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Conserved domains on  [gi|1720364755|ref|XP_030101559|]
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dehydrogenase/reductase SDR family member 11 isoform X1 [Mus musculus]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 1-177 5.90e-120

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


The actual alignment was detected with superfamily member cd05343:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 250  Bit Score: 339.10  E-value: 5.90e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIDDGHIININSMCGHRVPP 80
Cdd:cd05343    74 MFSAIRTQHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVDDGHIININSMSGHRVPP 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIHFYSATKYAVTALTEGLRQELLEAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCLRPEDVAEAVIYV 160
Cdd:cd05343   154 VSVFHFYAATKHAVTALTEGLRQELREAKTHIRATSISPGLVETEFAFKLHDNDPEKAAATYESIPCLKPEDVANAVLYV 233

                         170
                  ....*....|....*..
gi 1720364755 161 LSTPPHVQVGDIQMRPT 177
Cdd:cd05343   234 LSTPPHVQIHDILLRPT 250
 
Name Accession Description Interval E-value
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 1-177 5.90e-120

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: 339.10  E-value: 5.90e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIDDGHIININSMCGHRVPP 80
Cdd:cd05343    74 MFSAIRTQHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVDDGHIININSMSGHRVPP 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIHFYSATKYAVTALTEGLRQELLEAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCLRPEDVAEAVIYV 160
Cdd:cd05343   154 VSVFHFYAATKHAVTALTEGLRQELREAKTHIRATSISPGLVETEFAFKLHDNDPEKAAATYESIPCLKPEDVANAVLYV 233

                         170
                  ....*....|....*..
gi 1720364755 161 LSTPPHVQVGDIQMRPT 177
Cdd:cd05343   234 LSTPPHVQIHDILLRPT 250
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-177 2.41e-58

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 182.30  E-value: 2.41e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPP 80
Cdd:COG4221    69 AVAAAVAEFGRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARG--SGHIVNISSIAGLRPYP 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCLRPEDVAEAVIYV 160
Cdd:COG4221   147 GGAV--YAATKAAVRGLSESLRAEL--RPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPLTPEDVAEAVLFA 222

                         170
                  ....*....|....*..
gi 1720364755 161 LSTPPHVQVGDIQMRPT 177
Cdd:COG4221   223 LTQPAHVNVNELVLRPT 239
SDR_TniO_fam NF038213
SDR family oxidoreductase;
13-179 7.14e-30

SDR family oxidoreductase;


Pssm-ID: 439515  Cd Length: 249  Bit Score: 109.74  E-value: 7.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  13 DICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIDD-----GHIININSMCGHRVPPQSVihFY 87
Cdd:NF038213   82 DIVVVNAGRGLGGSVLDSDLSQWEELLRINVLGAARLMRAAAQYMVESQKADfprqaADIVVIGSVVGRNISPFSP--VY 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  88 SATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFafklhdkdpgEAAATY----------EHIKCLRPEDVAEAV 157
Cdd:NF038213  160 GATKFAVHSLAEGLRREV--CPKGVRVTLVEPGIVVSGF----------QEVAGYdmelfakfeeEFGPLLEGEDVAEAI 227

                         170       180
                  ....*....|....*....|..
gi 1720364755 158 IYVLSTPPHVQVGDIQMRPTEQ 179
Cdd:NF038213  228 HFVVTQPPHVHINDIMIRPTRQ 249
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-167 5.49e-29

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 107.08  E-value: 5.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPq 81
Cdd:PRK07666   75 IEQLKNELGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQ--SGDIINISSTAGQKGAA- 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  82 sVIHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAF--KLHDKDPGeaaatyehiKCLRPEDVAEAVIY 159
Cdd:PRK07666  152 -VTSAYSASKFGVLGLTESLMQEV--RKHNIRVTALTPSTVATDMAVdlGLTDGNPD---------KVMQPEDLAEFIVA 219


                  ....*...
gi 1720364755 160 VLSTPPHV 167
Cdd:PRK07666  220 QLKLNKRT 227
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 1-127 2.14e-28

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 104.23  E-value: 2.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHrvpp 80
Cdd:pfam00106  67 LVEQAVERLGRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGS--GGRIVNISSVAGL---- 140

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1720364755  81 QSVIHF--YSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFA 127
Cdd:pfam00106 141 VPYPGGsaYSASKAAVIGFTRSLALEL--APHGIRVNAVAPGGVDTDMT 187
 
Name Accession Description Interval E-value
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 1-177 5.90e-120

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: 339.10  E-value: 5.90e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIDDGHIININSMCGHRVPP 80
Cdd:cd05343    74 MFSAIRTQHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVDDGHIININSMSGHRVPP 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIHFYSATKYAVTALTEGLRQELLEAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCLRPEDVAEAVIYV 160
Cdd:cd05343   154 VSVFHFYAATKHAVTALTEGLRQELREAKTHIRATSISPGLVETEFAFKLHDNDPEKAAATYESIPCLKPEDVANAVLYV 233

                         170
                  ....*....|....*..
gi 1720364755 161 LSTPPHVQVGDIQMRPT 177
Cdd:cd05343   234 LSTPPHVQIHDILLRPT 250
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-177 2.41e-58

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 182.30  E-value: 2.41e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPP 80
Cdd:COG4221    69 AVAAAVAEFGRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARG--SGHIVNISSIAGLRPYP 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCLRPEDVAEAVIYV 160
Cdd:COG4221   147 GGAV--YAATKAAVRGLSESLRAEL--RPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPLTPEDVAEAVLFA 222

                         170
                  ....*....|....*..
gi 1720364755 161 LSTPPHVQVGDIQMRPT 177
Cdd:COG4221   223 LTQPAHVNVNELVLRPT 239
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 1-164 8.93e-45

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: 147.82  E-value: 8.93e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPP 80
Cdd:cd05233    64 LVEEALEEFGRLDILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQG--GGRIVNISSVAGLRPLP 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDP-GEAAATYEHIKCLRPEDVAEAVIY 159
Cdd:cd05233   142 GQAA--YAASKAALEGLTRSLALEL--APYGIRVNAVAPGLVDTPMLAKLGPEEAeKELAAAIPLGRLGTPEEVAEAVVF 217


                  ....*
gi 1720364755 160 VLSTP 164
Cdd:cd05233   218 LASDE 222
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 12-179 1.50e-43

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: 145.12  E-value: 1.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMAR-PDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQSVIhfYSAT 90
Cdd:cd05346    79 IDILVNNAGLALgLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARN--QGHIINLGSIAGRYPYAGGNV--YCAT 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  91 KYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCLRPEDVAEAVIYVLSTPPHVQVG 170
Cdd:cd05346   155 KAAVRQFSLNLRKDL--IGTGIRVTNIEPGLVETEFSLVRFHGDKEKADKVYEGVEPLTPEDIAETILWVASRPAHVNIN 232


                  ....*....
gi 1720364755 171 DIQMRPTEQ 179
Cdd:cd05346   233 DIEIMPVNQ 241
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 11-179 4.30e-39

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: 133.43  E-value: 4.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIddGHIININSMCGHRVPPQSVIhfYSAT 90
Cdd:cd08934    80 RLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNK--GTIVNISSVAGRVAVRNSAV--YNAT 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  91 KYAVTALTEGLRQELLEAQthIRATCISPGLVETQFAFklHDKDPGEAAATYEHIKCLRP---EDVAEAVIYVLSTPPHV 167
Cdd:cd08934   156 KFGVNAFSEGLRQEVTERG--VRVVVIEPGTVDTELRD--HITHTITKEAYEERISTIRKlqaEDIAAAVRYAVTAPHHV 231

                         170
                  ....*....|..
gi 1720364755 168 QVGDIQMRPTEQ 179
Cdd:cd08934   232 TVNEILIRPTDQ 243
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-170 8.44e-39

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 132.69  E-value: 8.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPP 80
Cdd:COG0300    72 LAEAVLARFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARG--RGRIVNVSSVAGLRGLP 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAfklhdkdpgEAAATYEHIKCLRPEDVAEAVIYV 160
Cdd:COG0300   150 GMAA--YAASKAALEGFSESLRAEL--APTGVRVTAVCPGPVDTPFT---------ARAGAPAGRPLLSPEEVARAILRA 216

                         170
                  ....*....|.
gi 1720364755 161 LSTP-PHVQVG 170
Cdd:COG0300   217 LERGrAEVYVG 227
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-162 4.38e-34

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: 120.66  E-value: 4.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERniDDGHIININSMCGHRVPP 80
Cdd:COG1028    73 LVAAAVAAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRER--GGGRIVNISSIAGLRGSP 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDpgEAAATYEHIKCLR----PEDVAEA 156
Cdd:COG1028   151 GQAA--YAASKAAVVGLTRSLALEL--APRGIRVNAVAPGPIDTPMTRALLGAE--EVREALAARIPLGrlgtPEEVAAA 224


                  ....*.
gi 1720364755 157 VIYVLS 162
Cdd:COG1028   225 VLFLAS 230
SDR_TniO_fam NF038213
SDR family oxidoreductase;
13-179 7.14e-30

SDR family oxidoreductase;


Pssm-ID: 439515  Cd Length: 249  Bit Score: 109.74  E-value: 7.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  13 DICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIDD-----GHIININSMCGHRVPPQSVihFY 87
Cdd:NF038213   82 DIVVVNAGRGLGGSVLDSDLSQWEELLRINVLGAARLMRAAAQYMVESQKADfprqaADIVVIGSVVGRNISPFSP--VY 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  88 SATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFafklhdkdpgEAAATY----------EHIKCLRPEDVAEAV 157
Cdd:NF038213  160 GATKFAVHSLAEGLRREV--CPKGVRVTLVEPGIVVSGF----------QEVAGYdmelfakfeeEFGPLLEGEDVAEAI 227

                         170       180
                  ....*....|....*....|..
gi 1720364755 158 IYVLSTPPHVQVGDIQMRPTEQ 179
Cdd:NF038213  228 HFVVTQPPHVHINDIMIRPTRQ 249
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-167 5.49e-29

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 107.08  E-value: 5.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPq 81
Cdd:PRK07666   75 IEQLKNELGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQ--SGDIINISSTAGQKGAA- 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  82 sVIHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAF--KLHDKDPGeaaatyehiKCLRPEDVAEAVIY 159
Cdd:PRK07666  152 -VTSAYSASKFGVLGLTESLMQEV--RKHNIRVTALTPSTVATDMAVdlGLTDGNPD---------KVMQPEDLAEFIVA 219


                  ....*...
gi 1720364755 160 VLSTPPHV 167
Cdd:PRK07666  220 QLKLNKRT 227
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 2-170 5.58e-29

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: 107.32  E-value: 5.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHR-VPP 80
Cdd:cd05374    65 VKEVIERFGRIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQG--SGRIVNVSSVAGLVpTPF 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPG------------EAAATYEHIKCL 148
Cdd:cd05374   143 LGP---YCASKAALEALSESLRLEL--APFGIKVTIIEPGPVRTGFADNAAGSALEdpeispyaperkEIKENAAGVGSN 217

                         170       180
                  ....*....|....*....|....*..
gi 1720364755 149 --RPEDVAEAVIYVL---STPPHVQVG 170
Cdd:cd05374   218 pgDPEKVADVIVKALtseSPPLRYFLG 244
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 1-127 2.14e-28

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 104.23  E-value: 2.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHrvpp 80
Cdd:pfam00106  67 LVEQAVERLGRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGS--GGRIVNISSVAGL---- 140

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1720364755  81 QSVIHF--YSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFA 127
Cdd:pfam00106 141 VPYPGGsaYSASKAAVIGFTRSLALEL--APHGIRVNAVAPGGVDTDMT 187
PRK08219 PRK08219
SDR family oxidoreductase;
2-177 3.58e-27

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 101.93  E-value: 3.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERnidDGHIININSMCGHRVPPQ 81
Cdd:PRK08219   62 IAAAVEQLGRLDVLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAA---HGHVVFINSGAGLRANPG 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  82 SVIhfYSATKYAVTALTEGLRQEllEAqTHIRATCISPGLVETQFAFKLHDKDPGEaaatYEHIKCLRPEDVAEAVIYVL 161
Cdd:PRK08219  139 WGS--YAASKFALRALADALREE--EP-GNVRVTSVHPGRTDTDMQRGLVAQEGGE----YDPERYLRPETVAKAVRFAV 209

                         170
                  ....*....|....*.
gi 1720364755 162 STPPHVQVGDIQMRPT 177
Cdd:PRK08219  210 DAPPDAHITEVVVRPR 225
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 12-179 4.35e-27

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 102.53  E-value: 4.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMA---RPDTLlsGSTSGWKDMFNVNVLALSICTREAYQSMKERNIddGHIININSMCGHRvpPQSVIHFYS 88
Cdd:PRK10538   75 IDVLVNNAGLAlglEPAHK--ASVEDWETMIDTNNKGLVYMTRAVLPGMVERNH--GHIINIGSTAGSW--PYAGGNVYG 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  89 ATKYAVTALTEGLRQELleAQTHIRATCISPGLVE-TQFAFKLHDKDPGEAAATYEHIKCLRPEDVAEAVIYVLSTPPHV 167
Cdd:PRK10538  149 ATKAFVRQFSLNLRTDL--HGTAVRVTDIEPGLVGgTEFSNVRFKGDDGKAEKTYQNTVALTPEDVSEAVWWVATLPAHV 226

                         170
                  ....*....|..
gi 1720364755 168 QVGDIQMRPTEQ 179
Cdd:PRK10538  227 NINTLEMMPVTQ 238
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 4-164 5.52e-27

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 101.67  E-value: 5.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQSV 83
Cdd:cd08932    66 ALRDRFGRIDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAG--SGRVVFLNSLSGKRVLAGNA 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  84 IhfYSATKYAVTALTEGLRQEllEAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEhikclrPEDVAEAVIYVLST 163
Cdd:cd08932   144 G--YSASKFALRALAHALRQE--GWDHGVRVSAVCPGFVDTPMAQGLTLVGAFPPEEMIQ------PKDIANLVRMVIEL 213


                  .
gi 1720364755 164 P 164
Cdd:cd08932   214 P 214
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 3-158 8.32e-25

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: 96.50  E-value: 8.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   3 SAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQS 82
Cdd:cd05332    73 EEALKLFGGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERS--QGSIVVVSSIAGKIGVPFR 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364755  83 VIhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQF---AFKLHDKDPGEAAATYEHIkcLRPEDVAEAVI 158
Cdd:cd05332   151 TA--YAASKHALQGFFDSLRAEL--SEPNISVTVVCPGLIDTNIamnALSGDGSMSAKMDDTTANG--MSPEECALEIL 223
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 1-162 1.08e-23

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


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 93.26  E-value: 1.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDT--LLSGSTSGWKDMFNVNVLALSICTREAYQSMKERniddGHIININSMCGHRV 78
Cdd:pfam13561  61 LVAAAVEKFGRLDILVNNAGFAPKLKgpFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEG----GSIVNLSSIGAERV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  79 PPQSVIhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEH-IKCL-RPEDVAEA 156
Cdd:pfam13561 137 VPNYNA--YGAAKAALEALTRYLAVEL--GPRGIRVNAISPGPIKTLAASGIPGFDELLAAAEARApLGRLgTPEEVANA 212


                  ....*.
gi 1720364755 157 VIYVLS 162
Cdd:pfam13561 213 AAFLAS 218
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 4-167 5.23e-23

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: 91.53  E-value: 5.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQSV 83
Cdd:cd05339    69 KIKKEVGDVTILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERN--HGHIVTIASVAGLISPAGLA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  84 IhfYSATKYAVTALTEGLRQELLEAQ-THIRATCISPGLVETQFaFKlHDKDPGEAaatyeHIKCLRPEDVAEAVI-YVL 161
Cdd:cd05339   147 D--YCASKAAAVGFHESLRLELKAYGkPGIKTTLVCPYFINTGM-FQ-GVKTPRPL-----LAPILEPEYVAEKIVrAIL 217


                  ....*.
gi 1720364755 162 STPPHV 167
Cdd:cd05339   218 TNQQML 223
FabG-like PRK07231
SDR family oxidoreductase;
4-162 3.19e-22

