGrvinvssVGGRLAIVGggytpSKYAV 243
Cdd:cd08943   84 NAGIATS-SPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKS-QG-------IGGNIVFNA-----SKNAV 141
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 86-269 2.62e-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: 2.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAacltesgsTALKAE----TSERLRT------VLLDVTDPENVKRTAQ 155
Cdd:cd08942    3 SVAGKIVLVTGGSRGIGRMIAQGFLEAGARVII--------SARKAEacadAAEELSAygeciaIPADLSSEEGIEALVA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 156 wvknQVGEKG--LWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-----GRVINVSSVGGr 228
Cdd:cd08942   75 ----RVAERSdrLDVLVNNAGA-TWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAAtaenpARVINIGSIAG- 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 576796343 229 laIVGGG-----YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLF 269
Cdd:cd08942  149 --IVVSGlenysYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRF 192
PRK12746 PRK12746
SDR family oxidoreductase;
84-273 6.09e-09

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 56.20  E-value: 6.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  84 IEDITDKYIFITGCDSGFGNLAARTFDKKGFHVI---AACLTESGSTALKAETSE-RLRTVLLDVTDPENVKRTAQWVKN 159
Cdd:PRK12746   1 MKNLDGKVALVTGASRGIGRAIAMRLANDGALVAihyGRNKQAADETIREIESNGgKAFLIEADLNSIDGVKKLVEQLKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 160 Q----VGEKGLWGLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKkAQGRVINVSSVGGRLAIVGG- 234
Cdd:PRK12746  81 ElqirVGTSEIDILVNNAGI-GTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLR-AEGRVINISSAEVRLGFTGSi 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 576796343 235 GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:PRK12746 159 AYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDI 197
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
90-224 6.13e-09

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 57.55  E-value: 6.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE--TSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLW 167
Cdd:PRK08324 423 KVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAElgGPDRALGVACDVTDEAAVQAAFEEAALAFG--GVD 500

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 576796343 168 GLINNAGVPGVlAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ--GRVINVSS 224
Cdd:PRK08324 501 IVVSNAGIAIS-GPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGlgGSIVFIAS 558
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 86-276 6.20e-09

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 56.31  E-value: 6.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVI-----AACLtESGSTALKAETSErLRTVLLDVTDPENVKRTAQWVKNQ 160
Cdd:PRK07523   7 DLTGRRALVTGSSQGIGYALAEGLAQAGAEVIlngrdPAKL-AAAAESLKGQGLS-AHALAFDVTDHDAVRAAIDAFEAE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 161 VGEKGLwgLINNAGVPgVLAPTDWLTLEDYREPIEVNLFGLISVTLNML-PLVKKAQGRVINVSSVGGRLAIVG-GGYTP 238
Cdd:PRK07523  85 IGPIDI--LVNNAGMQ-FRTPLEDFPADAFERLLRTNISSVFYVGQAVArHMIARGAGKIINIASVQSALARPGiAPYTA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 576796343 239 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL-----ADP 276
Cdd:PRK07523 162 TKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLnaalvADP 204
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 86-267 6.41e-09

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 56.17  E-value: 6.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekG 165
Cdd:PRK08265   3 GLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFG--R 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LWGLINNAGV---PGVLAP-TDWLTLEDyrepieVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGGG-YTPSK 240
Cdd:PRK08265  81 VDILVNLACTyldDGLASSrADWLAALD------VNLVSAAMLAQAAHPHLARGGGAIVNFTSISAKFAQTGRWlYPASK 154

                        170       180
                 ....*....|....*....|....*..
gi 576796343 241 YAVEGFNDSLRRDMKAFGVHVSCIEPG 267
Cdd:PRK08265 155 AAIRQLTRSMAMDLAPDGIRVNSVSPG 181
PRK08628 PRK08628
SDR family oxidoreductase;
86-266 7.77e-09

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 55.74  E-value: 7.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGfhVIAACLTESgstALKAETSERLR-------TVLLDVTDPENVKRTaqwVK 158
Cdd:PRK08628   4 NLKDKVVIVTGGASGIGAAISLRLAEEG--AIPVIFGRS---APDDEFAEELRalqpraeFVQVDLTDDAQCRDA---VE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 159 NQVGEKG-LWGLINNAGVpgvlapTDWLTLE----DYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSvggRLAIVG 233
Cdd:PRK08628  76 QTVAKFGrIDGLVNNAGV------NDGVGLEagreAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISS---KTALTG 146

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 576796343 234 ----GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEP 266
Cdd:PRK08628 147 qggtSGYAAAKGAQLALTREWAVALAKDGVRVNAVIP 183
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
82-272 8.87e-09

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 55.68  E-value: 8.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  82 LKIEDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE-TSERLRTVLLDVTDPENVKRTAQWVKNQ 160
Cdd:PRK12481   1 MQLFDLNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEAPETQAQVEaLGRKFHFITADLIQQKDIDSIVSQAVEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 161 VGEKGLwgLINNAGVpgvLAPTDWLTL--EDYREPIEVNLFGLISVTLNMLPLVKKAQ--GRVINVSSVggrLAIVGG-- 234
Cdd:PRK12481  81 MGHIDI--LINNAGI---IRRQDLLEFgnKDWDDVININQKTVFFLSQAVAKQFVKQGngGKIINIASM---LSFQGGir 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 576796343 235 --GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTN 272
Cdd:PRK12481 153 vpSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATD 192
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 86-278 1.05e-08