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 89.50  E-value: 3.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMA-RPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPqs 82
Cdd:PRK07231   74 AALERFGSVDILVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEG--GGAIVNVASTAGLRPRP-- 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  83 VIHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEA----AATYEHIKCLRPEDVAEAVI 158
Cdd:PRK07231  150 GLGWYNASKGAVITLTKALAAEL--GPDKIRVNAVAPVVVETGLLEAFMGEPTPENrakfLATIPLGRLGTPEDIANAAL 227


                  ....
gi 1720364755 159 YVLS 162
Cdd:PRK07231  228 FLAS 231
PRK07326 PRK07326
SDR family oxidoreductase;
11-177 7.51e-22

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 88.53  E-value: 7.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAG---MARPDTLlsgSTSGWKDMFNVNVLALSICTREAYQSMKERNiddGHIININSMCGHRVppqsvihF- 86
Cdd:PRK07326   82 GLDVLIANAGvghFAPVEEL---TPEEWRLVIDTNLTGAFYTIKAAVPALKRGG---GYIINISSLAGTNF-------Fa 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  87 ----YSATKYAVTALTEGLRQELLEAQthIRATCISPGLVETQFAfklhDKDPGEAAATYehikcLRPEDVAEAVIYVLS 162
Cdd:PRK07326  149 ggaaYNASKFGLVGFSEAAMLDLRQYG--IKVSTIMPGSVATHFN----GHTPSEKDAWK-----IQPEDIAQLVLDLLK 217

                         170
                  ....*....|....*
gi 1720364755 163 TPPHVQVGDIQMRPT 177
Cdd:PRK07326  218 MPPRTLPSKIEVRPS 232
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 1-162 1.21e-21

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 87.94  E-value: 1.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIddGHIININSMCGH-RVP 79
Cdd:PRK05557   73 AVDEAKAEFGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRS--GRIINISSVVGLmGNP 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  80 PQSVihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPgEAAATYEHIKCL-RPEDVAEAVI 158
Cdd:PRK05557  151 GQAN---YAASKAGVIGFTKSLAREL--ASRGITVNAVAPGFIETDMTDALPEDVK-EAILAQIPLGRLgQPEEIASAVA 224


                  ....
gi 1720364755 159 YVLS 162
Cdd:PRK05557  225 FLAS 228
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 4-169 3.73e-21

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 87.30  E-value: 3.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGhRVPP--Q 81
Cdd:PRK07825   71 AVEADLGPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRG--RGHVVNVASLAG-KIPVpgM 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  82 SVihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFafklhdkdpgeAAATYEH--IKCLRPEDVAEAVIY 159
Cdd:PRK07825  148 AT---YCASKHAVVGFTDAARLEL--RGTGVHVSVVLPSFVNTEL-----------IAGTGGAkgFKNVEPEDVAAAIVG 211

                         170
                  ....*....|.
gi 1720364755 160 VLSTP-PHVQV 169
Cdd:PRK07825  212 TVAKPrPEVRV 222
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 2-177 4.33e-21

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: 86.41  E-value: 4.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGhrVPPQ 81
Cdd:cd08929    65 VDAMEEAFGGLDALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRG--GGTIVNVGSLAG--KNAF 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  82 SVIHFYSATKYAVTALTEGLRQELLEAqtHIRATCISPGLVETQFAfklhdkdpGEAAATYEHIKclrPEDVAEAVIYVL 161
Cdd:cd08929   141 KGGAAYNASKFGLLGLSEAAMLDLREA--NIRVVNVMPGSVDTGFA--------GSPEGQAWKLA---PEDVAQAVLFAL 207

                         170
                  ....*....|....*.
gi 1720364755 162 STPPHVQVGDIQMRPT 177
Cdd:cd08929   208 EMPARALVSRIELRPT 223
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 2-164 9.96e-21

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 85.43  E-value: 9.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARPDTLLSGS--TSGWKDMFNVNVLALSICTREAYQSMKERNIDD-GHIININSMCGHR- 77
Cdd:cd05323    68 FKKAIEKFGRVDILINNAGILDEKSYLFAGklPPPWEKTIDVNLTGVINTTYLALHYMDKNKGGKgGVIVNIGSVAGLYp 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  78 VPPQSVihfYSATKYAVTALTEGLRqELLEAQTHIRATCISPGLVETQFafkLHDkDPGEAAATYEHIKCLRPEDVAEAV 157
Cdd:cd05323   148 APQFPV---YSASKHGVVGFTRSLA-DLLEYKTGVRVNAICPGFTNTPL---LPD-LVAKEAEMLPSAPTQSPEVVAKAI 219


                  ....*..
gi 1720364755 158 IYVLSTP 164
Cdd:cd05323   220 VYLIEDD 226
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-162 2.16e-20

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 84.83  E-value: 2.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCG----- 75
Cdd:PRK05653   72 LIEAAVEAFGALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKAR--YGRIVNISSVSGvtgnp 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  76 HRVPpqsvihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCLRPEDVAE 155
Cdd:PRK05653  150 GQTN-------YSAAKAGVIGFTKALALEL--ASRGITVNAVAPGFIDTDMTEGLPEEVKAEILKEIPLGRLGQPEEVAN 220


                  ....*..
gi 1720364755 156 AVIYVLS 162
Cdd:PRK05653  221 AVAFLAS 227
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-162 2.53e-20

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 84.51  E-value: 2.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMA-------RPDTLlsgstsgWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSM 73
Cdd:PRK05565   73 LVEQIVEKFGKIDILVNNAGISnfglvtdMTDEE-------WDRVIDVNLTGVMLLTRYALPYMIKRK--SGVIVNISSI 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  74 CGHRVPPQSVIhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFA--FKLHDKDpgeaAATYEHIKCL--R 149
Cdd:PRK05565  144 WGLIGASCEVL--YSASKGAVNAFTKALAKEL--APSGIRVNAVAPGAIDTEMWssFSEEDKE----GLAEEIPLGRlgK 215

                         170
                  ....*....|...
gi 1720364755 150 PEDVAEAVIYVLS 162
Cdd:PRK05565  216 PEEIAKVVLFLAS 228
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 1-162 9.60e-20

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: 83.20  E-value: 9.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIdDGHIININSMcgHRVPP 80
Cdd:cd05358    71 LFQSAIKEFGTLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKI-KGKIINMSSV--HEKIP 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQF---AFklhdKDPGEAAATYEHIKCLR---PEDVA 154
Cdd:cd05358   148 WPGHVNYAASKGGVKMMTKTLAQEY--APKGIRVNAIAPGAINTPInaeAW----DDPEQRADLLSLIPMGRigePEEIA 221


                  ....*...
gi 1720364755 155 EAVIYVLS 162
Cdd:cd05358   222 AAAAWLAS 229
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 1-162 9.99e-20

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: 82.98  E-value: 9.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERniDDGHIININSMCGHR-VP 79
Cdd:cd05333    67 LVEKVEAEFGPVDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKR--RSGRIINISSVVGLIgNP 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  80 PQSVihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLhDKDPGEAAATYEHIKCL-RPEDVAEAVI 158
Cdd:cd05333   145 GQAN---YAASKAGVIGFTKSLAKEL--ASRGITVNAVAPGFIDTDMTDAL-PEKVKEKILKQIPLGRLgTPEEVANAVA 218


                  ....
gi 1720364755 159 YVLS 162
Cdd:cd05333   219 FLAS 222
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 1-162 1.88e-19

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: 82.32  E-value: 1.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKerniDDGHIININS-MCGHRVP 79
Cdd:cd05362    71 LFDAAEKAFGGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLR----DGGRIINISSsLTAAYTP 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  80 PQSVihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCL-RPEDVAEAVI 158
Cdd:cd05362   147 NYGA---YAGSKAAVEAFTRVLAKEL--GGRGITVNAVAPGPVDTDMFYAGKTEEAVEGYAKMSPLGRLgEPEDIAPVVA 221


                  ....
gi 1720364755 159 YVLS 162
Cdd:cd05362   222 FLAS 225
PRK07454 PRK07454
SDR family oxidoreductase;
12-176 1.90e-19

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 82.31  E-value: 1.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQsvIHFYSATK 91
Cdd:PRK07454   84 PDVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARG--GGLIINVSSIAARNAFPQ--WGAYCVSK 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  92 YAVTALTEGLRQEllEAQTHIRATCISPGLVETqfafKLHDKDpgEAAATYEHIKCLRPEDVAEAVIYVLSTPPHVQVGD 171
Cdd:PRK07454  160 AALAAFTKCLAEE--ERSHGIRVCTITLGAVNT----PLWDTE--TVQADFDRSAMLSPEQVAQTILHLAQLPPSAVIED 231


                  ....*
gi 1720364755 172 IQMRP 176
Cdd:PRK07454  232 LTLMP 236
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
1-162 3.40e-19

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 81.69  E-value: 3.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNA--GMARPdtLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRV 78
Cdd:PRK08063   72 MFAQIDEEFGRLDVFVNNAasGVLRP--AMELEESHWDWTMNINAKALLFCAQEAAKLMEKVG--GGKIISLSSLGSIRY 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  79 PPQSVihFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQfAFKlH----DKDPGEAAATYEHIKCLRPEDVA 154
Cdd:PRK08063  148 LENYT--TVGVSKAALEALTRYLAVEL--APKGIAVNAVSGGAVDTD-ALK-HfpnrEELLEDARAKTPAGRMVEPEDVA 221


                  ....*...
gi 1720364755 155 EAVIYVLS 162
Cdd:PRK08063  222 NAVLFLCS 229
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 1-162 1.86e-18

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: 79.71  E-value: 1.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERniDDGHIININSMCGHRVPP 80
Cdd:cd05347    72 AVEAIEEDFGKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQ--GHGKIINICSLLSELGGP 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QsvIHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDkDPGEAAATYEHIKCLR---PEDVAEAV 157
Cdd:cd05347   150 P--VPAYAASKGGVAGLTKALATEW--ARHGIQVNAIAPGYFATEMTEAVVA-DPEFNDDILKRIPAGRwgqPEDLVGAA 224


                  ....*
gi 1720364755 158 IYVLS 162
Cdd:cd05347   225 VFLAS 229
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 2-162 2.43e-18

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


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 79.34  E-value: 2.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNiDDGHIININSMCGHR-VPP 80
Cdd:cd05366    71 IDQAVEKFGSFDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLG-HGGKIINASSIAGVQgFPN 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAF-------KLHDKDPGEAAATYEHIKCLR---- 149
Cdd:cd05366   150 LGA---YSASKFAVRGLTQTAAQEL--APKGITVNAYAPGIVKTEMWDyideevgEIAGKPEGEGFAEFSSSIPLGrlse 224

                         170
                  ....*....|...
gi 1720364755 150 PEDVAEAVIYVLS 162
Cdd:cd05366   225 PEDVAGLVSFLAS 237
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 1-162 3.26e-18

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 78.86  E-value: 3.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMkeRNIDDGHIININSMcghrVPP 80
Cdd:PRK12939   74 FFDAAAAALGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHL--RDSGRGRIVNLASD----TAL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIHF--YSATKYAVTALTEGLRQELLEAQthIRATCISPGLVETQFAFKlhdkdpGEAAATYEHIKCLR-------PE 151
Cdd:PRK12939  148 WGAPKLgaYVASKGAVIGMTRSLARELGGRG--ITVNAIAPGLTATEATAY------VPADERHAYYLKGRalerlqvPD 219

                         170
                  ....*....|.
gi 1720364755 152 DVAEAVIYVLS 162
Cdd:PRK12939  220 DVAGAVLFLLS 230
PRK06947 PRK06947
SDR family oxidoreductase;
1-162 9.12e-18

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 77.92  E-value: 9.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSG-STSGWKDMFNVNVLALSICTREAYQSM-KERNIDDGHIININSMCGHRV 78
Cdd:PRK06947   70 MFDAVQSAFGRLDALVNNAGIVAPSMPLADmDAARLRRMFDTNVLGAYLCAREAARRLsTDRGGRGGAIVNVSSIASRLG 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  79 PPQSVIHfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQfafkLHDK--DPGEAA---ATYEHIKCLRPEDV 153
Cdd:PRK06947  150 SPNEYVD-YAGSKGAVDTLTLGLAKEL--GPHGVRVNAVRPGLIETE----IHASggQPGRAArlgAQTPLGRAGEADEV 222


                  ....*....
gi 1720364755 154 AEAVIYVLS 162
Cdd:PRK06947  223 AETIVWLLS 231
PRK12826 PRK12826
SDR family oxidoreductase;
1-162 1.06e-17

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 77.65  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPP 80
Cdd:PRK12826   73 AVAAGVEDFGRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAG--GGRIVLTSSVAGPRVGY 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIHfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCL-RPEDVAEAVIY 159
Cdd:PRK12826  151 PGLAH-YAASKAGLVGFTRALALEL--AARNITVNSVHPGGVDTPMAGNLGDAQWAEAIAAAIPLGRLgEPEDIAAAVLF 227


                  ...
gi 1720364755 160 VLS 162
Cdd:PRK12826  228 LAS 230
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-164 2.11e-17

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 77.07  E-value: 2.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKErnidDGHIININSMCGHRvpPQSV 83
Cdd:PRK06077   77 ATIDRYGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMRE----GGAIVNIASVAGIR--PAYG 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  84 IHFYSATKYAVTALTEGLRQELleAQtHIRATCISPGLVETQFA---FKLHDKDPGEAAATYEHI-KCLRPEDVAEAVIY 159
Cdd:PRK06077  151 LSIYGAMKAAVINLTKYLALEL--AP-KIRVNAIAPGFVKTKLGeslFKVLGMSEKEFAEKFTLMgKILDPEEVAEFVAA 227


                  ....*
gi 1720364755 160 VLSTP 164
Cdd:PRK06077  228 ILKIE 232
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 2-162 2.78e-17

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: 76.60  E-value: 2.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRV--P 79
Cdd:cd05352    77 FKQIQKDFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQG--KGSLIITASMSGTIVnrP 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  80 PQSVihFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVET-QFAFklHDKDPGEAAATYehIKCLR---PEDVAE 155
Cdd:cd05352   155 QPQA--AYNASKAAVIHLAKSLAVEW--AKYFIRVNSISPGYIDTdLTDF--VDKELRKKWESY--IPLKRialPEELVG 226


                  ....*..
gi 1720364755 156 AVIYVLS 162
Cdd:cd05352   227 AYLYLAS 233
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 3-163 1.49e-16

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: 74.44  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   3 SAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTrEAYQSMKERNIDDGH---IININSMCGHRVP 79
Cdd:cd08942    74 ARVAERSDRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLT-QALLPLLRAAATAENparVINIGSIAGIVVS 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  80 PQSViHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQF-AFKLHDKDPGEA-AATYEHIKCLRPEDVAEAV 157
Cdd:cd08942   153 GLEN-YSYGASKAAVHQLTRKLAKEL--AGEHITVNAIAPGRFPSKMtAFLLNDPAALEAeEKSIPLGRWGRPEDMAGLA 229


                  ....*.
gi 1720364755 158 IYVLST 163
Cdd:cd08942   230 IMLASR 235
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 8-172 1.71e-16

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


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 74.43  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   8 QHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRvpPQSVIHFY 87
Cdd:cd05331    65 EHGPIDALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRR--TGAIVTVASNAAHV--PRISMAAY 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  88 SATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEA------AATYE-HI---KCLRPEDVAEAV 157
Cdd:cd05331   141 GASKAALASLSKCLGLEL--APYGVRCNVVSPGSTDTAMQRTLWHDEDGAAqviagvPEQFRlGIplgKIAQPADIANAV 218

                         170
                  ....*....|....*.
gi 1720364755 158 IYVLS-TPPHVQVGDI 172
Cdd:cd05331   219 LFLASdQAGHITMHDL 234
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 1-158 2.30e-16

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: 73.83  E-value: 2.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGhRVPp 80
Cdd:cd08939    72 AFAQAVEKGGPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQR--PGHIVFVSSQAA-LVG- 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 qsVIHF--YSATKYAVTALTEGLRQELLEAQTHIraTCISPGLVET-QFAFKLHDKdPGEAAATYEHIKCLRPEDVAEAV 157
Cdd:cd08939   148 --IYGYsaYCPSKFALRGLAESLRQELKPYNIRV--SVVYPPDTDTpGFEEENKTK-PEETKAIEGSSGPITPEEAARII 222


                  .
gi 1720364755 158 I 158
Cdd:cd08939   223 V 223
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
12-163 2.35e-16