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 55.50  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLT-ESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQV 161
Cdd:PRK08936   4 DLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSdEEEANDVAEEIKKaggEAIAVKGDVTVESDVVNLIQTAVKEF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 162 GEKGLWglINNAGVPgVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKK--AQGRVINVSSVGGRL---AIVggGY 236
Cdd:PRK08936  84 GTLDVM--INNAGIE-NAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEhdIKGNIINMSSVHEQIpwpLFV--HY 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 576796343 237 TPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKT-----NLADPVK 278
Cdd:PRK08936 159 AASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTpinaeKFADPKQ 205
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 94-298 1.50e-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: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRT----VLLDVTDPENVKRTAQWVKNQVGEKGLwgL 169
Cdd:cd05373    4 VVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGsakaVPTDARDEDEVIALFDLIEEEIGPLEV--L 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 170 INNAG--VPGVLAPTdwlTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVI---NVSSVGGR--LAivggGYTPSKY 241
Cdd:cd05373   82 VYNAGanVWFPILET---TPRVFEKVWEMAAFGGFLAAREAAKrMLARGRGTIIftgATASLRGRagFA----AFAGAKF 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576796343 242 AVEGFNDSLRRDMKAFGVHV------SCIEPGLFKTNLADPVKVIEKKlaiwEQLSPD-IKQQY 298
Cdd:cd05373  155 ALRALAQSMARELGPKGIHVahviidGGIDTDFIRERFPKRDERKEED----GILDPDaIAEAY 214
PRK07985 PRK07985
SDR family oxidoreductase;
76-273 1.56e-08

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 55.39  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  76 WTRKGKLKieditDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTA--LKAETSERLRTVLL---DVTDPENV 150
Cdd:PRK07985  41 YVGSGRLK-----DRKALVTGGDSGIGRAAAIAYAREGADVAISYLPVEEEDAqdVKKIIEECGRKAVLlpgDLSDEKFA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 151 KRTAQWVKNQVGEKGLWGLInnAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAqGRVINVSSVggrla 230
Cdd:PRK07985 116 RSLVHEAHKALGGLDIMALV--AGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPKG-ASIITTSSI----- 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 576796343 231 ivgGGYTPS---------KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:PRK07985 188 ---QAYQPSphlldyaatKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTAL 236
PRK07074 PRK07074
SDR family oxidoreductase;
88-271 1.98e-08

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 54.78  E-value: 1.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  88 TDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETS-ERLRTVLLDVTDPENVKRTaqwVKNQVGEKGL 166
Cdd:PRK07074   1 TKRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGdARFVPVACDLTDAASLAAA---LANAAAERGP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 167 WG-LINNAGVPGVLAPTDwLTLEDYREPIEVNLFG-LISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGGGYTPSKYAVE 244
Cdd:PRK07074  78 VDvLVANAGAARAASLHD-TTPASWRADNALNLEAaYLCVEAVLEGMLKRSRGAVVNIGSVNGMAALGHPAYSAAKAGLI 156

                        170       180
                 ....*....|....*....|....*..
gi 576796343 245 GFNDSLRRDMKAFGVHVSCIEPGLFKT 271
Cdd:PRK07074 157 HYTKLLAVEYGRFGIRANAVAPGTVKT 183
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 82-272 2.02e-08

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 54.86  E-value: 2.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  82 LKIeDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESG----STALKAETSERLRTVLLDVTDPENVKRTAQWV 157
Cdd:PRK08339   2 LKI-DLSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENlkkaREKIKSESNVDVSYIVADLTKREDLERTVKEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 158 KNqVGEKGLWGLINNAGVPGVLAPtdwLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVGGGY 236
Cdd:PRK08339  81 KN-IGEPDIFFFSTGGPKPGYFME---MSMEDWEGAVKLLLYPAVYLTRALVPaMERKGFGRIIYSTSVAIKEPIPNIAL 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 576796343 237 TP-SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTN 272
Cdd:PRK08339 157 SNvVRISMAGLVRTLAKELGPKGITVNGIMPGIIRTD 193
PRK06947 PRK06947
SDR family oxidoreductase;
90-273 4.26e-08

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 53.66  E-value: 4.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHViaaCLTESGSTALKAETSE-------RLRTVLLDVTDPENVKRTAQWVKNQVG 162
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSV---GINYARDAAAAEETADavraaggRACVVAGDVANEADVIAMFDAVQSAFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 ekGLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ----GRVINVSSVGGRLaivgGG--- 235
Cdd:PRK06947  80 --RLDALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRggrgGAIVNVSSIASRL----GSpne 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 576796343 236 ---YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:PRK06947 154 yvdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEI 194
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
88-272 4.73e-08

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 53.57  E-value: 4.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  88 TDKYIFITGCDSGFGNLAARTFDKKGFHvIAACLTESGSTALkaETSERLR-------TVLLDVTDPENVKRTAQWVKNQ 160
Cdd:PRK08063   3 SGKVALVTGSSRGIGKAIALRLAEEGYD-IAVNYARSRKAAE--ETAEEIEalgrkalAVKANVGDVEKIKEMFAQIDEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 161 VGekGLWGLINNAGvPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIvgGGYTP- 238
Cdd:PRK08063  80 FG--RLDVFVNNAA-SGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGgGKIISLSSLGSIRYL--ENYTTv 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 576796343 239 --SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTN 272
Cdd:PRK08063 155 gvSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTD 190
PRK12743 PRK12743
SDR family oxidoreductase;
94-275 4.85e-08

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 53.50  E-value: 4.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKGFHV-IAACLTESGSTALKAETSERLR---TVLLDVTDPEnvkRTAQWVKNQVGEKG-LWG 168
Cdd:PRK12743   7 VTASDSGIGKACALLLAQQGFDIgITWHSDEEGAKETAEEVRSHGVraeIRQLDLSDLP---EGAQALDKLIQRLGrIDV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAGVpGVLAPTDWLTLEDYREPIEVNLFGlisVTL-------NMlplVKKAQ-GRVINVSSVGGRLAIVGGG-YTPS 239
Cdd:PRK12743  84 LVNNAGA-MTKAPFLDMDFDEWRKIFTVDVDG---AFLcsqiaarHM---VKQGQgGRIINITSVHEHTPLPGASaYTAA 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 576796343 240 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLAD 275
Cdd:PRK12743 157 KHALGGLTKAMALELVEHGILVNAVAPGAIATPMNG 192
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 86-278 5.73e-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: 53.24  E-value: 5.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSErLRTVLLDVTDPENVKRTaqwvknqVGEKG 165
Cdd:cd05351    4 DFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPG-IEPVCVDLSDWDATEEA-------LGSVG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LW-GLINNAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ--GRVINVSSVGGRLAIVG-GGYTPSKY 241
Cdd:cd05351   76 PVdLLVNNAAV-AILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvpGSIVNVSSQASQRALTNhTVYCSTKA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 576796343 242 AVEGFNDSLRRDMKAFGVHVSCIEPGLFKT-----NLADPVK 278
Cdd:cd05351  155 ALDMLTKVMALELGPHKIRVNSVNPTVVMTdmgrdNWSDPEK 196
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
92-269 1.17e-07

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 52.67  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  92 IFITGCdSGF-GNLAARTFDKKGFHVIAACLTESGSTALKAetSERLRTVLLDVTDPENVKRTAQWVKnqvgekglwGLI 170
Cdd:COG0451    2 ILVTGG-AGFiGSHLARRLLARGHEVVGLDRSPPGAANLAA--LPGVEFVRGDLRDPEALAAALAGVD---------AVV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 171 NNAGVPGVlaptdwlTLEDYREPIEVNLFGlisvTLNMLPLVKKAQ-GRVINVSSVggrlAIVGGGYTP----------- 238
Cdd:COG0451   70 HLAAPAGV-------GEEDPDETLEVNVEG----TLNLLEAARAAGvKRFVYASSS----SVYGDGEGPidedtplrpvs 134

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 576796343 239 ----SKYAVEGFndsLRRDMKAFGVHVSCIEPGLF 269
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 ...
 90-273 1.27e-07

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 52.49  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVkNQVGEkgLWGL 169
Cdd:cd08951    8 KRIFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSSLAETRKLADQV-NAIGR--FDAV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 170 INNAGV---PGVLAPTdwltlEDYREPIEVNLFGLISVTlnmlPLVKKAQgRVINVSS--------------VGGRLAIV 232
Cdd:cd08951   85 IHNAGIlsgPNRKTPD-----TGIPAMVAVNVLAPYVLT----ALIRRPK-RLIYLSSgmhrggnaslddidWFNRGEND 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 576796343 233 GGGYTPSKYAVEGFNDSLRRDMKafGVHVSCIEPGLFKTNL 273
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; ...
 89-312 1.49e-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: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGStALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKG-LW 167
Cdd:cd08937    4 GKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVH-EVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGrVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 168 GLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRlAIVGGGYTPSKYAVEGF 246
Cdd:cd08937   83 VLINNVGGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPhMLERQQGVIVNVSSIATR-GIYRIPYSAAKGGVNAL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576796343 247 NDSLRRDMKAFGVHVSCIEPGLFKTnladPVKVIEKKLAIWEQLSPDIKQQYGEGYIEKSLDKLKG 312
Cdd:cd08937  162 TASLAFEHARDGIRVNAVAPGGTEA----PPRKIPRNAAPMSEQEKVWYQRIVDQTLDSSLMGRYG 223
PRK07775 PRK07775
SDR family oxidoreductase;
94-287 1.74e-07

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 52.06  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKGFHV------------IAACLTESGSTALkaetserlrTVLLDVTDPENVKRTAQWVKNQV 161
Cdd:PRK07775  15 VAGASSGIGAATAIELAAAGFPValgarrvekceeLVDKIRADGGEAV---------AFPLDVTDPDSVKSFVAQAEEAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 162 GEKGLwgLINNAG--VPGVLAPTDwltLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSS-VGGRLAIVGGGYT 237
Cdd:PRK07775  86 GEIEV--LVSGAGdtYFGKLHEIS---TEQFESQVQIHLVGANRLATAVLPgMIERRRGDLIFVGSdVALRQRPHMGAYG 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 576796343 238 PSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLA--DPVKVIEKKLAIW 287
Cdd:PRK07775 161 AAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGMGwsLPAEVIGPMLEDW 212
PRK07023 PRK07023
SDR family oxidoreductase;
94-273 2.36e-07

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 51.17  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKGFHVIaaCLTESGSTALKAETSERLRTVLLDVTDPEnvkRTAQWVKNQVGEKGLWG----- 168
Cdd:PRK07023   6 VTGHSRGLGAALAEQLLQPGIAVL--GVARSRHPSLAAAAGERLAEVELDLSDAA---AAAAWLAGDLLAAFVDGasrvl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKK-AQGRVINVSSVGGRLAIVG-GGYTPSKYAVEGF 246
Cdd:PRK07023  81 LINNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDaAERRILHISSGAARNAYAGwSVYCATKAALDHH 160

                        170       180
                 ....*....|....*....|....*..
gi 576796343 247 NDSLRRDMKAfGVHVSCIEPGLFKTNL 273
Cdd:PRK07023 161 ARAVALDANR-ALRIVSLAPGVVDTGM 186
PRK06953 PRK06953
SDR family oxidoreductase;
90-273 2.77e-07

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 50.84  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSErlrTVLLDVTDPENVKRTAqWvknQVGEKGLWGL 169
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQALGAE---ALALDVADPASVAGLA-W---KLDGEALDAA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 170 INNAGVPGV-LAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGGG----YTPSKYAVe 244
Cdd:PRK06953  75 VYVAGVYGPrTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSRMGSIGDATGTtgwlYRASKAAL- 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 576796343 245 gfNDSLR---RDMKafgvHVSCI--EPGLFKTNL 273
Cdd:PRK06953 154 --NDALRaasLQAR----HATCIalHPGWVRTDM 181
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 83-272 3.09e-07

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 51.44  E-value: 3.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  83 KIEDITDKYIFITGCDSGFGNLAARTFDKKGFHV------------IAACLTESGSTALKAETserlrtvllDVTDPENV 150
Cdd:PRK08277   4 NLFSLKGKVAVITGGGGVLGGAMAKELARAGAKVaildrnqekaeaVVAEIKAAGGEALAVKA---------DVLDKESL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 151 KRTAQWVKNQVGEKGLwgLINNAG--VPGvlAPTDW--------------LTLEDYREPIEVNLFGlisvtlNMLP---- 210
Cdd:PRK08277  75 EQARQQILEDFGPCDI--LINGAGgnHPK--ATTDNefhelieptktffdLDEEGFEFVFDLNLLG------TLLPtqvf 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 211 ---LVKKAQGRVINVSSVGG-----RLAivggGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTN 272
Cdd:PRK08277 145 akdMVGRKGGNIINISSMNAftpltKVP----AYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTE 210
PRK07035 PRK07035
SDR family oxidoreductase;
86-274 3.57e-07