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 74.17  E-value: 2.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTRE-AYQSMKERNidDGHIININSMC----GHRVPPqsvihf 86
Cdd:PRK12481   84 IDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAvAKQFVKQGN--GGKIINIASMLsfqgGIRVPS------ 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  87 YSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHdKDPGEAAATYEHIKCLR---PEDVAEAVIYVLST 163
Cdd:PRK12481  156 YTASKSAVMGLTRALATEL--SQYNINVNAIAPGYMATDNTAALR-ADTARNEAILERIPASRwgtPDDLAGPAIFLSSS 232
PRK06123 PRK06123
SDR family oxidoreductase;
1-162 2.76e-16

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 73.66  E-value: 2.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSG-WKDMFNVNVLALSICTREAYQSMKERNID-DGHIININSMCGHRV 78
Cdd:PRK06123   70 LFEAVDRELGRLDALVNNAGILEAQMRLEQMDAArLTRIFATNVVGSFLCAREAVKRMSTRHGGrGGAIVNVSSMAARLG 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  79 PPQSVIHfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQfafkLHDK--DPGEAAATYEHIKCLR---PEDV 153
Cdd:PRK06123  150 SPGEYID-YAASKGAIDTMTIGLAKEV--AAEGIRVNAVRPGVIYTE----IHASggEPGRVDRVKAGIPMGRggtAEEV 222


                  ....*....
gi 1720364755 154 AEAVIYVLS 162
Cdd:PRK06123  223 ARAILWLLS 231
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-161 2.86e-16

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 73.84  E-value: 2.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARpDTLLSGSTSG----------WKDMFNVNVLALSICTREAYQSMKERNiDDGHIINI 70
Cdd:PRK08217   72 TFAQIAEDFGQLNGLINNAGILR-DGLLVKAKDGkvtskmsleqFQSVIDVNLTGVFLCGREAAAKMIESG-SKGVIINI 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  71 NSMCGHRVPPQSVihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAfklhDKDPGEAAATYEHIKCLR- 149
Cdd:PRK08217  150 SSIARAGNMGQTN---YSASKAGVAAMTVTWAKEL--ARYGIRVAAIAPGVIETEMT----AAMKPEALERLEKMIPVGr 220

                         170
                  ....*....|....*
gi 1720364755 150 ---PEDVAEAVIYVL 161
Cdd:PRK08217  221 lgePEEIAHTVRFII 235
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 11-163 3.75e-16

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 73.41  E-value: 3.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIddGHIININSMCGHRVPPQSVihFYSAT 90
Cdd:PRK12936   80 GVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRY--GRIINITSVVGVTGNPGQA--NYCAS 155

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720364755  91 KYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCLRPEDVAEAVIYVLST 163
Cdd:PRK12936  156 KAGMIGFSKSLAQEI--ATRNVTVNCVAPGFIESAMTGKLNDKQKEAIMGAIPMKRMGTGAEVASAVAYLASS 226
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 1-162 4.78e-16

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 73.19  E-value: 4.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMA-RPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRvp 79
Cdd:cd05345    69 MVEAALSKFGRLDILVNNAGIThRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQG--GGVIINIASTAGLR-- 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  80 PQSVIHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATY-EHI---KCLRPEDVAE 155
Cdd:cd05345   145 PRPGLTWYNASKGWVVTATKAMAVEL--APRNIRVNCLCPVAGETPLLSMFMGEDTPENRAKFrATIplgRLSTPDDIAN 222


                  ....*..
gi 1720364755 156 AVIYVLS 162
Cdd:cd05345   223 AALYLAS 229
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 7-162 5.52e-16

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: 72.87  E-value: 5.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   7 SQHSGVDICINNAGM--ARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGhrVPPQSVI 84
Cdd:cd05326    75 ARFGRLDIMFNNAGVlgAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAK--KGSIVSVASVAG--VVGGLGP 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  85 HFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQF---AFKLHDKDPGEAAATYEHIK--CLRPEDVAEAVIY 159
Cdd:cd05326   151 HAYTASKHAVLGLTRSAATEL--GEHGIRVNCVSPYGVATPLltaGFGVEDEAIEEAVRGAANLKgtALRPEDIAAAVLY 228


                  ...
gi 1720364755 160 VLS 162
Cdd:cd05326   229 LAS 231
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
8-162 5.54e-16

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 72.88  E-value: 5.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   8 QHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRvpPQSVIHFY 87
Cdd:PRK12824   77 EEGPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQG--YGRIINISSVNGLK--GQFGQTNY 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364755  88 SATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDkdpgEAAATY-EHIKCLR---PEDVAEAVIYVLS 162
Cdd:PRK12824  153 SAAKAGMIGFTKALASEG--ARYGITVNCIAPGYIATPMVEQMGP----EVLQSIvNQIPMKRlgtPEEIAAAVAFLVS 225
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 2-162 5.76e-16

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 72.80  E-value: 5.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERniDDGHIININSMCGHRVPPQ 81
Cdd:cd05341    70 VDTAREAFGRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEA--GGGSIINMSSIEGLVGDPA 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  82 svIHFYSATKYAVTALTEGLRQELLEAQTHIRATCISPGLVETQFAFKLHDKdpGEAAATYEHIKCLR---PEDVAEAVI 158
Cdd:cd05341   148 --LAAYNASKGAVRGLTKSAALECATQGYGIRVNSVHPGYIYTPMTDELLIA--QGEMGNYPNTPMGRagePDEIAYAVV 223


                  ....
gi 1720364755 159 YVLS 162
Cdd:cd05341   224 YLAS 227
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 1-162 6.21e-16

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 73.08  E-value: 6.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGhRVPp 80
Cdd:cd05344    68 LVEKAGDAFGRVDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERG--WGRIVNISSLTV-KEP- 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 qsVIHFY--SATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCL---------- 148
Cdd:cd05344   144 --EPNLVlsNVARAGLIGLVKTLSREL--APDGVTVNSVLPGYIDTERVRRLLEARAEKEGISVEEAEKEvasqiplgrv 219

                         170
                  ....*....|....*
gi 1720364755 149 -RPEDVAEAVIYVLS 162
Cdd:cd05344   220 gKPEELAALIAFLAS 234
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 3-158 9.73e-16

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: 72.05  E-value: 9.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   3 SAVRSQHSGVDICINNAGMARPDTLL-SGSTSGWKDMFNVNVLA-LSICTreAYQSMKERNiDDGHIININSMCGHRVPP 80
Cdd:cd05354    66 KAAAAQAKDVDVVINNAGVLKPATLLeEGALEALKQEMDVNVFGlLRLAQ--AFAPVLKAN-GGGAIVNLNSVASLKNFP 142

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364755  81 QSVIhfYSATKYAVTALTEGLRQELLEAQTHIRAtcISPGLVETQFAfklHDKDPGEAAatyehikclrPEDVAEAVI 158
Cdd:cd05354   143 AMGT--YSASKSAAYSLTQGLRAELAAQGTLVLS--VHPGPIDTRMA---AGAGGPKES----------PETVAEAVL 203
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 4-127 9.80e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 72.64  E-value: 9.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQsv 83
Cdd:PRK06180   71 DAEATFGPIDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARR--RGHIVNITSMGGLITMPG-- 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720364755  84 IHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFA 127
Cdd:PRK06180  147 IGYYCGSKFALEGISESLAKEV--APFGIHVTAVEPGSFRTDWA 188
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 2-131 1.05e-15

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: 71.98  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQ 81
Cdd:cd05350    66 IAELEAELGGLDLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKG--RGHLVLISSVAALRGLPG 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720364755  82 SVIhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLH 131
Cdd:cd05350   144 AAA--YSASKAALSSLAESLRYDV--KKRGIRVTVINPGFIDTPLTANMF 189
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 1-162 1.06e-15

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


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 72.00  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNA--GMARPdtLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRV 78
Cdd:cd05359    66 MFAAVKERFGRLDVLVSNAaaGAFRP--LSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERG--GGRIVAISSLGSIRA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  79 PPQSVIHfySATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQ-FAFKLHDKDPGEAAAtyEHI---KCLRPEDVA 154
Cdd:cd05359   142 LPNYLAV--GTAKAALEALVRYLAVEL--GPRGIRVNAVSPGVIDTDaLAHFPNREDLLEAAA--ANTpagRVGTPQDVA 215


                  ....*...
gi 1720364755 155 EAVIYVLS 162
Cdd:cd05359   216 DAVGFLCS 223
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 1-165 1.10e-15

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


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 72.04  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHR-VP 79
Cdd:cd05338    82 LVEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAG--QGHILNISPPLSLRpAR 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  80 PQSVihfYSATKYAVTALTEGLRQELLEAQthIRATCISPG-LVETQFAFKLhdKDPGEAAAtyehikCLRPEDVAEAVI 158
Cdd:cd05338   160 GDVA---YAAGKAGMSRLTLGLAAELRRHG--IAVNSLWPStAIETPAATEL--SGGSDPAR------ARSPEILSDAVL 226


                  ....*..
gi 1720364755 159 YVLSTPP 165
Cdd:cd05338   227 AILSRPA 233
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
8-124 1.38e-15

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 72.08  E-value: 1.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   8 QHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMC----GHRVPPqsv 83
Cdd:PRK06935   88 EFGKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQG--SGKIINIASMLsfqgGKFVPA--- 162

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1720364755  84 ihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVET 124
Cdd:PRK06935  163 ---YTASKHGVAGLTKAFANEL--AAYNIQVNAIAPGYIKT 198
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 3-162 1.80e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 71.96  E-value: 1.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   3 SAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIdDGHIININSMCGHrvPPQS 82
Cdd:PRK06198   76 AAADEAFGRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKA-EGTIVNIGSMSAH--GGQP 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  83 VIHFYSATKYAVTALTEGLrqelleAQTH----IRATCISPGLVET------QFAFklHDKDPG---EAAATYEHIKCLR 149
Cdd:PRK06198  153 FLAAYCASKGALATLTRNA------AYALlrnrIRVNGLNIGWMATegedriQREF--HGAPDDwleKAAATQPFGRLLD 224

                         170
                  ....*....|...
gi 1720364755 150 PEDVAEAVIYVLS 162
Cdd:PRK06198  225 PDEVARAVAFLLS 237
PRK05855 PRK05855
SDR family oxidoreductase;
5-158 2.21e-15

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 73.09  E-value: 2.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   5 VRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNiDDGHIININSMCGHRvpPQSVI 84
Cdd:PRK05855  386 VRAEHGVPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERG-TGGHIVNVASAAAYA--PSRSL 462

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  85 HFYSATKYAVTALTEGLRQELLEAqtHIRATCISPGLVET------QFAfklhDKDPGEAAATYEHIKCL------RPED 152
Cdd:PRK05855  463 PAYATSKAAVLMLSECLRAELAAA--GIGVTAICPGFVDTnivattRFA----GADAEDEARRRGRADKLyqrrgyGPEK 536


                  ....*.
gi 1720364755 153 VAEAVI 158
Cdd:PRK05855  537 VAKAIV 542
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 5-141 2.64e-15

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: 70.73  E-value: 2.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   5 VRSQHSGVDICINNAGMARPDTLLSGSTSG-WKDMFNVNVLALSICTREAYQSMKerNIDDGHIININSMCGHRVPPqsv 83
Cdd:cd05324    72 VEEKYGGLDILVNNAGIAFKGFDDSTPTREqARETMKTNFFGTVDVTQALLPLLK--KSPAGRIVNVSSGLGSLTSA--- 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364755  84 ihfYSATKYAVTALTEGLRQELLEaqTHIRATCISPGLVETQFAFKLHDKDPGEAAAT 141
Cdd:cd05324   147 ---YGVSKAALNALTRILAKELKE--TGIKVNACCPGWVKTDMGGGKAPKTPEEGAET 199
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 1-162 3.80e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 70.91  E-value: 3.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARP--DTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRV 78
Cdd:PRK06057   69 LFDTAAETYGSVDIAFNNAGISPPedDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQG--KGSIINTASFVAVMG 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  79 PPQSVIHfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCLR---PEDVAE 155
Cdd:PRK06057  147 SATSQIS-YTASKGGVLAMSRELGVQF--ARQGIRVNALCPGPVNTPLLQELFAKDPERAARRLVHVPMGRfaePEEIAA 223


                  ....*..
gi 1720364755 156 AVIYVLS 162
Cdd:PRK06057  224 AVAFLAS 230
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-162 5.86e-15

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 70.28  E-value: 5.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   7 SQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIddGHIININSMCG-----HRVPpq 81
Cdd:PRK12825   80 ERFGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRG--GRIVNISSVAGlpgwpGRSN-- 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  82 svihfYSATKYAVTALTEGLRQEllEAQTHIRATCISPGLVETQFAfklhDKDPGEAAATYEHIKCLR----PEDVAEAV 157
Cdd:PRK12825  156 -----YAAAKAGLVGLTKALARE--LAEYGITVNMVAPGDIDTDMK----EATIEEAREAKDAETPLGrsgtPEDIARAV 224


                  ....*
gi 1720364755 158 IYVLS 162
Cdd:PRK12825  225 AFLCS 229
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 12-162 6.43e-15

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: 70.19  E-value: 6.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGH--RVPPQSVihfYSA 89
Cdd:cd05368    71 IDVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARK--DGSIINMSSVASSikGVPNRFV---YST 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364755  90 TKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFA-FKLHDKDPGEAA----ATYEHIKCL-RPEDVAEAVIYVLS 162
Cdd:cd05368   146 TKAAVIGLTKSVAADF--AQQGIRCNAICPGTVDTPSLeERIQAQPDPEEAlkafAARQPLGRLaTPEEVAALAVYLAS 222
PRK06484 PRK06484
short chain dehydrogenase; Validated
 2-164 1.04e-14

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 71.03  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARP-DTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKErnidDGHIININSMCGHRVPP 80
Cdd:PRK06484  334 FAQIQARWGRLDVLVNNAGIAEVfKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQ----GGVIVNLGSIASLLALP 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSviHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCLR---PEDVAEAv 157
Cdd:PRK06484  410 PR--NAYCASKAAVTMLSRSLACEW--APAGIRVNTVAPGYIETPAVLALKASGRADFDSIRRRIPLGRlgdPEEVAEA- 484


                  ....*..
gi 1720364755 158 IYVLSTP 164
Cdd:PRK06484  485 IAFLASP 491
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 4-162 1.88e-14

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 68.67  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQsv 83
Cdd:PRK12828   75 EVNRQFGRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASG--GGRIVNIGAGAALKAGPG-- 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  84 IHFYSATKYAVTALTEGLRQELLEAQthIRATCISPGLVET-QFAFKLHDKDPGeaaatyehiKCLRPEDVAEAVIYVLS 162
Cdd:PRK12828  151 MGAYAAAKAGVARLTEALAAELLDRG--ITVNAVLPSIIDTpPNRADMPDADFS---------RWVTPEQIAAVIAFLLS 219
PRK07856 PRK07856
SDR family oxidoreductase;
1-162 2.14e-14

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 68.81  E-value: 2.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKeRNIDDGHIININSMCGHRVPP 80
Cdd:PRK07856   65 LVDAIVERHGRLDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQ-QQPGGGSIVNIGSVSGRRPSP 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIhfYSATKYAVTALTEGLRQELLEAqthIRATCISPGLVETQFAfKLHDKDPGEAAATYEHIKCLR---PEDVAEAV 157
Cdd:PRK07856  144 GTAA--YGAAKAGLLNLTRSLAVEWAPK---VRVNAVVVGLVRTEQS-ELHYGDAEGIAAVAATVPLGRlatPADIAWAC 217


                  ....*
gi 1720364755 158 IYVLS 162
Cdd:PRK07856  218 LFLAS 222
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 2-162 3.62e-14

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 68.16  E-value: 3.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARPD-TLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNiDDGHIININSMCGH---- 76
Cdd:PRK12829   77 FDTAVERFGGLDVLVNNAGIAGPTgGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASG-HGGVIIALSSVAGRlgyp 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  77 -RVPpqsvihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVET-------QFAFKLHDKDPGEAAATY-EHIKC 147
Cdd:PRK12829  156 gRTP-------YAASKWAVVGLVKSLAIEL--GPLGIRVNAILPGIVRGprmrrviEARAQQLGIGLDEMEQEYlEKISL 226

                         170
                  ....*....|....*...
gi 1720364755 148 LR---PEDVAEAVIYVLS 162
Cdd:PRK12829  227 GRmvePEDIAATALFLAS 244
PRK05693 PRK05693
SDR family oxidoreductase;
8-127 4.47e-14