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 50.78  E-value: 3.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVG 162
Cdd:PRK07035   5 DLTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAaggKAEALACHIGEMEQIDALFAHIRERHG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 EkgLWGLINNAGV-P--GVLAPTDwltLEDYREPIEVNLFGLISVTLNMLPLVKK-AQGRVINVSSVGG-RLAIVGGGYT 237
Cdd:PRK07035  85 R--LDILVNNAAAnPyfGHILDTD---LGAFQKTVDVNIRGYFFMSVEAGKLMKEqGGGSIVNVASVNGvSPGDFQGIYS 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 576796343 238 PSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLA 274
Cdd:PRK07035 160 ITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFA 196
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
86-272 4.31e-07

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 50.64  E-value: 4.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERlrtVLLDVT-DPENVKRTAQWVKNQVGEK 164
Cdd:PRK08993   7 SLEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEPTETIEQVTALGR---RFLSLTaDLRKIDGIPALLERAVAEF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 GLWG-LINNAGVPGVLAPTDWlTLEDYREPIEVNlfglISVTLNMLPLVKK---AQG---RVINVSSVggrLAIVGG--- 234
Cdd:PRK08993  84 GHIDiLVNNAGLIRREDAIEF-SEKDWDDVMNLN----IKSVFFMSQAAAKhfiAQGnggKIINIASM---LSFQGGirv 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 576796343 235 -GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTN 272
Cdd:PRK08993 156 pSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATN 194
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 94-305 5.51e-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: 50.54  E-value: 5.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALK----AETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLwgL 169
Cdd:cd05322    7 VIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVAdeinAEYGEKAYGFGADATNEQSVIALSKGVDEIFKRVDL--L 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 170 INNAGVpGVLAPTDWLTLEDYREPIEVNLFG--LISVTLNMLPLVKKAQGRVINVSSVGGRlaiVGG----GYTPSKYAV 243
Cdd:cd05322   85 VYSAGI-AKSAKITDFELGDFDRSLQVNLVGyfLCAREFSKLMIRDGIQGRIIQINSKSGK---VGSkhnsGYSAAKFGG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576796343 244 EGFNDSLRRDMKAFGVHVSCIEPG-LFKTNLADP-VKVIEKKLAIweqlSPDIKQQYgegYIEK 305
Cdd:cd05322  161 VGLTQSLALDLAEHGITVNSLMLGnLLKSPMFQSlLPQYAKKLGI----KESEVEQY---YIDK 217
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 93-277 6.83e-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: 6.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  93 FITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVllDVTDPENVKRTAQwvknQVGEKGLWGLINN 172
Cdd:cd11730    2 LILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALARPA--DVAAELEVWALAQ----ELGPLDLLVYAAG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 173 AGVPGVLAPTdwlTLEDYREPIEVNLFGLISVTLNMLPLVkKAQGRVINVSSVGGRLAIVG-GGYTPSKYAVEGFNDSLR 251
Cdd:cd11730   76 AILGKPLART---KPAAWRRILDANLTGAALVLKHALALL-AAGARLVFLGAYPELVMLPGlSAYAAAKAALEAYVEVAR 151

                        170       180
                 ....*....|....*....|....*.
gi 576796343 252 RDMKafGVHVSCIEPGLFKTNLADPV 277
Cdd:cd11730  152 KEVR--GLRLTLVRPPAVDTGLWAPP 175
PRK07577 PRK07577
SDR family oxidoreductase;
88-273 6.89e-07

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 49.73  E-value: 6.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  88 TDKYIFITGCDSGFGNLAARTFDKKGFHVIaacltesgstALKAETSERLRTVLL--DVTDPEnvkRTAQWVKNQVGEKG 165
Cdd:PRK07577   2 SSRTVLVTGATKGIGLALSLRLANLGHQVI----------GIARSAIDDFPGELFacDLADIE---QTAATLAQINEIHP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LWGLINNAGV--PGVLAPTDWLTLEDYrepIEVNLFGLISVTLNMLPLVKKA-QGRVINVSSvggrLAIVGG----GYTP 238
Cdd:PRK07577  69 VDAIVNNVGIalPQPLGKIDLAALQDV---YDLNVRAAVQVTQAFLEGMKLReQGRIVNICS----RAIFGAldrtSYSA 141

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 576796343 239 SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:PRK07577 142 AKSALVGCTRTWALELAEYGITVNAVAPGPIETEL 176
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 94-229 7.63e-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: 7.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAET-----SERLRTVLLDVTDPenvKRTAQWVKNQVGE-KGLW 167
Cdd:cd09808    6 ITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIetesgNQNIFLHIVDMSDP---KQVWEFVEEFKEEgKKLH 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 576796343 168 GLINNAgvpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQG-RVINVSSvGGRL 229
Cdd:cd09808   83 VLINNA---GCMVNKRELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDpRVITVSS-GGML 141
PRK05867 PRK05867
SDR family oxidoreductase;
82-292 9.29e-07

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 49.65  E-value: 9.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  82 LKIEDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAAClteSGSTALKAETSE------RLRTVLLDVTDPENVKRTAQ 155
Cdd:PRK05867   2 LDLFDLHGKRALITGASTGIGKRVALAYVEAGAQVAIAA---RHLDALEKLADEigtsggKVVPVCCDVSQHQQVTSMLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 156 WVKNQVGekGLWGLINNAGVPGVLAPTDwLTLEDYREPIEVNLFGL-ISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG 233
Cdd:PRK05867  79 QVTAELG--GIDIAVCNAGIITVTPMLD-MPLEEFQRLQNTNVTGVfLTAQAAAKAMVKQGQgGVIINTASMSGHIINVP 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 576796343 234 ---GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPvkvIEKKLAIWEQLSP 292
Cdd:PRK05867 156 qqvSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEP---YTEYQPLWEPKIP 214
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 89-277 9.46e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 49.80  E-value: 9.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHV---------IAACLTEsgSTALKAETSerLRTVLLDVTDPENVKRTAQWVKN 159
Cdd:PRK05875   7 DRTYLVTGGGSGIGKGVAAGLVAAGAAVmivgrnpdkLAAAAEE--IEALKGAGA--VRYEPADVTDEDQVARAVDAATA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 160 QVGekGLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNML-PLVKKAQGRVINVSSVGG----RLAivgG 234
Cdd:PRK05875  83 WHG--RLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAArELVRGGGGSFVGISSIAAsnthRWF---G 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 576796343 235 GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPV 277
Cdd:PRK05875 158 AYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPI 200
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 87-274 1.32e-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: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  87 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTES----GSTALKAETSERLRTVLlDVTDPENVKRTAQWVKNQVG 162
Cdd:cd08936    8 LANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQnvdrAVATLQGEGLSVTGTVC-HVGKAEDRERLVATAVNLHG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 163 ekGLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLP-LVKKAQGRVINVSSVGGRLAIVG-GGYTPSK 240
Cdd:cd08936   87 --GVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPeMEKRGGGSVVIVSSVAAFHPFPGlGPYNVSK 164