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 68.28  E-value: 4.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   8 QHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNiddGHIININSMCGHRVPPqsvihF- 86
Cdd:PRK05693   69 EHGGLDVLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSR---GLVVNIGSVSGVLVTP-----Fa 140

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720364755  87 --YSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFA 127
Cdd:PRK05693  141 gaYCASKAAVHALSDALRLEL--APFGVQVMEVQPGAIASQFA 181
PRK07063 PRK07063
SDR family oxidoreductase;
1-162 4.68e-14

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 67.77  E-value: 4.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIddGHIININSMCGHRVPP 80
Cdd:PRK07063   76 AVAAAEEAFGPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGR--GSIVNIASTHAFKIIP 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSvihF-YSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCL------RPEDV 153
Cdd:PRK07063  154 GC---FpYPVAKHGLLGLTRALGIEY--AARNVRVNAIAPGYIETQLTEDWWNAQPDPAAARAETLALQpmkrigRPEEV 228


                  ....*....
gi 1720364755 154 AEAVIYVLS 162
Cdd:PRK07063  229 AMTAVFLAS 237
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 11-165 1.02e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 67.64  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERniDDGHIININSMCGHR-VPPQSVihfYSA 89
Cdd:PRK07109   85 PIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPR--DRGAIIQVGSALAYRsIPLQSA---YCA 159

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364755  90 TKYAVTALTEGLRQELLEAQTHIRATCISPGLVETQFAFKLHDKDPGEAAAT---YEhikclrPEDVAEAVIYVLSTPP 165
Cdd:PRK07109  160 AKHAIRGFTDSLRCELLHDGSPVSVTMVQPPAVNTPQFDWARSRLPVEPQPVppiYQ------PEVVADAILYAAEHPR 232
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 1-162 1.02e-13

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


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 66.75  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAG-MARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVP 79
Cdd:cd08944    67 LFERAVEEFGGLDLLVNNAGaMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARG--GGSIVNLSSIAGQSGD 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  80 PqsVIHFYSATKYAVTALTEGLRQELLEAQthIRATCISPGLVET-----QFAFKLHDKDPGEAAATYEHI--KCLRPED 152
Cdd:cd08944   145 P--GYGAYGASKAAIRNLTRTLAAELRHAG--IRCNALAPGLIDTplllaKLAGFEGALGPGGFHLLIHQLqgRLGRPED 220

                         170
                  ....*....|
gi 1720364755 153 VAEAVIYVLS 162
Cdd:cd08944   221 VAAAVVFLLS 230
PRK08264 PRK08264
SDR family oxidoreductase;
12-158 1.05e-13

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 66.84  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARP-DTLLSGSTSGWKDMFNVNVLALSICTReAYQSMKERNiDDGHIININSMCghrvppqSVIHF---- 86
Cdd:PRK08264   74 VTILVNNAGIFRTgSLLLEGDEDALRAEMETNYFGPLAMAR-AFAPVLAAN-GGGAIVNVLSVL-------SWVNFpnlg 144

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720364755  87 -YSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETqfafKLHDKDPGEAAAtyehikclrPEDVAEAVI 158
Cdd:PRK08264  145 tYSASKAAAWSLTQALRAEL--APQGTRVLGVHPGPIDT----DMAAGLDAPKAS---------PADVARQIL 202
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 1-161 1.12e-13

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 66.83  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIddGHIININSMCGHRVPP 80
Cdd:PRK12429   71 GIDYAVETFGGVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGG--GRIINMASVHGLVGSA 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIhfYSATKYAVTALTEGLRQEllEAQTHIRATCISPGLVETQfafkLHDKDPGEAAATyehiKCLRPEDVAEAVIYV 160
Cdd:PRK12429  149 GKAA--YVSAKHGLIGLTKVVALE--GATHGVTVNAICPGYVDTP----LVRKQIPDLAKE----RGISEEEVLEDVLLP 216


                  .
gi 1720364755 161 L 161
Cdd:PRK12429  217 L 217
PRK07774 PRK07774
SDR family oxidoreductase;
1-162 1.18e-13

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 66.69  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNA---GMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHr 77
Cdd:PRK07774   73 MADATVSAFGGIDYLVNNAaiyGGMKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRG--GGAIVNQSSTAAW- 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  78 vPPQSvihFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLhdkDPGE-AAATYEHIKCLR---PEDV 153
Cdd:PRK07774  150 -LYSN---FYGLAKVGLNGLTQQLAREL--GGMNIRVNAIAPGPIDTEATRTV---TPKEfVADMVKGIPLSRmgtPEDL 220


                  ....*....
gi 1720364755 154 AEAVIYVLS 162
Cdd:PRK07774  221 VGMCLFLLS 229
PRK09730 PRK09730
SDR family oxidoreductase;
1-162 1.36e-13

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 66.41  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAG-MARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIDDG-HIININSMCGHRV 78
Cdd:PRK09730   69 MFTAIDQHDEPLAALVNNAGiLFTQCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALKHGGSGgAIVNVSSAASRLG 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  79 PPQSVIHfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQfafkLHDK--DPGEAAATYEHIKCLR---PEDV 153
Cdd:PRK09730  149 APGEYVD-YAASKGAIDTLTTGLSLEV--AAQGIRVNCVRPGFIYTE----MHASggEPGRVDRVKSNIPMQRggqPEEV 221


                  ....*....
gi 1720364755 154 AEAVIYVLS 162
Cdd:PRK09730  222 AQAIVWLLS 230
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 8-162 1.54e-13

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: 66.41  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   8 QHSGVDICINNAGMaRP--DTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRvpPQSVIH 85
Cdd:cd08936    84 LHGGVDILVSNAAV-NPffGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRG--GGSVVIVSSVAAFH--PFPGLG 158

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364755  86 FYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKL-HDKDPGEAAATYEHIKCL-RPEDVAEAVIYVLS 162
Cdd:cd08936   159 PYNVSKTALLGLTKNLAPEL--APRNIRVNCLAPGLIKTSFSSALwMDKAVEESMKETLRIRRLgQPEDCAGIVSFLCS 235
PRK06138 PRK06138
SDR family oxidoreductase;
1-162 2.47e-13

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 65.94  E-value: 2.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININS---MCGHR 77
Cdd:PRK06138   71 LVDFVAARWGRLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQG--GGSIVNTASqlaLAGGR 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  78 VPPQsvihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHD--KDPGEAAATYEHIKCLR----PE 151
Cdd:PRK06138  149 GRAA-----YVASKGAIASLTRAMALDH--ATDGIRVNAVAPGTIDTPYFRRIFArhADPEALREALRARHPMNrfgtAE 221

                         170
                  ....*....|.
gi 1720364755 152 DVAEAVIYVLS 162
Cdd:PRK06138  222 EVAQAALFLAS 232
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 1-164 2.49e-13

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 65.92  E-value: 2.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKerniDDGHIININ-SMCGHRVP 79
Cdd:PRK12937   73 LFDAAETAFGRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLG----QGGRIINLStSVIALPLP 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  80 PQSVihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFklhDKDPGEAAATYEHIKCL----RPEDVAE 155
Cdd:PRK12937  149 GYGP---YAASKAAVEGLVHVLANEL--RGRGITVNAVAPGPVATELFF---NGKSAEQIDQLAGLAPLerlgTPEEIAA 220


                  ....*....
gi 1720364755 156 AVIYvLSTP 164
Cdd:PRK12937  221 AVAF-LAGP 228
PRK06124 PRK06124
SDR family oxidoreductase;
1-162 3.84e-13

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 65.50  E-value: 3.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPP 80
Cdd:PRK06124   78 AFARIDAEHGRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQG--YGRIIAITSIAGQVARA 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQF-AFKLHDKDPGEAAATYEHI-KCLRPEDVAEAVI 158
Cdd:PRK06124  156 GDAV--YPAAKQGLTGLMRALAAEF--GPHGITSNAIAPGYFATETnAAMAADPAVGPWLAQRTPLgRWGRPEEIAGAAV 231


                  ....
gi 1720364755 159 YVLS 162
Cdd:PRK06124  232 FLAS 235
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 1-169 4.30e-13

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 65.30  E-value: 4.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSM-KERNidDGHIININSMCGHRVP 79
Cdd:PRK13394   74 GIDKVAERFGSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMyKDDR--GGVVIYMGSVHSHEAS 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  80 P-QSVihfYSATKYAVTALTEGLRQEllEAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKC----------- 147
Cdd:PRK13394  152 PlKSA---YVTAKHGLLGLARVLAKE--GAKHNVRSHVVCPGFVRTPLVDKQIPEQAKELGISEEEVVKkvmlgktvdgv 226

                         170       180
                  ....*....|....*....|...
gi 1720364755 148 -LRPEDVAEAVIYvLSTPPHVQV 169
Cdd:PRK13394  227 fTTVEDVAQTVLF-LSSFPSAAL 248
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 11-163 5.86e-13

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 65.13  E-value: 5.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIdDGHIININSMcgHRVPPQSVIHFYSAT 90
Cdd:PRK08936   85 TLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDI-KGNIINMSSV--HEQIPWPLFVHYAAS 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  91 KYAVTALTEGLRQELleAQTHIRATCISPGLVET-----QFAfklhdkDPGEAAATYEHIKCLR---PEDVAEAVIYVLS 162
Cdd:PRK08936  162 KGGVKLMTETLAMEY--APKGIRVNNIGPGAINTpinaeKFA------DPKQRADVESMIPMGYigkPEEIAAVAAWLAS 233


                  .
gi 1720364755 163 T 163
Cdd:PRK08936  234 S 234
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 12-126 1.24e-12

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 64.15  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMarpdTLLSG----STSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGhrVPPQSVIHFY 87
Cdd:PRK06179   74 IDVLVNNAGV----GLAGAaeesSIAQAQALFDTNVFGILRMTRAVLPHMRAQG--SGRIINISSVLG--FLPAPYMALY 145

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1720364755  88 SATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQF 126
Cdd:PRK06179  146 AASKHAVEGYSESLDHEV--RQFGIRVSLVEPAYTKTNF 182
PRK06172 PRK06172
SDR family oxidoreductase;
7-162 1.26e-12

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 64.00  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   7 SQHSGVDICINNAGMA-RPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQSVIh 85
Cdd:PRK06172   80 AAYGRLDYAFNNAGIEiEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQG--GGAIVNTASVAGLGAAPKMSI- 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  86 fYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAA-ATYEHI--KCLRPEDVAEAVIYVLS 162
Cdd:PRK06172  157 -YAASKHAVIGLTKSAAIEY--AKKGIRVNAVCPAVIDTDMFRRAYEADPRKAEfAAAMHPvgRIGKVEEVASAVLYLCS 233
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 12-124 1.46e-12

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: 63.71  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPD-TLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNiddGHIININSMCG-----HRVPpqsvih 85
Cdd:cd08933    88 IDCLVNNAGWHPPHqTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQ---GNIINLSSLVGsigqkQAAP------ 158

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1720364755  86 fYSATKYAVTALTEGLrqELLEAQTHIRATCISPGLVET 124
Cdd:cd08933   159 -YVATKGAITAMTKAL--AVDESRYGVRVNCISPGNIWT 194
PRK06914 PRK06914
SDR family oxidoreductase;
2-164 1.89e-12

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 63.89  E-value: 1.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPq 81
Cdd:PRK06914   72 FQLVLKEIGRIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQK--SGKIINISSISGRVGFP- 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  82 sVIHFYSATKYAVTALTEGLRQELLEAQthIRATCISPGLVET---QFAFKLHDKDPGEAAATYEHIKCLR--------- 149
Cdd:PRK06914  149 -GLSPYVSSKYALEGFSESLRLELKPFG--IDVALIEPGSYNTniwEVGKQLAENQSETTSPYKEYMKKIQkhinsgsdt 225

                         170
                  ....*....|....*...
gi 1720364755 150 ---PEDVAEAVIYVLSTP 164
Cdd:PRK06914  226 fgnPIDVANLIVEIAESK 243
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 12-171 2.00e-12

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: 63.17  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHR-VPPQSVihfYSAT 90
Cdd:cd05360    78 IDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRG--GGALINVGSLLGYRsAPLQAA---YSAS 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  91 KYAVTALTEGLRQELLEAQTHIRATCISPGLVETQFAFKLH---DKDPGEAAATYEhikclrPEDVAEAVIYVLSTPPH- 166
Cdd:cd05360   153 KHAVRGFTESLRAELAHDGAPISVTLVQPTAMNTPFFGHARsymGKKPKPPPPIYQ------PERVAEAIVRAAEHPRRe 226


                  ....*
gi 1720364755 167 VQVGD 171
Cdd:cd05360   227 VKVGD 231
PRK08251 PRK08251
SDR family oxidoreductase;
2-125 2.24e-12

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 63.03  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVN-VLALSICtrEAYQSM-KERNidDGHIININSMCGHRVP 79
Cdd:PRK08251   72 FAEFRDELGGLDRVIVNAGIGKGARLGTGKFWANKATAETNfVAALAQC--EAAMEIfREQG--SGHLVLISSVSAVRGL 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720364755  80 PqSVIHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQ 125
Cdd:PRK08251  148 P-GVKAAYAASKAGVASLGEGLRAEL--AKTPIKVSTIEPGYIRSE 190
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 2-162 2.58e-12

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 63.20  E-value: 2.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNiDDGHIININSMCGHR---- 77
Cdd:PRK12827   78 LDAGVEEFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRAR-RGGRIVNIASVAGVRgnrg 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  78 -VPpqsvihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAfklhdkdpgEAAATYEHIKCL-------R 149
Cdd:PRK12827  157 qVN-------YAASKAGLIGLTKTLANEL--APRGITVNAVAPGAINTPMA---------DNAAPTEHLLNPvpvqrlgE 218

                         170
                  ....*....|...
gi 1720364755 150 PEDVAEAVIYVLS 162
Cdd:PRK12827  219 PDEVAALVAFLVS 231
PRK05867 PRK05867
SDR family oxidoreductase;
1-132 2.92e-12

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 63.13  E-value: 2.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIDdGHIININSMCGHRVP- 79
Cdd:PRK05867   76 MLDQVTAELGGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQG-GVIINTASMSGHIINv 154

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720364755  80 PQSVIHfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHD 132
Cdd:PRK05867  155 PQQVSH-YCASKAAVIHLTKAMAVEL--APHKIRVNSVSPGYILTELVEPYTE 204
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 4-162 3.82e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 62.75  E-value: 3.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQSV 83
Cdd:PRK06841   82 AVISAFGRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAG--GGKIVNLASQAGVVALERHV 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  84 IhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATyeHIKCLR---PEDVAEAVIYV 160
Cdd:PRK06841  160 A--YCASKAGVVGMTKVLALEW--GPYGITVNAISPTVVLTELGKKAWAGEKGERAKK--LIPAGRfayPEEIAAAALFL 233


                  ..
gi 1720364755 161 LS 162
Cdd:PRK06841  234 AS 235
PRK07577 PRK07577
SDR family oxidoreductase;
9-162 4.26e-12

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 62.05  E-value: 4.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   9 HSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERniDDGHIININSMCGHRVPPQSVihfYS 88
Cdd:PRK07577   66 IHPVDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLR--EQGRIVNICSRAIFGALDRTS---YS 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720364755  89 ATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCLR---PEDVAEAVIYVLS 162
Cdd:PRK07577  141 AAKSALVGCTRTWALEL--AEYGITVNAVAPGPIETELFRQTRPVGSEEEKRVLASIPMRRlgtPEEVAAAIAFLLS 215
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 7-164 4.95e-12

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


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 61.91  E-value: 4.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   7 SQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQSVIhf 86
Cdd:cd05357    74 RAFGRCDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSR--NGSIINIIDAMTDRPLTGYFA-- 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  87 YSATKYAVTALTEGLRQELleaQTHIRATCISPGLVetqfafKLHDKDPGEAAATYEHIKCLR----PEDVAEAVIYVLS 162
Cdd:cd05357   150 YCMSKAALEGLTRSAALEL---APNIRVNGIAPGLI------LLPEDMDAEYRENALRKVPLKrrpsAEEIADAVIFLLD 220


                  ..
gi 1720364755 163 TP 164
Cdd:cd05357   221 SN 222
PRK08267 PRK08267
SDR family oxidoreductase;
7-170 5.10e-12

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 62.26  E-value: 5.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   7 SQHSG--VDICINNAGMARpdtllsgstSGW---------KDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCG 75
Cdd:PRK08267   71 AAATGgrLDVLFNNAGILR---------GGPfedipleahDRVIDINVKGVLNGAHAALPYLKATP--GARVINTSSASA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  76 -HRVPPQSVihfYSATKYAVTALTEGLRqelLEAQTH-IRATCISPGLVETQFAfklhDKDPGE--AAATYEHIKCLRPE 151
Cdd:PRK08267  140 iYGQPGLAV---YSATKFAVRGLTEALD---LEWRRHgIRVADVMPLFVDTAML----DGTSNEvdAGSTKRLGVRLTPE 209

                         170       180
                  ....*....|....*....|.
gi 1720364755 152 DVAEAV--IYVLSTPPHVQVG 170
Cdd:PRK08267  210 DVAEAVwaAVQHPTRLHWPVG 230
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 4-162 5.25e-12

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


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 62.17  E-value: 5.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIDDGHIININSMCGHrvppQSV 83
Cdd:cd08945    73 AAVARYGPIDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAGGMLERGTGRIINIASTGGK----QGV 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  84 IHF--YSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHI-----------KCLRP 150
Cdd:cd08945   149 VHAapYSASKHGVVGFTKALGLEL--ARTGITVNAVCPGFVETPMAASVREHYADIWEVSTEEAfdritarvplgRYVTP 226

                         170
                  ....*....|..
gi 1720364755 151 EDVAEAVIYVLS 162
Cdd:cd08945   227 EEVAGMVAYLIG 238
PRK06182 PRK06182
short chain dehydrogenase; Validated
 7-128 6.17e-12

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 62.28  E-value: 6.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   7 SQHSGVDICINNAGMarpdtllsGSTSGWKDM--------FNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRV 78
Cdd:PRK06182   70 AEEGRIDVLVNNAGY--------GSYGAIEDVpidearrqFEVNLFGAARLTQLVLPHMRAQR--SGRIINISSMGGKIY 139

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720364755  79 PPQSVihFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAF 128
Cdd:PRK06182  140 TPLGA--WYHATKFALEGFSDALRLEV--APFGIDVVVIEPGGIKTEWGD 185
PRK07035 PRK07035
SDR family oxidoreductase;
2-162 6.70e-12

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 61.96  E-value: 6.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGmARP------DTLLsgstSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCG 75
Cdd:PRK07035   76 FAHIRERHGRLDILVNNAA-ANPyfghilDTDL----GAFQKTVDVNIRGYFFMSVEAGKLMKEQG--GGSIVNVASVNG 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  76 hrVPPQSVIHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDpgeaaATYE----HIKCLR-- 149
Cdd:PRK07035  149 --VSPGDFQGIYSITKAAVISMTKAFAKEC--APFGIRVNALLPGLTDTKFASALFKND-----AILKqalaHIPLRRha 219

                         170
                  ....*....|....
gi 1720364755 150 -PEDVAEAVIYVLS 162
Cdd:PRK07035  220 ePSEMAGAVLYLAS 233
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 12-162 7.64e-12

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


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 61.72  E-value: 7.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIDdGHIININSMCGHR-VPPQSVihfYSAT 90
Cdd:cd05351    77 VDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVP-GSIVNVSSQASQRaLTNHTV---YCST 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720364755  91 KYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAfKLHDKDPGEAAATYEHI---KCLRPEDVAEAVIYVLS 162
Cdd:cd05351   153 KAALDMLTKVMALEL--GPHKIRVNSVNPTVVMTDMG-RDNWSDPEKAKKMLNRIplgKFAEVEDVVNAILFLLS 224
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 11-157 8.55e-12

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: 61.31  E-value: 8.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKErnIDDGHIININSMCGHRVPPQSVIhfYSAT 90
Cdd:cd08931    76 RLDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKA--TPGARVINTASSSAIYGQPDLAV--YSAT 151

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364755  91 KYAVTALTEGLRqelLEAQTH-IRATCISPGLVETQFAFKLHDkdpgEAAATYEHIKCLRPEDVAEAV 157
Cdd:cd08931   152 KFAVRGLTEALD---VEWARHgIRVADVWPWFVDTPILTKGET----GAAPKKGLGRVLPVSDVAKVV 212
PRK05650 PRK05650
SDR family oxidoreductase;
11-136 1.01e-11

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 61.60  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLAL-SICtrEAYQSMKERNiDDGHIININSMCGHRVPPQSVihFYSA 89
Cdd:PRK05650   77 GIDVIVNNAGVASGGFFEELSLEDWDWQIAINLMGVvKGC--KAFLPLFKRQ-KSGRIVNIASMAGLMQGPAMS--SYNV 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1720364755  90 TKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPG 136
Cdd:PRK05650  152 AKAGVVALSETLLVEL--ADDEIGVHVVCPSFFQTNLLDSFRGPNPA 196
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
2-159 1.17e-11

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 61.28  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMArPDTLLSGST-SGWKDMFNVNVLALSICTREAYQSMKERNiDDGHIININSMCGHRVPP 80
Cdd:PRK08643   70 VRQVVDTFGDLNVVVNNAGVA-PTTPIETITeEQFDKVYNINVGGVIWGIQAAQEAFKKLG-HGGKIINATSQAGVVGNP 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QsvIHFYSATKYAVTALTEGLRQELLEAQTHIRATCisPGLVETQFAFKLhDKDPGEAA------ATYEHIKCL------ 148
Cdd:PRK08643  148 E--LAVYSSTKFAVRGLTQTAARDLASEGITVNAYA--PGIVKTPMMFDI-AHQVGENAgkpdewGMEQFAKDItlgrls 222

                         170
                  ....*....|.
gi 1720364755 149 RPEDVAEAVIY 159
Cdd:PRK08643  223 EPEDVANCVSF 233
PRK06181 PRK06181
SDR family oxidoreductase;
11-158 1.35e-11

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 61.15  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAGM---ARPDTLlsGSTSGWKDMFNVNVLALSICTREAYQSMKERnidDGHIININSMCGHR-VPPQSVihf 86
Cdd:PRK06181   78 GIDILVNNAGItmwSRFDEL--TDLSVFERVMRVNYLGAVYCTHAALPHLKAS---RGQIVVVSSLAGLTgVPTRSG--- 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720364755  87 YSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDpGEAAAT--YEHIKCLRPEDVAEAVI 158
Cdd:PRK06181  150 YAASKHALHGFFDSLRIEL--ADDGVAVTVVCPGFVATDIRKRALDGD-GKPLGKspMQESKIMSAEECAEAIL 220
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 1-162 1.43e-11

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: 61.06  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNiddGHIININSMCGHRVPP 80
Cdd:cd09761    65 VVYAMLEKLGRIDVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK---GRIINIASTRAFQSEP 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSviHFYSATKYAVTALTEGLRQELleaQTHIRATCISPGLVETQFAFKL---------HDKDPGEAAATyehikclrPE 151
Cdd:cd09761   142 DS--EAYAASKGGLVALTHALAMSL---GPDIRVNCISPGWINTTEQQEFtaapltqedHAQHPAGRVGT--------PK 208

                         170
                  ....*....|.
gi 1720364755 152 DVAEAVIYVLS 162
Cdd:cd09761   209 DIANLVLFLCQ 219
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 1-169 2.39e-11

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


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 60.54  E-value: 2.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIddGHIININSMCGHRVPP 80
Cdd:cd08940    71 MVAYAQRQFGGVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGW--GRIINIASVHGLVASA 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFK----LHDK--DPGEAAAT------YEHIKCL 148
Cdd:cd08940   149 NKSA--YVAAKHGVVGLTKVVALET--AGTGVTCNAICPGWVLTPLVEKqisaLAQKngVPQEQAARelllekQPSKQFV 224

                         170       180
                  ....*....|....*....|.
gi 1720364755 149 RPEDVAEAVIYvLSTPPHVQV 169
Cdd:cd08940   225 TPEQLGDTAVF-LASDAASQI 244
PRK06194 PRK06194
hypothetical protein; Provisional
 4-124 2.65e-11

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 60.41  E-value: 2.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIDD----GHIININSMCGHRVP 79
Cdd:PRK06194   76 AALERFGAVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAEKDpayeGHIVNTASMAGLLAP 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720364755  80 PQSVIhfYSATKYAVTALTEGLRQELLEAQTHIRATCISPGLVET 124
Cdd:PRK06194  156 PAMGI--YNVSKHAVVSLTETLYQDLSLVTDQVGASVLCPYFVPT 198
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 3-164 2.67e-11

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: 60.17  E-value: 2.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   3 SAVRSQHsgVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCG-HRVPPQ 81
Cdd:cd09806    73 ERVTERH--VDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRG--SGRILVTSSVGGlQGLPFN 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  82 SVihfYSATKYAVTALTEGLRQELLEAQTHIraTCISPGLVETQFAFKLHDKDPG--EAAATYEHIKCLR---------- 149
Cdd:cd09806   149 DV---YCASKFALEGLCESLAVQLLPFNVHL--SLIECGPVHTAFMEKVLGSPEEvlDRTADDITTFHFFyqylahskqv 223

                         170       180
                  ....*....|....*....|..
gi 1720364755 150 -------PEDVAEAVIYVLSTP 164
Cdd:cd09806   224 freaaqnPEEVAEVFLTAIRAP 245
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
12-162 3.15e-11

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 60.27  E-value: 3.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTRE-AYQSMKERNidDGHIININSMC----GHRVPPqsvihf 86
Cdd:PRK08993   86 IDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAaAKHFIAQGN--GGKIINIASMLsfqgGIRVPS------ 157

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364755  87 YSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHdKDPGEAAATYEHIKCLR---PEDVAEAVIYVLS 162
Cdd:PRK08993  158 YTASKSGVMGVTRLMANEW--AKHNINVNAIAPGYMATNNTQQLR-ADEQRSAEILDRIPAGRwglPSDLMGPVVFLAS 233
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 4-162 3.84e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 59.73  E-value: 3.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIdDGHIININSMCGHRVPPQSV 83
Cdd:PRK07060   70 AALAAAGAFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGR-GGSIVNVSSQAALVGLPDHL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  84 IhfYSATKYAVTALTEGLRQELLEaqtH-IRATCISPGLVETQFAFKLHDkDPGEAAATYEHIKCLR---PEDVAEAVIY 159
Cdd:PRK07060  149 A--YCASKAALDAITRVLCVELGP---HgIRVNSVNPTVTLTPMAAEAWS-DPQKSGPMLAAIPLGRfaeVDDVAAPILF 222


                  ...
gi 1720364755 160 VLS 162
Cdd:PRK07060  223 LLS 225
PRK07074 PRK07074
SDR family oxidoreductase;
12-164 4.53e-11

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 59.78  E-value: 4.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRV---PPqsvihfYS 88
Cdd:PRK07074   78 VDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRS--RGAVVNIGSVNGMAAlghPA------YS 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364755  89 ATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPG---EAAATYEHIKCLRPEDVAEAVIYvLSTP 164
Cdd:PRK07074  150 AAKAGLIHYTKLLAVEY--GRFGIRANAVAPGTVKTQAWEARVAANPQvfeELKKWYPLQDFATPDDVANAVLF-LASP 225
PRK06484 PRK06484
short chain dehydrogenase; Validated
 2-172 4.58e-11

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 60.63  E-value: 4.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARP--DTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKErNIDDGHIININSMCGHRVP 79
Cdd:PRK06484   70 FEQLHREFGRIDVLVNNAGVTDPtmTATLDTTLEEFARLQAINLTGAYLVAREALRLMIE-QGHGAAIVNVASGAGLVAL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  80 PQSVIhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDK---DPGEAAATYEHIKCLRPEDVAEA 156
Cdd:PRK06484  149 PKRTA--YSASKAAVISLTRSLACEW--AAKGIRVNAVLPGYVRTQMVAELERAgklDPSAVRSRIPLGRLGRPEEIAEA 224

                         170
                  ....*....|....*.
gi 1720364755 157 VIYVLSTPPHVQVGDI 172
Cdd:PRK06484  225 VFFLASDQASYITGST 240
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 12-162 5.48e-11

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: 59.35  E-value: 5.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNiddGHIININSMCGHRvpPQSVIHFYSATK 91
Cdd:cd05364    84 LDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK---GEIVNVSSVAGGR--SFPGVLYYCISK 158

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364755  92 YAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLhDKDPGEAAATYEHIK-------CLRPEDVAEAVIYVLS 162
Cdd:cd05364   159 AALDQFTRCTALEL--APKGVRVNSVSPGVIVTGFHRRM-GMPEEQYIKFLSRAKethplgrPGTVDEVAEAIAFLAS 233
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 5-124 1.27e-10

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: 58.46  E-value: 1.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   5 VRSQHSGVDICINNAGMARP-DTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKErnidDGHIININSMCGHRVPPQSV 83
Cdd:cd05355    99 VVKEFGKLDILVNNAAYQHPqESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKK----GSSIINTTSVTAYKGSPHLL 174

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1720364755  84 IhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVET 124
Cdd:cd05355   175 D--YAATKGAIVAFTRGLSLQL--AEKGIRVNAVAPGPIWT 211
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 8-125 1.29e-10

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 58.23  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   8 QHSG-VDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMcghrvppQS---- 82
Cdd:PRK08085   82 KDIGpIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQ--AGKIINICSM-------QSelgr 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720364755  83 -VIHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQ 125
Cdd:PRK08085  153 dTITPYAASKGAVKMLTRGMCVEL--ARHNIQVNGIAPGYFKTE 194
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 2-126 1.72e-10

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: 58.00  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDI--CINNAGMAR--PDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCG-H 76
Cdd:cd05356    67 YERIEKELEGLDIgiLVNNVGISHsiPEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRK--KGAIVNISSFAGlI 144

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720364755  77 RVPPQSVihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQF 126
Cdd:cd05356   145 PTPLLAT---YSASKAFLDFFSRALYEEY--KSQGIDVQSLLPYLVATKM 189
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 1-162 1.93e-10

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


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 57.85  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNA-------GMARPdtllSGSTSGWKD---MFNVNVLALSICTREAYQSMKERNidDGHIINI 70
Cdd:cd05349    65 MIEEAKNHFGPVDTIVNNAlidfpfdPDQRK----TFDTIDWEDyqqQLEGAVKGALNLLQAVLPDFKERG--SGRVINI 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  71 NS-MCGHRVPPqsvIHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEA-AATYEHIKCL 148
Cdd:cd05349   139 GTnLFQNPVVP---YHDYTTAKAALLGFTRNMAKEL--GPYGITVNMVSGGLLKVTDASAATPKEVFDAiAQTTPLGKVT 213

                         170
                  ....*....|....
gi 1720364755 149 RPEDVAEAVIYVLS 162
Cdd:cd05349   214 TPQDIADAVLFFAS 227
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 12-162 2.10e-10

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 57.67  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMArpD---TLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIINinsMCghrvppqSVIHF-- 86
Cdd:PRK06550   68 VDILCNTAGIL--DdykPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERK--SGIIIN---MC-------SIASFva 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  87 ------YSATKYAVTALTEGLrqELLEAQTHIRATCISPGLVETqfAFKLHDKDPGEAA---ATYEHIK-CLRPEDVAEA 156
Cdd:PRK06550  134 ggggaaYTASKHALAGFTKQL--ALDYAKDGIQVFGIAPGAVKT--PMTAADFEPGGLAdwvARETPIKrWAEPEEVAEL 209


                  ....*.
gi 1720364755 157 VIYVLS 162
Cdd:PRK06550  210 TLFLAS 215
PRK12743 PRK12743
SDR family oxidoreductase;
11-164 4.52e-10

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 56.97  E-value: 4.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMkernIDDGH---IININSMCGHRVPPQSVIhfY 87
Cdd:PRK12743   80 RIDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHM----VKQGQggrIINITSVHEHTPLPGASA--Y 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  88 SATKYAVTALTEGLRQELleAQTHIRATCISPGLVETqfafKLHDKDPGEAAA-TYEHIKCLRPEDVAE--AVIYVLSTP 164
Cdd:PRK12743  154 TAAKHALGGLTKAMALEL--VEHGILVNAVAPGAIAT----PMNGMDDSDVKPdSRPGIPLGRPGDTHEiaSLVAWLCSE 227
PRK07069 PRK07069
short chain dehydrogenase; Validated
 11-162 5.19e-10