                        170       180       190
                 ....*....|....*....|....*....|....
gi 576796343 241 YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLA 274
Cdd:cd08936  165 TALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFS 198
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 94-285 1.59e-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: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERL----RTVLLDVTDPENVKRTAQWVKNQVGekGLWGL 169
Cdd:cd05337    6 VTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAgrraIYFQADIGELSDHEALLDQAWEDFG--RLDCL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 170 INNAGVpGVLAPTDWL--TLEDYREPIEVNLFGLI----SVTLNMLPLVKKAQG---RVINVSSVGGRLAIVG-GGYTPS 239
Cdd:cd05337   84 VNNAGI-AVRPRGDLLdlTEDSFDRLIAINLRGPFfltqAVARRMVEQPDRFDGphrSIIFVTSINAYLVSPNrGEYCIS 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 576796343 240 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVK-VIEKKLA 285
Cdd:cd05337  163 KAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKeKYDELIA 209
PRK07814 PRK07814
SDR family oxidoreductase;
87-267 1.96e-06

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 48.62  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  87 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLR---TVLLDVTDPENvkrTAQWVKNQVGE 163
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRrahVVAADLAHPEA---TAGLAGQAVEA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 164 KG-LWGLINNAG--VPGVLAPTdwlTLEDYREPIEVNLFGLISVTLNMLPLVKK--AQGRVINVSSVGGRLAIVG-GGYT 237
Cdd:PRK07814  85 FGrLDIVVNNVGgtMPNPLLST---STKDLADAFTFNVATAHALTVAAVPLMLEhsGGGSVINISSTMGRLAGRGfAAYG 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 576796343 238 PSKYAVEGFNDSLRRDMkAFGVHVSCIEPG 267
Cdd:PRK07814 162 TAKAALAHYTRLAALDL-CPRIRVNAIAPG 190
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 90-292 2.23e-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: 48.35  E-value: 2.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGC--DSGFGNLAARTFDKKGFHVIAACLTESGS---TALKAETSERLRTVLLDVTDPENVKRTAqwvkNQVGEK 164
Cdd:cd05372    2 KRILITGIanDRSIAWGIAKALHEAGAELAFTYQPEALRkrvEKLAERLGESALVLPCDVSNDEEIKELF----AEVKKD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 glWGLINnagvpGVL-----APTDWL-------TLEDYREPIEVNLFGLISVTLNMLPLVKKaQGRVINVSSVGGRLAIV 232
Cdd:cd05372   78 --WGKLD-----GLVhsiafAPKVQLkgpfldtSRKGFLKALDISAYSLVSLAKAALPIMNP-GGSIVTLSYLGSERVVP 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 576796343 233 G-GGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSP 292
Cdd:cd05372  150 GyNVMGVAKAALESSVRYLAYELGRKGIRVNAISAGPIKTLAASGITGFDKMLEYSEQRAP 210
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 84-274 3.11e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 48.48  E-value: 3.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  84 IEDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACL-TESGSTALKAETSER----LRTVLLDVTDPENVKRTAQWVK 158
Cdd:PRK06197  11 IPDQSGRVAVVTGANTGLGYETAAALAAKGAHVVLAVRnLDKGKAAAARITAATpgadVTLQELDLTSLASVRAAADALR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 159 NQVGEKGLwgLINNAgvpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQG-RVINVSSVGGRL--AI---- 231
Cdd:PRK06197  91 AAYPRIDL--LINNA---GVMYTPKQTTADGFELQFGTNHLGHFALTGLLLDRLLPVPGsRVVTVSSGGHRIraAIhfdd 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 576796343 232 --------VGGGYTPSKYAVEGFNDSLRRDMKAFGVHVSCI--EPGLFKTNLA 274
Cdd:PRK06197 166 lqwerrynRVAAYGQSKLANLLFTYELQRRLAAAGATTIAVaaHPGVSNTELA 218
PRK06196 PRK06196
oxidoreductase; Provisional
 86-287 3.88e-06

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 48.14  E-value: 3.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVI-AACLTESGSTALKAetSERLRTVLLDVTDPENVKRTAqwvkNQVGEK 164
Cdd:PRK06196  23 DLSGKTAIVTGGYSGLGLETTRALAQAGAHVIvPARRPDVAREALAG--IDGVEVVMLDLADLESVRAFA----ERFLDS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 165 G--LWGLINNAgvpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQG-RVINVSSVGGRLAIV-------GG 234
Cdd:PRK06196  97 GrrIDILINNA---GVMACPETRVGDGWEAQFATNHLGHFALVNLLWPALAAGAGaRVVALSSAGHRRSPIrwddphfTR 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 576796343 235 GYTP------SKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIW 287
Cdd:PRK06196 174 GYDKwlaygqSKTANALFAVHLDKLGKDQGVRAFSVHPGGILTPLQRHLPREEQVALGW 232
PRK06123 PRK06123
SDR family oxidoreductase;
89-273 4.15e-06

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 47.47  E-value: 4.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHV-------------IAACLTESGSTALkaetserlrTVLLDVTDPENVKRTAQ 155
Cdd:PRK06123   2 RKVMIITGASRGIGAATALLAAERGYAVclnylrnrdaaeaVVQAIRRQGGEAL---------AVAADVADEADVLRLFE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 156 WVKNQVGEkgLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLI----SVTLNMLPLVKKAQGRVINVSSVGGRLAI 231
Cdd:PRK06123  73 AVDRELGR--LDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSFlcarEAVKRMSTRHGGRGGAIVNVSSMAARLGS 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 576796343 232 VGG--GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
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 ...
 89-267 5.24e-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: 5.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTA-----LKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGE 163
Cdd:cd09809    1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAavsriLEEWHKARVEAMTLDLASLRSVQRFAEAFKAKNSP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 164 kgLWGLINNAGVPGVlaptDW-LTLEDYREPIEVNLFGLISVTLNMLPLVKK-AQGRVINVSSVG----------GRLAI 231
Cdd:cd09809   81 --LHVLVCNAAVFAL----PWtLTEDGLETTFQVNHLGHFYLVQLLEDVLRRsAPARVIVVSSEShrftdlpdscGNLDF 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 576796343 232 VGGGYTPSKY-AVEGFNDS----------LRRDMKAFGVHVSCIEPG 267
Cdd:cd09809  155 SLLSPPKKKYwSMLAYNRAklcnilfsneLHRRLSPRGITSNSLHPG 201
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 87-276 5.54e-06

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 47.26  E-value: 5.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  87 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGL 166
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAFG--KL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 167 WGLINNAGVPGVLAP---TDWLTLED-YREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAivGGG---YTPS 239
Cdd:PRK06200  82 DCFVGNAGIWDYNTSlvdIPAETLDTaFDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLSNSSFYP--GGGgplYTAS 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 576796343 240 KYAVEGFNDSLRRDMkAFGVHVSCIEPGLFKTNLADP 276
Cdd:PRK06200 160 KHAVVGLVRQLAYEL-APKIRVNGVAPGGTVTDLRGP 195
PRK09730 PRK09730
SDR family oxidoreductase;
94-273 5.76e-06

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 47.15  E-value: 5.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKGFHV-------IAAC------LTESG--STALKAetserlrtvllDVTDPENVKRTAQWVK 158
Cdd:PRK09730   6 VTGGSRGIGRATALLLAQEGYTVavnyqqnLHAAqevvnlITQAGgkAFVLQA-----------DISDENQVVAMFTAID 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 159 NQVGEkgLWGLINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLIsvtLNMLPLVKKAQ-------GRVINVSSVGGRLAI 231
Cdd:PRK09730  75 QHDEP--LAALVNNAGILFTQCTVENLTAERINRVLSTNVTGYF---LCCREAVKRMAlkhggsgGAIVNVSSAASRLGA 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 576796343 232 VGG--GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:PRK09730 150 PGEyvDYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEM 193
PRK12742 PRK12742
SDR family oxidoreductase;
86-273 7.25e-06

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 46.67  E-value: 7.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVI----------AACLTESGSTALKAETSERLRTV-LLDVTDPENVkrta 154
Cdd:PRK12742   3 AFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRftyagskdaaERLAQETGATAVQTDSADRDAVIdVVRKSGALDI---- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 155 qwvknqvgekglwgLINNAGVpgvLAPTDWLTL--EDYREPIEVNL----FGLISVTLNMlplvkKAQGRVINVSSVGG- 227
Cdd:PRK12742  79 --------------LVVNAGI---AVFGDALELdaDDIDRLFKINIhapyHASVEAARQM-----PEGGRIIIIGSVNGd 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 576796343 228 RLAIVGG-GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:PRK12742 137 RMPVAGMaAYAASKSALQGMARGLARDFGPRGITINVVQPGPIDTDA 183
PRK06128 PRK06128
SDR family oxidoreductase;
94-273 7.61e-06

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 47.16  E-value: 7.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKA----ETSERLRTVLL-DVTDPENVKRTAQWVKNQVGekGLWG 168
Cdd:PRK06128  60 ITGADSGIGRATAIAFAREGADIALNYLPEEEQDAAEVvqliQAEGRKAVALPgDLKDEAFCRQLVERAVKELG--GLDI 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVkKAQGRVINVSSVggrlaivgGGYTPS--------- 239
Cdd:PRK06128 138 LVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHL-PPGASIINTGSI--------QSYQPSptlldyast 208

                        170       180       190
                 ....*....|....*....|....*....|....
gi 576796343 240 KYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:PRK06128 209 KAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPL 242
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 94-246 8.57e-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: 8.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKG-FHVIAACLTESGSTALKAET---SERLRTVLLDVTDPENVKrtaQWVKN-QVGEKGLWG 168
Cdd:cd09810    6 ITGASSGLGLAAAKALARRGeWHVVMACRDFLKAEQAAQEVgmpKDSYSVLHCDLASLDSVR---QFVDNfRRTGRPLDA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAGVPGVLAPTDWLTLEDYREPIEVNLFG---LISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGGGyTPSKY---A 242
Cdd:cd09810   83 LVCNAAVYLPTAKEPRFTADGFELTVGVNHLGhflLTNLLLEDLQRSENASPRIVIVGSITHNPNTLAGN-VPPRAtlgD 161


                 ....
gi 576796343 243 VEGF 246
Cdd:cd09810  162 LEGL 165
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 94-271 2.59e-05

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 45.98  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKGFHVIAACLTESGsTALkAETSERLR--TVLLDVTDPENVKRTAQWVKNQVGekGLWGLIN 171
Cdd:PRK08261 215 VTGAARGIGAAIAEVLARDGAHVVCLDVPAAG-EAL-AAVANRVGgtALALDITAPDAPARIAEHLAERHG--GLDIVVH 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 172 NAGVP--GVLAPTDwltlEDY-REPIEVNLFGLISVTLNML-PLVKKAQGRVINVSSVGGrlaIVGG----GYTPSKYAV 243
Cdd:PRK08261 291 NAGITrdKTLANMD----EARwDSVLAVNLLAPLRITEALLaAGALGDGGRIVGVSSISG---IAGNrgqtNYAASKAGV 363