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 56.64  E-value: 5.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQSVIhfYSAT 90
Cdd:PRK07069   79 GLSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQ--PASIVNISSVAAFKAEPDYTA--YNAS 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  91 KYAVTALTEGLRQELLEAQTHIRATCISPGLVETQFAfklhdkDP-----GEAAATYE---HIKCLR---PEDVAEAVIY 159
Cdd:PRK07069  155 KAAVASLTKSIALDCARRGLDVRCNSIHPTFIRTGIV------DPifqrlGEEEATRKlarGVPLGRlgePDDVAHAVLY 228


                  ...
gi 1720364755 160 VLS 162
Cdd:PRK07069  229 LAS 231
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 7-162 5.94e-10

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 56.43  E-value: 5.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   7 SQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHrVPPQSvIHF 86
Cdd:PRK08220   72 AETGPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQR--SGAIVTVGSNAAH-VPRIG-MAA 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  87 YSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAA------ATYE-HI---KCLRPEDVAEA 156
Cdd:PRK08220  148 YGASKAALTSLAKCVGLEL--APYGVRCNVVSPGSTDTDMQRTLWVDEDGEQQviagfpEQFKlGIplgKIARPQEIANA 225


                  ....*.
gi 1720364755 157 VIYVLS 162
Cdd:PRK08220  226 VLFLAS 231
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 12-162 1.23e-09

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


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 55.67  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIDdGHIINInSMCGHRVPPQSVIHfYSATK 91
Cdd:cd05369    82 IDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHG-GSILNI-SATYAYTGSPFQVH-SAAAK 158

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720364755  92 YAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCLR---PEDVAEAVIYVLS 162
Cdd:cd05369   159 AGVDALTRSLAVEW--GPYGIRVNAIAPGPIPTTEGMERLAPSGKSEKKMIERVPLGRlgtPEEIANLALFLLS 230
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
2-178 1.35e-09

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 55.40  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIddGHIININSMCGHRvpPQ 81
Cdd:PRK12938   72 FDKVKAEVGEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGW--GRIINISSVNGQK--GQ 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  82 SVIHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETqfafklhdkdpgeaaatyEHIKCLRPeDVAEAVIyvl 161
Cdd:PRK12938  148 FGQTNYSTAKAGIHGFTMSLAQEV--ATKGVTVNTVSPGYIGT------------------DMVKAIRP-DVLEKIV--- 203

                         170
                  ....*....|....*..
gi 1720364755 162 STPPHVQVGDiqmrPTE 178
Cdd:PRK12938  204 ATIPVRRLGS----PDE 216
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 3-162 1.44e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 55.30  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   3 SAVRSQHSGVDICINNAGMARpdTLLSGSTS----GWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMcGHRV 78
Cdd:PRK06523   69 RAVLERLGGVDILVHVLGGSS--APAGGFAAltdeEWQDELNLNLLAAVRLDRALLPGMIARG--SGVIIHVTSI-QRRL 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  79 P-PQSVIHfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCL--------- 148
Cdd:PRK06523  144 PlPESTTA-YAAAKAALSTYSKSLSKEV--APKGVRVNTVSPGWIETEAAVALAERLAEAAGTDYEGAKQIimdslggip 220

                         170
                  ....*....|....*....
gi 1720364755 149 -----RPEDVAEAVIYVLS 162
Cdd:PRK06523  221 lgrpaEPEEVAELIAFLAS 239
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 11-162 1.75e-09

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 55.35  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAGMARPDTLLSGST-SGWKDMFNVNVLALSICTREAYQSMKERNiddGHIININSMC-GHRVPPQSVihfYS 88
Cdd:PRK07890   82 RVDALVNNAFRVPSMKPLADADfAHWRAVIELNVLGTLRLTQAFTPALAESG---GSIVMINSMVlRHSQPKYGA---YK 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  89 ATKYAVTALTEGLRQELleAQTHIRATCISPGL-----VETQFAFKLHDKDP------GEAAATYEHIKCLRPEDVAEAV 157
Cdd:PRK07890  156 MAKGALLAASQSLATEL--GPQGIRVNSVAPGYiwgdpLKGYFRHQAGKYGVtveqiyAETAANSDLKRLPTDDEVASAV 233


                  ....*
gi 1720364755 158 IYVLS 162
Cdd:PRK07890  234 LFLAS 238
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 12-162 1.93e-09

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: 55.16  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPD--------------TLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERniDDGHIININSMCGHR 77
Cdd:cd08935    83 VDILINGAGGNHPDattdpehyepeteqNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQ--KGGSIINISSMNAFS 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  78 vpPQSVIHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHI-------KCLRP 150
Cdd:cd08935   161 --PLTKVPAYSAAKAAVSNFTQWLAVEF--ATTGVRVNAIAPGFFVTPQNRKLLINPDGSYTDRSNKIlgrtpmgRFGKP 236

                         170
                  ....*....|..
gi 1720364755 151 EDVAEAVIYVLS 162
Cdd:cd08935   237 EELLGALLFLAS 248
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
1-137 1.96e-09

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 55.03  E-value: 1.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGM--ARPdtLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIdDGHIININSMCGHRV 78
Cdd:PRK07067   70 IVAAAVERFGGIDILFNNAALfdMAP--ILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGR-GGKIINMASQAGRRG 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720364755  79 PPQSVIhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQ--------FAfKLHDKDPGE 137
Cdd:PRK07067  147 EALVSH--YCATKAAVISYTQSAALAL--IRHGINVNAIAPGVVDTPmwdqvdalFA-RYENRPPGE 208
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 12-160 2.42e-09

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 54.63  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERniDDGHIININSMCGHRVPPQSVihFYSATK 91
Cdd:PRK12935   85 VDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEA--EEGRIISISSIIGQAGGFGQT--NYSAAK 160

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364755  92 YAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCLRPEDVAEAVIYV 160
Cdd:PRK12935  161 AGMLGFTKSLALEL--AKTNVTVNAICPGFIDTEMVAEVPEEVRQKIVAKIPKKRFGQADEIAKGVVYL 227
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 11-167 2.46e-09

(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: 54.64  E-value: 2.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIddGHIININSMCGhrvppqsvIH--F-- 86
Cdd:cd05353    88 RVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKF--GRIINTSSAAG--------LYgnFgq 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  87 --YSATKYAVTALTEGLRQELleAQTHIRATCISPG----LVETQFAFKLHDKdpgeaaatyehikcLRPEDVAEAVIYV 160
Cdd:cd05353   158 anYSAAKLGLLGLSNTLAIEG--AKYNITCNTIAPAagsrMTETVMPEDLFDA--------------LKPEYVAPLVLYL 221


                  ....*..
gi 1720364755 161 LSTPPHV 167
Cdd:cd05353   222 CHESCEV 228
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 4-124 6.29e-09

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 53.75  E-value: 6.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMARPD---------------TLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERniDDGHII 68
Cdd:PRK08277   80 QILEDFGPCDILINGAGGNHPKattdnefhelieptkTFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGR--KGGNII 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720364755  69 NINSMCGHRvpPQSVIHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVET 124
Cdd:PRK08277  158 NISSMNAFT--PLTKVPAYSAAKAAISNFTQWLAVHF--AKVGIRVNAIAPGFFLT 209
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-162 7.83e-09

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 53.25  E-value: 7.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMK-ERNiddGHIININSMCGHRVP 79
Cdd:PRK06463   69 SKEVVEKEFGRVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKlSKN---GAIVNIASNAGIGTA 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  80 PQSVIhFYSATKYAVTALTEGLRQELLEAQthIRATCISPGLVETQFAfkLHDKDPGEAAATYEHIKCL-------RPED 152
Cdd:PRK06463  146 AEGTT-FYAITKAGIIILTRRLAFELGKYG--IRVNAVAPGWVETDMT--LSGKSQEEAEKLRELFRNKtvlkttgKPED 220

                         170
                  ....*....|
gi 1720364755 153 VAEAVIYVLS 162
Cdd:PRK06463  221 IANIVLFLAS 230
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 2-127 1.07e-08

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 53.12  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRS--QHSG-VDICINNAGmarpdTLLSG-----STSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSM 73
Cdd:PRK08263   65 FAAVETavEHFGrLDIVVNNAG-----YGLFGmieevTESEARAQIDTNFFGALWVTQAVLPYLREQR--SGHIIQISSI 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720364755  74 CGHRVPPQSVIhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFA 127
Cdd:PRK08263  138 GGISAFPMSGI--YHASKWALEGMSEALAQEV--AEFGIKVTLVEPGGYSTDWA 187
PRK06114 PRK06114
SDR family oxidoreductase;
12-124 1.41e-08

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 52.48  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPDTLLSGSTSGWKDMFNVNV--LALSiCTREAyQSMKERNidDGHIININSMCG---HRVPPQSviHf 86
Cdd:PRK06114   87 LTLAVNAAGIANANPAEEMEEEQWQTVMDINLtgVFLS-CQAEA-RAMLENG--GGSIVNIASMSGiivNRGLLQA--H- 159

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1720364755  87 YSATKYAVTALTEGLRQELleAQTHIRATCISPGLVET 124
Cdd:PRK06114  160 YNASKAGVIHLSKSLAMEW--VGRGIRVNSISPGYTAT 195
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 1-165 1.66e-08

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


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 52.39  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIdDGHIININSMCGHRVPP 80
Cdd:cd08943    67 AFEQAVLEFGGLDIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGI-GGNIVFNASKNAVAPGP 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIhfYSATKYAVTALtegLRQELLE-AQTHIRATCISP-GLVETQFAF-----KLHDKDPGEAAATYEHIKCLR---- 149
Cdd:cd08943   146 NAAA--YSAAKAAEAHL---ARCLALEgGEDGIRVNTVNPdAVFRGSKIWegvwrAARAKAYGLLEEEYRTRNLLKrevl 220

                         170
                  ....*....|....*.
gi 1720364755 150 PEDVAEAViYVLSTPP 165
Cdd:cd08943   221 PEDVAEAV-VAMASED 235
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 13-164 2.23e-08

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: 51.36  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  13 DICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIddGHIININSMCGHR-VPPQSVihfYSATK 91
Cdd:cd02266    33 DVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRL--GRFILISSVAGLFgAPGLGG---YAASK 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720364755  92 YAVTALTEGLRQELLEAQTHIRATCISPglVETQFAFKLHDkDPGEAAATYEHI-KCLRPEDVAEAVIYVLSTP 164
Cdd:cd02266   108 AALDGLAQQWASEGWGNGLPATAVACGT--WAGSGMAKGPV-APEEILGNRRHGvRTMPPEEVARALLNALDRP 178
PLN02253 PLN02253
xanthoxin dehydrogenase
 12-162 2.38e-08

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 52.13  E-value: 2.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPDT--LLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMcghrvppQSVI----- 84
Cdd:PLN02253   95 LDIMVNNAGLTGPPCpdIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLK--KGSIVSLCSV-------ASAIgglgp 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  85 HFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFK-LHDKDPGEAA-----------ATYEHIKcLRPED 152
Cdd:PLN02253  166 HAYTGSKHAVLGLTRSVAAEL--GKHGIRVNCVSPYAVPTALALAhLPEDERTEDAlagfrafagknANLKGVE-LTVDD 242

                         170
                  ....*....|
gi 1720364755 153 VAEAVIYVLS 162
Cdd:PLN02253  243 VANAVLFLAS 252
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
12-127 2.47e-08

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 52.11  E-value: 2.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRV--PPQSVihfYSA 89
Cdd:PRK08226   83 IDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARK--DGRIVMMSSVTGDMVadPGETA---YAL 157

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1720364755  90 TKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFA 127
Cdd:PRK08226  158 TKAAIVGLTKSLAVEY--AQSGIRVNAICPGYVRTPMA 193
PRK06949 PRK06949
SDR family oxidoreductase;
12-137 2.68e-08

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 51.69  E-value: 2.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIDDGH------IININSMCGHRVPPQsvIH 85
Cdd:PRK06949   87 IDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKGAGNtkpggrIINIASVAGLRVLPQ--IG 164

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720364755  86 FYSATKYAVTALTEGLRQELLEAQTHIRATCisPGLVETQFAFKLHDKDPGE 137
Cdd:PRK06949  165 LYCMSKAAVVHMTRAMALEWGRHGINVNAIC--PGYIDTEINHHHWETEQGQ 214
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 7-124 3.02e-08

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: 51.68  E-value: 3.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   7 SQHSG--VDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQSVI 84
Cdd:cd05329    78 ASHFGgkLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASG--NGNIVFISSVAGVIAVPSGAP 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1720364755  85 hfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVET 124
Cdd:cd05329   156 --YGATKGALNQLTRSLACEW--AKDNIRVNAVAPWVIAT 191
PRK12742 PRK12742
SDR family oxidoreductase;
1-162 3.67e-08

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 51.30  E-value: 3.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRsQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKerniDDGHIININSMCGHRVPP 80
Cdd:PRK12742   66 VIDVVR-KSGALDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHASVEAARQMP----EGGRIIIIGSVNGDRMPV 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIHfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETqfafklhDKDPGEAA---------ATYEHIkclRPE 151
Cdd:PRK12742  141 AGMAA-YAASKSALQGMARGLARDF--GPRGITINVVQPGPIDT-------DANPANGPmkdmmhsfmAIKRHG---RPE 207

                         170
                  ....*....|.
gi 1720364755 152 DVAEAVIYVLS 162
Cdd:PRK12742  208 EVAGMVAWLAG 218
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 1-142 3.69e-08

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


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 51.68  E-value: 3.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSG-VDICINNAgMARPDTLLSGSTSG--------WKDMFNVNVLALSICTREAYQSMKERNidDGHIININ 71
Cdd:cd09763    71 LFERVAREQQGrLDILVNNA-YAAVQLILVGVAKPfweepptiWDDINNVGLRAHYACSVYAAPLMVKAG--KGLIVIIS 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720364755  72 SMCG----HRVPpqsvihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATY 142
Cdd:cd09763   148 STGGleylFNVA-------YGVGKAAIDRMAADMAHEL--KPHGVAVVSLWPGFVRTELVLEMPEDDEGSWHAKE 213
PRK06398 PRK06398
aldose dehydrogenase; Validated
 5-162 4.52e-08

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 51.37  E-value: 4.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   5 VRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKErnIDDGHIININSMcghrvppQSVI 84
Cdd:PRK06398   66 VISKYGRIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLK--QDKGVIINIASV-------QSFA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  85 -----HFYSATKYAVTALTeglRQELLEAQTHIRATCISPGLVETQFAFKLHDKDPGEAAatyEHI-------------- 145
Cdd:PRK06398  137 vtrnaAAYVTSKHAVLGLT---RSIAVDYAPTIRCVAVCPGSIRTPLLEWAAELEVGKDP---EHVerkirewgemhpmk 210

                         170
                  ....*....|....*..
gi 1720364755 146 KCLRPEDVAEAVIYVLS 162
Cdd:PRK06398  211 RVGKPEEVAYVVAFLAS 227
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 1-162 5.25e-08

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 51.19  E-value: 5.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIdDGHIININSMCG----- 75
Cdd:PRK12384   71 LSRGVDEIFGRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGI-QGRIIQINSKSGkvgsk 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  76 HRVPpqsvihfYSATKYAVTALTEGLRQELLEAQTHIRATCI-----SP---GLVEtQFAFKLH-----------DKDPG 136
Cdd:PRK12384  150 HNSG-------YSAAKFGGVGLTQSLALDLAEYGITVHSLMLgnllkSPmfqSLLP-QYAKKLGikpdeveqyyiDKVPL 221

                         170       180
                  ....*....|....*....|....*.
gi 1720364755 137 EAAATYehikclrpEDVAEAVIYVLS 162
Cdd:PRK12384  222 KRGCDY--------QDVLNMLLFYAS 239
PRK05866 PRK05866
SDR family oxidoreductase;
5-124 6.62e-08

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 50.90  E-value: 6.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   5 VRSQHSGVDICINNAGMA--RPdtlLSGSTSGWKDM---FNVNVLALSICTREAYQSMKERNidDGHIININSMcghRVP 79
Cdd:PRK05866  111 VEKRIGGVDILINNAGRSirRP---LAESLDRWHDVertMVLNYYAPLRLIRGLAPGMLERG--DGHIINVATW---GVL 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1720364755  80 PQSVIHF--YSATKYAVTALTEGLRQELLEAQTHirATCISPGLVET 124
Cdd:PRK05866  183 SEASPLFsvYNASKAALSAVSRVIETEWGDRGVH--STTLYYPLVAT 227
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 3-125 7.20e-08