                        170       180
                 ....*....|....*....|....*...
gi 576796343 244 EGFNDSLRRDMKAFGVHVSCIEPGLFKT 271
Cdd:PRK08261 364 IGLVQALAPLLAERGITINAVAPGFIET 391
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 90-267 3.28e-05

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 45.05  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSE---RLRTVLLDVTDPENVKRTAQWVKNQVGEkgL 166
Cdd:PRK07677   2 KVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQfpgQVLTVQMDVRNPEDVQKMVEQIDEKFGR--I 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 167 WGLINNAGvPGVLAPTDWLTLEDYREPIEVNLFG--LISVTLNMLPLVKKAQGRVINVSSVGGRLAivGGGYTPSKYAVE 244
Cdd:PRK07677  80 DALINNAA-GNFICPAEDLSVNGWNSVIDIVLNGtfYCSQAVGKYWIEKGIKGNIINMVATYAWDA--GPGVIHSAAAKA 156

                        170       180
                 ....*....|....*....|....*...
gi 576796343 245 GFNdSLRRDM-----KAFGVHVSCIEPG 267
Cdd:PRK07677 157 GVL-AMTRTLavewgRKYGIRVNAIAPG 183
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 93-278 5.09e-05

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 44.18  E-value: 5.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  93 FITGCDSGFGNLAARTFDKKGFHVIaacLTESGSTALKAETSERLRT-------VLLDVTDPENVKRTAQWVKNQVGekG 165
Cdd:PRK12745   6 LVTGGRRGIGLGIARALAAAGFDLA---INDRPDDEELAATQQELRAlgvevifFPADVADLSAHEAMLDAAQAAWG--R 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 166 LWGLINNAGVpGVLAPTDWL--TLEDYREPIEVNLFGLI----SVTLNMLPLVKKAQGR---VINVSSV-GGRLAIVGGG 235
Cdd:PRK12745  81 IDCLVNNAGV-GVKVRGDLLdlTPESFDRVLAINLRGPFfltqAVAKRMLAQPEPEELPhrsIVFVSSVnAIMVSPNRGE 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 576796343 236 YTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVK 278
Cdd:PRK12745 160 YCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPVT 202
PLN00015 PLN00015
protochlorophyllide reductase
 94-238 5.43e-05

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 44.70  E-value: 5.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  94 ITGCDSGFGNLAARTFDKKG-FHVIAACLT-ESGSTALK-AETSERLRTVL-LDVTDPENVKrtaQWVKN-QVGEKGLWG 168
Cdd:PLN00015   2 ITGASSGLGLATAKALAETGkWHVVMACRDfLKAERAAKsAGMPKDSYTVMhLDLASLDSVR---QFVDNfRRSGRPLDV 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 576796343 169 LINNAGVPGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKA---QGRVINVSSVGGRLAIVGGGYTP 238
Cdd:PLN00015  79 LVCNAAVYLPTAKEPTFTADGFELSVGTNHLGHFLLSRLLLDDLKKSdypSKRLIIVGSITGNTNTLAGNVPP 151
PRK06500 PRK06500
SDR family oxidoreductase;
89-297 6.33e-05

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 44.18  E-value: 6.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  89 DKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEkgLWG 168
Cdd:PRK06500   6 GKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAAQKALAQALAEAFGR--LDA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAGVpgvlapTDWLTLEDYREP-----IEVNLFGLISVTLNMLPLVKKAQGRVINvSSVGGRLAIVGGG-YTPSKYA 242
Cdd:PRK06500  84 VFINAGV------AKFAPLEDWDEAmfdrsFNTNVKGPYFLIQALLPLLANPASIVLN-GSINAHIGMPNSSvYAASKAA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 576796343 243 VEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLaiwEQLSPDIKQQ 297
Cdd:PRK06500 157 LLSLAKTLSGELLPRGIRVNAVSPGPVQTPLYGKLGLPEATL---DAVAAQIQAL 208
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 157-277 6.96e-05

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 43.91  E-value: 6.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 157 VKNQVGEKGLWGLINNAGV-PGvlAPTDWLTLEDYREPIEVNL---FGLISVTLNMLplvkKAQGRVINVSSVGGRLAIV 232
Cdd:PRK12747  80 LQNRTGSTKFDILINNAGIgPG--AFIEETTEQFFDRMVSVNAkapFFIIQQALSRL----RDNSRIINISSAATRISLP 153

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 576796343 233 GG-GYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTN-----LADPV 277
Cdd:PRK12747 154 DFiAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDmnaelLSDPM 204
PRK08177 PRK08177
SDR family oxidoreductase;
90-273 6.98e-05

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 43.87  E-value: 6.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTvlLDVTDPENVKRTAQWVKNQVGEKglwgL 169
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIEK--LDMNDPASLDQLLQRLQGQRFDL----L 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 170 INNAGVPGVLA-PTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGGG----YTPSKYAVE 244
Cdd:PRK08177  76 FVNAGISGPAHqSAADATAAEIGQLFLTNAIAPIRLARRLLGQVRPGQGVLAFMSSQLGSVELPDGGemplYKASKAALN 155

                        170       180
                 ....*....|....*....|....*....
gi 576796343 245 GFNDSLRRDMKAFGVHVSCIEPGLFKTNL 273
Cdd:PRK08177 156 SMTRSFVAELGEPTLTVLSMHPGWVKTDM 184
PRK09186 PRK09186
flagellin modification protein A; Provisional
 87-267 1.28e-04

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 43.05  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  87 ITDKYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAE-----TSERLRTVLLDVTDPENVKRTAQWVKNQV 161
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESlgkefKSKKLSLVELDITDQESLEEFLSKSAEKY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 162 GEkgLWGLINNAgVPgvlAPTDW------LTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLA---- 230
Cdd:PRK09186  82 GK--IDGAVNCA-YP---RNKDYgkkffdVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGgGNLVNISSIYGVVApkfe 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 576796343 231 ---------------IVGGGYTPSKYAVEGFNDSlrrdmkafGVHVSCIEPG 267
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 ...
 169-267 1.53e-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: 42.69  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAGV--PGVLAPTdwlTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ-GRVINVSSVGGRLAIVG-GGYTPSKYAVE 244
Cdd:cd05353   92 LVNNAGIlrDRSFAKM---SEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKfGRIINTSSAAGLYGNFGqANYSAAKLGLL 168