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: 50.69  E-value: 7.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   3 SAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNiDDGHIININSMCGHRvpPQS 82
Cdd:cd05363    69 AALVDRWGSIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQG-RGGKIINMASQAGRR--GEA 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720364755  83 VIHFYSATKYAVTALTEGLRQELLEAQTHIRAtcISPGLVETQ 125
Cdd:cd05363   146 LVGVYCATKAAVISLTQSAGLNLIRHGINVNA--IAPGVVDGE 186
PRK09291 PRK09291
SDR family oxidoreductase;
12-161 1.00e-07

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 50.00  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQSVIhfYSATK 91
Cdd:PRK09291   74 VDVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARG--KGKVVFTSSMAGLITGPFTGA--YCASK 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364755  92 YAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDK-----DPGEAAATYEHIKCLR----PEDVAEAVIYVL 161
Cdd:PRK09291  150 HALEAIAEAMHAEL--KPFGIQVATVNPGPYLTGFNDTMAETpkrwyDPARNFTDPEDLAFPLeqfdPQEMIDAMVEVI 226
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 2-164 1.17e-07

dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an NAD-binding protein related to the SDRs. It converts dihydrobiopterin into tetrahydrobiopterin, a cofactor necessary in catecholamines synthesis. Dihydropteridine reductase has the YXXXK of these tyrosine-dependent oxidoreductases, but lacks the typical upstream Asn and Ser catalytic residues. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in 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: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 49.63  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARPDTLLSGST-SGWKDMFNVNVLALSICTREAYQSMKErnidDGHIININSMCGHRvPP 80
Cdd:cd05334    59 VASVARLSGKVDALICVAGGWAGGSAKSKSFvKNWDLMWKQNLWTSFIASHLATKHLLS----GGLLVLTGAKAALE-PT 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIHfYSATKYAVTALTEGLRQELLEAQTHIRATCISPGLVETqfafklhdkdPG--EAAATYEHIKCLRPEDVAEaVI 158
Cdd:cd05334   134 PGMIG-YGAAKAAVHQLTQSLAAENSGLPAGSTANAILPVTLDT----------PAnrKAMPDADFSSWTPLEFIAE-LI 201


                  ....*.
gi 1720364755 159 YVLSTP 164
Cdd:cd05334   202 LFWASG 207
PRK05993 PRK05993
SDR family oxidoreductase;
12-127 1.36e-07

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 50.03  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGhrVPPQSVIHFYSATK 91
Cdd:PRK05993   77 LDALFNNGAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQG--QGRIVQCSSILG--LVPMKYRGAYNASK 152

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1720364755  92 YAVTALTEGLRQELleAQTHIRATCISPGLVETQFA 127
Cdd:PRK05993  153 FAIEGLSLTLRMEL--QGSGIHVSLIEPGPIETRFR 186
PRK09135 PRK09135
pteridine reductase; Provisional
 3-167 1.78e-07

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 49.54  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   3 SAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNiddGHIININSMCGHRVPPQS 82
Cdd:PRK09135   77 AACVAAFGRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQR---GAIVNITDIHAERPLKGY 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  83 VIhfYSATKYAVTALTEGLRQELleaQTHIRATCISPGLV---ETQFAFklhdkDPGEAAATYEHIKCLR---PEDVAEA 156
Cdd:PRK09135  154 PV--YCAAKAALEMLTRSLALEL---APEVRVNAVAPGAIlwpEDGNSF-----DEEARQAILARTPLKRigtPEDIAEA 223

                         170
                  ....*....|.
gi 1720364755 157 VIYVLSTPPHV 167
Cdd:PRK09135  224 VRFLLADASFI 234
PRK07062 PRK07062
SDR family oxidoreductase;
4-162 2.39e-07

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 49.27  E-value: 2.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTReAYQSMKERNiDDGHIININSMCGHRVPPQSV 83
Cdd:PRK07062   80 AVEARFGGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTR-AFLPLLRAS-AAASIVCVNSLLALQPEPHMV 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  84 IhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVET-QFAFKLHDK-DPGE-------AAATYEHIKCLR---PE 151
Cdd:PRK07062  158 A--TSAARAGLLNLVKSLATEL--APKGVRVNSILLGLVESgQWRRRYEARaDPGQsweawtaALARKKGIPLGRlgrPD 233

                         170
                  ....*....|.
gi 1720364755 152 DVAEAVIYVLS 162
Cdd:PRK07062  234 EAARALFFLAS 244
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 1-162 2.44e-07

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


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 48.87  E-value: 2.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGmarPDTLLSGST------SGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMC 74
Cdd:cd08930    70 LIESYLEKFGRIDILINNAY---PSPKVWGSRfeefpyEQWNEVLNVNLGGAFLCSQAFIKLFKKQG--KGSIINIASIY 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  75 GHRVPPQ----------SVIhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVetqfafklHDKDPGEAAATYEH 144
Cdd:cd08930   145 GVIAPDFriyentqmysPVE--YSVIKAGIIHLTKYLAKYY--ADTGIRVNAISPGGI--------LNNQPSEFLEKYTK 212

                         170       180
                  ....*....|....*....|...
gi 1720364755 145 iKC-----LRPEDVAEAVIYVLS 162
Cdd:cd08930   213 -KCplkrmLNPEDLRGAIIFLLS 234
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 1-120 2.79e-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: 49.00  E-value: 2.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIdDGHIININSMCGhRVPP 80
Cdd:cd05322    70 LSKGVDEIFKRVDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGI-QGRIIQINSKSG-KVGS 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720364755  81 QsviH--FYSATKYAVTALTEGLRQELleAQTHIRATCISPG 120
Cdd:cd05322   148 K---HnsGYSAAKFGGVGLTQSLALDL--AEHGITVNSLMLG 184
PRK07775 PRK07775
SDR family oxidoreductase;
3-176 4.56e-07

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 48.21  E-value: 4.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   3 SAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQS 82
Cdd:PRK07775   79 AQAEEALGEIEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERR--RGDLIFVGSDVALRQRPHM 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  83 viHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATY------EHIKCLRPEDVAEA 156
Cdd:PRK07775  157 --GAYGAAKAGLEAMVTNLQMEL--EGTGVRASIVHPGPTLTGMGWSLPAEVIGPMLEDWakwgqaRHDYFLRASDLARA 232

                         170       180
                  ....*....|....*....|
gi 1720364755 157 VIYVLSTPPHVQVGDIQMRP 176
Cdd:PRK07775  233 ITFVAETPRGAHVVNMEVQP 252
PRK06500 PRK06500
SDR family oxidoreductase;
4-162 4.78e-07

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 48.03  E-value: 4.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVlalsictREAY---QSMKERNIDDGHIININSMCGHRVPP 80
Cdd:PRK06500   73 ALAEAFGRLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNV-------KGPYfliQALLPLLANPASIVLNGSINAHIGMP 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  81 QSVIhfYSATKYAVTALTEGLRQELLEaqTHIRATCISPGLVETqfafKLHDK---DPGEAAATYEHIKCL-------RP 150
Cdd:PRK06500  146 NSSV--YAASKAALLSLAKTLSGELLP--RGIRVNAVSPGPVQT----PLYGKlglPEATLDAVAAQIQALvplgrfgTP 217

                         170
                  ....*....|..
gi 1720364755 151 EDVAEAVIYVLS 162
Cdd:PRK06500  218 EEIAKAVLYLAS 229
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 11-162 5.33e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 48.00  E-value: 5.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAGMARPDTLLSG-STSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRV--PPQSVihfY 87
Cdd:PRK07478   83 GLDIAFNNAGTLGEMGPVAEmSLEGWRETLATNLTSAFLGAKHQIPAMLARG--GGSLIFTSTFVGHTAgfPGMAA---Y 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  88 SATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAfklhdKDPGEAAATYEHIKCL-------RPEDVAEAVIYV 160
Cdd:PRK07478  158 AASKAGLIGLTQVLAAEY--GAQGIRVNALLPGGTDTPMG-----RAMGDTPEALAFVAGLhalkrmaQPEEIAQAALFL 230


                  ..
gi 1720364755 161 LS 162
Cdd:PRK07478  231 AS 232
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 1-125 6.34e-07

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 47.75  E-value: 6.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGhRVPP 80
Cdd:PRK07097   77 MVSQIEKEVGVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKG--HGKIINICSMMS-ELGR 153

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720364755  81 QSVIHfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQ 125
Cdd:PRK07097  154 ETVSA-YAAAKGGLKMLTKNIASEY--GEANIQCNGIGPGYIATP 195
PRK07831 PRK07831
SDR family oxidoreductase;
1-121 8.52e-07

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 47.72  E-value: 8.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNiDDGHIININSMCGHRVpp 80
Cdd:PRK07831   87 LIDAAVERLGRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARG-HGGVIVNNASVLGWRA-- 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720364755  81 QSVIHFYSATKYAVTALTeglRQELLEAQTH-IRATCISPGL 121
Cdd:PRK07831  164 QHGQAHYAAAKAGVMALT---RCSALEAAEYgVRINAVAPSI 202
PRK09072 PRK09072
SDR family oxidoreductase;
4-158 8.60e-07

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 47.63  E-value: 8.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERniDDGHIININSMCGH-RVPPQS 82
Cdd:PRK09072   73 ARAREMGGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQ--PSAMVVNVGSTFGSiGYPGYA 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  83 VihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFafklhdkdpgEAAATYEHIKCL-----RPEDVAEAV 157
Cdd:PRK09072  151 S---YCASKFALRGFSEALRREL--ADTGVRVLYLAPRATRTAM----------NSEAVQALNRALgnamdDPEDVAAAV 215


                  .
gi 1720364755 158 I 158
Cdd:PRK09072  216 L 216
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 1-136 8.79e-07

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: 47.30  E-value: 8.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDM--FNVNVLALSICTREAYQSMKERNidDGHIININSmcGHRV 78
Cdd:cd05370    68 LAEALLSEYPNLDILINNAGIQRPIDLRDPASDLDKADteIDTNLIGPIRLIKAFLPHLKKQP--EATIVNVSS--GLAF 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364755  79 PPQSVIHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPG 136
Cdd:cd05370   144 VPMAANPVYCATKAALHSYTLALRHQL--KDTGVEVVEIVPPAVDTELHEERRNPDGG 199
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
11-162 1.78e-06

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 47.15  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIdDGHIININSMCGHRVPPQSVIhfYSAT 90
Cdd:PRK08324  498 GVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGL-GGSIVFIASKNAVNPGPNFGA--YGAA 574

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  91 KYAVTALTeglRQELLE-AQTHIRATCISP-------GLVETQF------AFKLhdkDPGEAAATYEHIKCLR----PED 152
Cdd:PRK08324  575 KAAELHLV---RQLALElGPDGIRVNGVNPdavvrgsGIWTGEWiearaaAYGL---SEEELEEFYRARNLLKrevtPED 648

                         170
                  ....*....|
gi 1720364755 153 VAEAVIYVLS 162
Cdd:PRK08324  649 VAEAVVFLAS 658
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 2-176 2.10e-06

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: 46.22  E-value: 2.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQ 81
Cdd:cd05373    68 FDLIEEEIGPLEVLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARG--RGTIIFTGATASLRGRAG 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  82 SVIhfYSATKYAVTALTEGLRQELLEAQTHIrATCISPGLVETQFaFKLHDKDPGEAAatyEHIKCLRPEDVAEAVIYVL 161
Cdd:cd05373   146 FAA--FAGAKFALRALAQSMARELGPKGIHV-AHVIIDGGIDTDF-IRERFPKRDERK---EEDGILDPDAIAEAYWQLH 218

                         170
                  ....*....|....*
gi 1720364755 162 STPPHVQVGDIQMRP 176
Cdd:cd05373   219 TQPRSAWTHELDLRP 233
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 12-161 2.23e-06

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: 46.03  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPDTLLSGSTSG-WKDMFNVNVLALSICTREAYQSMKERniDDGHIININSMCGHRvpPQSVIHFYSAT 90
Cdd:cd05340    85 LDGVLHNAGLLGDVCPLSEQNPQvWQDV*QVNVNATFMLTQALLPLLLKS--DAGSLVFTSSSVGRQ--GRANWGAYAVS 160

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720364755  91 KYAvtalTEGLRQELLE--AQTHIRATCISPGLVETQFAFKLHdkdPGEaaatyEHIKCLRPEDVAEAVIYVL 161
Cdd:cd05340   161 KFA----TEGL*QVLADeyQQRNLRVNCINPGGTRTAMRASAF---PTE-----DPQKLKTPADIMPLYLWLM 221
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 3-162 2.59e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 46.16  E-value: 2.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   3 SAVRSQHSGVDICINNAGMARPDTLLSgSTSGWKDMFNVNVLALSICTREAYQSMKERNiddGHIININSMCGHRVppQS 82
Cdd:PRK08265   72 ATVVARFGRVDILVNLACTYLDDGLAS-SRADWLAALDVNLVSAAMLAQAAHPHLARGG---GAIVNFTSISAKFA--QT 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  83 VIHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEA---AATYEHIKCL-RPEDVAEAVI 158
Cdd:PRK08265  146 GRWLYPASKAAIRQLTRSMAMDL--APDGIRVNSVSPGWTWSRVMDELSGGDRAKAdrvAAPFHLLGRVgDPEEVAQVVA 223


                  ....
gi 1720364755 159 YVLS 162
Cdd:PRK08265  224 FLCS 227
PRK07832 PRK07832
SDR family oxidoreductase;
2-124 3.14e-06

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 45.80  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSA-VRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLAlSICTREAYQSMKERNIDDGHIININSMCGHRVPP 80
Cdd:PRK07832   68 FAAdIHAAHGSMDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMG-PIHVIETFVPPMVAAGRGGHLVNVSSAAGLVALP 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720364755  81 QsviHF-YSATKYAVTALTEGLRQELleAQTHIRATCISPGLVET 124
Cdd:PRK07832  147 W---HAaYSASKFGLRGLSEVLRFDL--ARHGIGVSVVVPGAVKT 186
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 1-157 4.39e-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: 45.53  E-value: 4.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMA---RPDtLLSGSTSGWKDMFNVNVLALSICTREAYQSMKER----NIDDGHIININSM 73
Cdd:cd05337    69 LLDQAWEDFGRLDCLVNNAGIAvrpRGD-LLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQpdrfDGPHRSIIFVTSI 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  74 CGHRVPPQSVIhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCL-RPED 152
Cdd:cd05337   148 NAYLVSPNRGE--YCISKAGLSMATRLLAYRL--ADEGIAVHEIRPGLIHTDMTAPVKEKYDELIAAGLVPIRRWgQPED 223


                  ....*
gi 1720364755 153 VAEAV 157
Cdd:cd05337   224 IAKAV 228
PRK08017 PRK08017
SDR family oxidoreductase;
64-164 4.75e-06

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 45.46  E-value: 4.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  64 DGHIININSMCGHRVPPQSVIhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLH----DK---DPG 136
Cdd:PRK08017  125 EGRIVMTSSVMGLISTPGRGA--YAASKYALEAWSDALRMEL--RHSGIKVSLIEPGPIRTRFTDNVNqtqsDKpveNPG 200

                          90       100
                  ....*....|....*....|....*...
gi 1720364755 137 EAAATyehikCLRPEDVAEAVIYVLSTP 164
Cdd:PRK08017  201 IAARF-----TLGPEAVVPKLRHALESP 223
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 11-120 5.44e-06

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 45.32  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTRE-AYQSMKERNidDGHIININSMCGHRVPPQSVIHF--Y 87
Cdd:PRK08213   89 HVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAvAKRSMIPRG--YGRIINVASVAGLGGNPPEVMDTiaY 166

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1720364755  88 SATKYAVTALTEGLRQELleAQTHIRATCISPG 120
Cdd:PRK08213  167 NTSKGAVINFTRALAAEW--GPHGIRVNAIAPG 197
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 4-124 1.02e-05

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 44.37  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQsv 83
Cdd:PRK07523   80 AFEAEIGPIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARG--AGKIINIASVQSALARPG-- 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1720364755  84 IHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVET 124
Cdd:PRK07523  156 IAPYTATKGAVGNLTKGMATDW--AKHGLQCNAIAPGYFDT 194
PRK08589 PRK08589
SDR family oxidoreductase;
3-162 1.06e-05