                         90       100
                 ....*....|....*....|...
gi 576796343 245 GFNDSLRRDMKAFGVHVSCIEPG 267
Cdd:cd05353  169 GLSNTLAIEGAKYNITCNTIAPA 191
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
92-231 3.19e-04

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


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 42.29  E-value: 3.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  92 IFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSER---LRTVLLDVTDPENVKRTAqwvkNQVGEKG--L 166
Cdd:COG5748    9 VIITGASSGVGLYAAKALADRGWHVIMACRDLEKAEAAAQELGIPpdsYTIIHIDLASLESVRRFV----ADFRALGrpL 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 576796343 167 WGLINNAGV--PGVLAPTdwLTLEDYREPIEVNLFGLISVTLNMLPLVKK---AQGRVINVSSV-------GGRLAI 231
Cdd:COG5748   85 DALVCNAAVyyPLLKEPL--RSPDGYELSVATNHLGHFLLCNLLLEDLKKspaSDPRLVILGTVtanpkelGGKIPI 159
PRK07831 PRK07831
SDR family oxidoreductase;
99-268 3.40e-04

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 41.94  E-value: 3.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  99 SGFGNLAARTFDKKGFHVI-----AACLTESgSTALKAETSE-RLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGLINN 172
Cdd:PRK07831  28 TGIGSATARRALEEGARVVisdihERRLGET-ADELAAELGLgRVEAVVCDVTSEAQVDALIDAAVERLG--RLDVLVNN 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 173 AGVPGVLAPTDwLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQ--GRVINVSSVGGRLAIVGGG-YTPSKYAVEGFNDS 249
Cdd:PRK07831 105 AGLGGQTPVVD-MTDDEWSRVLDVTLTGTFRATRAALRYMRARGhgGVIVNNASVLGWRAQHGQAhYAAAKAGVMALTRC 183

                        170
                 ....*....|....*....
gi 576796343 250 LRRDMKAFGVHVSCIEPGL 268
Cdd:PRK07831 184 SALEAAEYGVRINAVAPSI 202
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 92-273 5.29e-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: 40.64  E-value: 5.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  92 IFITGCDSGFGNLAARTFDKKGFHVIAAcltesGSTAlkaetserlRTVLLDVTDPENVKRTAQwvknQVGEkgLWGLIN 171
Cdd:cd11731    1 IIVIGATGTIGLAVAQLLSAHGHEVITA-----GRSS---------GDYQVDITDEASIKALFE----KVGH--FDAIVS 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 172 NAGVpGVLAPTDWLTLEDYREPIEVNLFGLISVTLNMLPLVkkAQGRVINVSS---------VGGRLAIVGGgytpskyA 242
Cdd:cd11731   61 TAGD-AEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYL--NDGGSITLTSgilaqrpipGGAAAATVNG-------A 130

                        170       180       190
                 ....*....|....*....|....*....|.
gi 576796343 243 VEGFNDSLRRDMKAfGVHVSCIEPGLFKTNL 273
Cdd:cd11731  131 LEGFVRAAAIELPR-GIRINAVSPGVVEESL 160
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 86-275 6.77e-04

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 40.86  E-value: 6.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  86 DITDKYIFITGCDSGFGNLAARTFDKKGFHVI--AACLTESGSTALK--AETSERLRTVLLDVTDPENVKRTAQWVKNQV 161
Cdd:PRK06077   3 SLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVvnAKKRAEEMNETLKmvKENGGEGIGVLADVSTREGCETLAKATIDRY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 162 GekGLWGLINNAGVpGVLAPtdWLTLED--YREPIEVNLFGLISVTlNMLPLVKKAQGRVINVSSVGGRLAIVG-GGYTP 238
Cdd:PRK06077  83 G--VADILVNNAGL-GLFSP--FLNVDDklIDKHISTDFKSVIYCS-QELAKEMREGGAIVNIASVAGIRPAYGlSIYGA 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 576796343 239 SKYAVEGFNDSLRRDMkAFGVHVSCIEPGLFKTNLAD 275
Cdd:PRK06077 157 MKAAVINLTKYLALEL-APKIRVNAIAPGFVKTKLGE 192
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
 92-224 7.19e-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: 7.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  92 IFITGcDSGF-GNLAARTFDKKGFHVIAA-CLTESGSTA----LKA-ETSERLRTVLLDV---TDPENVKRTAQWVknqv 161
Cdd:cd05258    3 VLITG-GAGFiGSNLARFFLKQGWEVIGFdNLMRRGSFGnlawLKAnREDGGVRFVHGDIrnrNDLEDLFEDIDLI---- 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 576796343 162 gekglwglINNAGVPGVLAptdwlTLEDYREPIEVNLFGlisvTLNMLPLVKKA--QGRVINVSS 224
Cdd:cd05258   78 --------IHTAAQPSVTT-----SASSPRLDFETNALG----TLNVLEAARQHapNAPFIFTST 125
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 90-224 8.47e-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: 40.64  E-value: 8.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343  90 KYIFITGCDSGFGNLAARTFDKKGFHVIAACLTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGekGLWGL 169
Cdd:cd09761    2 KVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLG--RIDVL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 576796343 170 INNAGV--PGVLAPtdwLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSS 224
Cdd:cd09761   80 VNNAARgsKGILSS---LLLEEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIAS 133
PRK05854 PRK05854
SDR family oxidoreductase;
169-273 1.13e-03

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 40.43  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576796343 169 LINNAgvpGVLAPTDWLTLEDYRE-PIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIV-------------GG 234
Cdd:PRK05854  97 LINNA---GVMTPPERQTTADGFElQFGTNHLGHFALTAHLLPLLRAGRARVTSQSSIAARRGAInwddlnwersyagMR 173

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 576796343 235 GYTPSKYAVEGFNDSLRRDMKA--FGVHVSCIEPGLFKTNL 273
Cdd:PRK05854 174 AYSQSKIAVGLFALELDRRSRAagWGITSNLAHPGVAPTNL 214
 
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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