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 44.38  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   3 SAVRSQHSGVDICINNAGMarpDT----LLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNiddGHIININSMCG--- 75
Cdd:PRK08589   74 SEIKEQFGRVDVLFNNAGV---DNaagrIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQG---GSIINTSSFSGqaa 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  76 --HRVPpqsvihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATY-EHIKCL---- 148
Cdd:PRK08589  148 dlYRSG-------YNAAKGAVINFTKSIAIEY--GRDGIRANAIAPGTIETPLVDKLTGTSEDEAGKTFrENQKWMtplg 218

                         170
                  ....*....|....*..
gi 1720364755 149 ---RPEDVAEAVIYVLS 162
Cdd:PRK08589  219 rlgKPEEVAKLVVFLAS 235
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 12-162 1.30e-05

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: 44.05  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGM-ARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIddGHIININSMCGHR-VPPQSVihfYSA 89
Cdd:cd05330    83 IDGFFNNAGIeGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGS--GMIVNTASVGGIRgVGNQSG---YAA 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  90 TKYAVTALTeglRQELLE-AQTHIRATCISPGLVETQF---AFK-LHDKDPGEAAATYEHIKCLR----PEDVAEAVIYV 160
Cdd:cd05330   158 AKHGVVGLT---RNSAVEyGQYGIRINAIAPGAILTPMvegSLKqLGPENPEEAGEEFVSVNPMKrfgePEEVAAVVAFL 234


                  ..
gi 1720364755 161 LS 162
Cdd:cd05330   235 LS 236
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 3-124 1.37e-05

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 44.06  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   3 SAVRSQHSGVDICINNAG---MARPdtLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMC---GH 76
Cdd:cd08937    72 RAAVERFGRVDVLINNVGgtiWAKP--YEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQ--QGVIVNVSSIAtrgIY 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1720364755  77 RVPpqsvihfYSATKYAVTALTEGLRQEllEAQTHIRATCISPGLVET 124
Cdd:cd08937   148 RIP-------YSAAKGGVNALTASLAFE--HARDGIRVNAVAPGGTEA 186
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-125 2.07e-05

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 43.67  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERniDDGHIININSM---CGHRvpP 80
Cdd:PRK08261  277 HLAERHGGLDIVVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEALLAAGALG--DGGRIVGVSSIsgiAGNR--G 352

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720364755  81 QSVihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQ 125
Cdd:PRK08261  353 QTN---YAASKAGVIGLVQALAPLL--AERGITINAVAPGFIETQ 392
PRK07102 PRK07102
SDR family oxidoreductase;
39-157 3.09e-05

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 42.99  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  39 FNVNVLA-LSICTREAyQSMKERNidDGHIININSMCGHRVPPQSviHFYSATKYAVTALTEGLRQELLEAQTHIRAtcI 117
Cdd:PRK07102  104 FRTNFEGpIALLTLLA-NRFEARG--SGTIVGISSVAGDRGRASN--YVYGSAKAALTAFLSGLRNRLFKSGVHVLT--V 176

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720364755 118 SPGLVETQF--AFKLhdkdPGEAAATyehikclrPEDVAEAV 157
Cdd:PRK07102  177 KPGFVRTPMtaGLKL----PGPLTAQ--------PEEVAKDI 206
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 2-164 3.22e-05

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: 43.05  E-value: 3.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMA-----------RPDTL----------LSGStsgwkdmFNVNVLALSICTREAYQSMKER 60
Cdd:cd05371    66 LALAKAKFGRLDIVVNCAGIAvaaktynkkgqQPHSLelfqrvinvnLIGT-------FNVIRLAAGAMGKNEPDQGGER 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  61 niddGHIININSMCGHRVPPQSVIhfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAA 140
Cdd:cd05371   139 ----GVIINTASVAAFEGQIGQAA--YSASKGGIVGMTLPIARDL--APQGIRVVTIAPGLFDTPLLAGLPEKVRDFLAK 210

                         170       180
                  ....*....|....*....|....*
gi 1720364755 141 TYEHIKCL-RPEDVAEAVIYVLSTP 164
Cdd:cd05371   211 QVPFPSRLgDPAEYAHLVQHIIENP 235
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 1-161 4.24e-05

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: 42.66  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLS-GSTSGWKDMFNVNVLALSICTREAYQSMKERNIdDGHIININSMCGHRVP 79
Cdd:cd05367    67 LLEAIRKLDGERDLLINNAGSLGPVSKIEfIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGL-KKTVVNVSSGAAVNPF 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  80 PQSVIhfYSATKYAVTALTEGLRQELLEaqthIRATCISPGLVET--QFAFKLHDKDPgEAAATY----EHIKCLRPEDV 153
Cdd:cd05367   146 KGWGL--YCSSKAARDMFFRVLAAEEPD----VRVLSYAPGVVDTdmQREIRETSADP-ETRSRFrslkEKGELLDPEQS 218


                  ....*...
gi 1720364755 154 AEAVIYVL 161
Cdd:cd05367   219 AEKLANLL 226
PRK09134 PRK09134
SDR family oxidoreductase;
12-164 4.27e-05

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 42.61  E-value: 4.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  12 VDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTRE-AYQSMKERnidDGHIINinsMCGHRV----PpqsviHF 86
Cdd:PRK09134   88 ITLLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAfARALPADA---RGLVVN---MIDQRVwnlnP-----DF 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  87 YSAT--KYAVTALTEGLRQELLEAqthIRATCISPGLV-------ETQFAfKLHDKDPGEAAATyehikclrPEDVAEAV 157
Cdd:PRK09134  157 LSYTlsKAALWTATRTLAQALAPR---IRVNAIGPGPTlpsgrqsPEDFA-RQHAATPLGRGST--------PEEIAAAV 224


                  ....*..
gi 1720364755 158 IYVLSTP 164
Cdd:PRK09134  225 RYLLDAP 231
PRK12744 PRK12744
SDR family oxidoreductase;
1-173 6.37e-05

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 42.03  E-value: 6.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNvlalsicTREAYQSMKE--RNIDD-GHIINI-NSMCGH 76
Cdd:PRK12744   79 LFDDAKAAFGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVN-------SKSAFFFIKEagRHLNDnGKIVTLvTSLLGA 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  77 RVPpqsvihFYSA---TKYAVTALTEGLRQELLEAQthIRATCISPGLVETQFAFklhdkdpgeaaatyehikclrPEDV 153
Cdd:PRK12744  152 FTP------FYSAyagSKAPVEHFTRAASKEFGARG--ISVTAVGPGPMDTPFFY---------------------PQEG 202

                         170       180
                  ....*....|....*....|....*
gi 1720364755 154 AEAVIY-----VLSTPPHVQVGDIQ 173
Cdd:PRK12744  203 AEAVAYhktaaALSPFSKTGLTDIE 227
PRK08278 PRK08278
SDR family oxidoreductase;
11-165 8.84e-05

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 41.81  E-value: 8.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERniDDGHIININ---SMCGHRVPPQSVihfY 87
Cdd:PRK08278   90 GIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKS--ENPHILTLSpplNLDPKWFAPHTA---Y 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  88 SATKYAVTALTEGLRQELLEAQthIRATCISP-GLVET---QFAFklhdkdPGEAAATyehiKCLRPEDVAEAVIYVLST 163
Cdd:PRK08278  165 TMAKYGMSLCTLGLAEEFRDDG--IAVNALWPrTTIATaavRNLL------GGDEAMR----RSRTPEIMADAAYEILSR 232


                  ..
gi 1720364755 164 PP 165
Cdd:PRK08278  233 PA 234
PRK07985 PRK07985
SDR family oxidoreductase;
11-162 1.01e-04

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 41.52  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAG--MARPDtLLSGSTSGWKDMFNVNVLALSICTREAYQSMKErnidDGHIININSMCGHRVPPQsvIHFYS 88
Cdd:PRK07985  128 GLDIMALVAGkqVAIPD-IADLTSEQFQKTFAINVFALFWLTQEAIPLLPK----GASIITTSSIQAYQPSPH--LLDYA 200

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364755  89 ATKYAVTALTEGLRQELleAQTHIRATCISPGLVETqfAFKLHDKDPGEAAATYEHIKCLR----PEDVAEAVIYVLS 162
Cdd:PRK07985  201 ATKAAILNYSRGLAKQV--AEKGIRVNIVAPGPIWT--ALQISGGQTQDKIPQFGQQTPMKragqPAELAPVYVYLAS 274
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 10-140 1.04e-04

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: 41.51  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  10 SGVDICINNAGMARPDTLLSG-STSGWKDMFNVNVLALSICTREAYQSMKERNIddGHIININSMCGH---RVPPQSVIh 85
Cdd:cd05325    74 AGLDVLINNAGILHSYGPASEvDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGAR--AKIINISSRVGSigdNTSGGWYS- 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364755  86 fYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVET----QFAFKLHDKDPGEAAA 140
Cdd:cd05325   151 -YRASKAALNMLTKSLAVEL--KRDGITVVSLHPGWVRTdmggPFAKNKGPITPEESVA 206
PRK07041 PRK07041
SDR family oxidoreductase;
76-164 1.43e-04

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 40.79  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  76 HRVPPQSVIhfYSATKYAVTALTEGLRQELleaqTHIRATCISPGLVETQfafkLHDKDPGEA-AATYEHI-------KC 147
Cdd:PRK07041  128 VRPSASGVL--QGAINAALEALARGLALEL----APVRVNTVSPGLVDTP----LWSKLAGDArEAMFAAAaerlparRV 197

                          90
                  ....*....|....*..
gi 1720364755 148 LRPEDVAEAVIYVLSTP 164
Cdd:PRK07041  198 GQPEDVANAILFLAANG 214
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 6-162 1.78e-04

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 40.83  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   6 RSQHSGVDICINNAGMArPDTLLSGSTSGWKD-MFNVNVLALSICTREAYQSMKerniDDGHIININSMCGHRVPPQSVI 84
Cdd:PRK12747   83 RTGSTKFDILINNAGIG-PGAFIEETTEQFFDrMVSVNAKAPFFIIQQALSRLR----DNSRIINISSAATRISLPDFIA 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  85 hfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQF-AFKLHDKDPGEAAATYEHIKCL-RPEDVAEAVIYVLS 162
Cdd:PRK12747  158 --YSMTKGAINTMTFTLAKQL--GARGITVNAILPGFIKTDMnAELLSDPMMKQYATTISAFNRLgEVEDIADTAAFLAS 233
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 7-162 2.68e-04

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: 40.25  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   7 SQHSGVDICINNAGMARP---DTLLSGSTSGWkdMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQsv 83
Cdd:cd05365    72 SQFGGITILVNNAGGGGPkpfDMPMTEEDFEW--AFKLNLFSAFRLSQLCAPHMQKAG--GGAILNISSMSSENKNVR-- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  84 IHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCL-RPEDVAEAVIYVLS 162
Cdd:cd05365   146 IAAYGSSKAAVNHMTRNLAFDL--GPKGIRVNAVAPGAVKTDALASVLTPEIERAMLKHTPLGRLgEPEDIANAALFLCS 223
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 11-125 2.84e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 40.03  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSMCGHRVPPQSVIHfySAT 90
Cdd:PRK06125   81 DIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARG--SGVIVNVIGAAGENPDADYICG--SAG 156

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1720364755  91 KYAVTALTEGLRQELLEAqtHIRATCISPGLVETQ 125
Cdd:PRK06125  157 NAALMAFTRALGGKSLDD--GVRVVGVNPGPVATD 189
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 11-164 3.48e-04

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 40.15  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  11 GVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREA--YQSMKERNIDD---GHIININSMCGHRVP---PQs 82
Cdd:PRK07792   89 GLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAaaYWRAKAKAAGGpvyGRIVNTSSEAGLVGPvgqAN- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  83 vihfYSATKYAVTALTEGLRQELleAQTHIRATCISP----GLVETQFAfklhdkDPGEAAAtyEHIKCLRPEDVAEAVI 158
Cdd:PRK07792  168 ----YGAAKAGITALTLSAARAL--GRYGVRANAICPrartAMTADVFG------DAPDVEA--GGIDPLSPEHVVPLVQ 233


                  ....*.
gi 1720364755 159 YvLSTP 164
Cdd:PRK07792  234 F-LASP 238
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
16-173 3.70e-04

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 39.67  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  16 INNAGMARPDTLLSGSTSgwkDMFN----VNVLALSICTREAYQSMKERNIDDgHIININSMCGHR-VPPQSVihfYSAT 90
Cdd:PRK06924   85 INNAGMVAPIKPIEKAES---EELItnvhLNLLAPMILTSTFMKHTKDWKVDK-RVINISSGAAKNpYFGWSA---YCSS 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  91 KYAVTALTEGLRQELLEAQTHIRATCISPGLVETQFAFKLHD------KDPGEAAATYEHIKCLRPEDVAEAVIYVLST- 163
Cdd:PRK06924  158 KAGLDMFTQTVATEQEEEEYPVKIVAFSPGVMDTNMQAQIRSsskedfTNLDRFITLKEEGKLLSPEYVAKALRNLLETe 237

                         170
                  ....*....|.
gi 1720364755 164 -PPHVQVGDIQ 173
Cdd:PRK06924  238 dFPNGEVIDID 248
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 16-124 6.34e-04

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: 39.18  E-value: 6.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  16 INNAGMARP--DTLLSgSTSGWKDMFNVNVLAlsicTREAYQSM-----KERniddGHIININSMCGhRVPPQsVIHFYS 88
Cdd:cd09805    83 VNNAGILGFggDEELL-PMDDYRKCMEVNLFG----TVEVTKAFlpllrRAK----GRVVNVSSMGG-RVPFP-AGGAYC 151

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1720364755  89 ATKYAVTALTEGLRQELleAQTHIRATCISPGLVET 124
Cdd:cd09805   152 ASKAAVEAFSDSLRREL--QPWGVKVSIIEPGNFKT 185
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 4-164 7.75e-04

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: 38.74  E-value: 7.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMARPDTLLsgSTSGWKDMFNVNVLALSICTREAYQSMKERNidDGHIININSmCGHRVPPQ-- 81
Cdd:cd05327    73 EFLARFPRLDILINNAGIMAPPRRL--TKDGFELQFAVNYLGHFLLTNLLLPVLKASA--PSRIVNVSS-IAHRAGPIdf 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  82 -----------SVIHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFaFKLHDKDPGEAAATYEHIKcLRP 150
Cdd:cd05327   148 ndldlennkeySPYKAYGQSKLANILFTRELARRL--EGTGVTVNALHPGVVRTEL-LRRNGSFFLLYKLLRPFLK-KSP 223

                         170
                  ....*....|....
gi 1720364755 151 EDVAEAVIYVLSTP 164
Cdd:cd05327   224 EQGAQTALYAATSP 237
PRK12746 PRK12746
SDR family oxidoreductase;
5-172 1.44e-03

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 38.09  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   5 VRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKErnidDGHIININSMCGHRVPPQSVI 84
Cdd:PRK12746   84 IRVGTSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRA----EGRVINISSAEVRLGFTGSIA 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755  85 hfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHI--KCLRPEDVAEAVIYVLS 162
Cdd:PRK12746  160 --YGLSKGALNTMTLPLAKHL--GERGITVNTIMPGYTKTDINAKLLDDPEIRNFATNSSVfgRIGQVEDIADAVAFLAS 235

                         170
                  ....*....|
gi 1720364755 163 TPPHVQVGDI 172
Cdd:PRK12746  236 SDSRWVTGQI 245
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-124 2.16e-03

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 37.36  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   2 FSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERniDDGHIININSmcGHRVPPQ 81
Cdd:PRK12748   86 FYAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGK--AGGRIINLTS--GQSLGPM 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720364755  82 SVIHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVET 124
Cdd:PRK12748  162 PDELAYAATKGAIEAFTKSLAPEL--AEKGITVNAVNPGPTDT 202
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 1-123 3.33e-03

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 36.85  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAG---MARP------------------DTLlsgstsgWkdmfnvnvlalsiCTREAYQSMKE 59
Cdd:PRK12823   74 AMAAAVEAFGRIDVLINNVGgtiWAKPfeeyeeeqieaeirrslfPTL-------W-------------CCRAVLPHMLA 133

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720364755  60 RniDDGHIININSMCG---HRVPpqsvihfYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVE 123
Cdd:PRK12823  134 Q--GGGAIVNVSSIATrgiNRVP-------YSAAKGGVNALTASLAFEY--AEHGIRVNAVAPGGTE 189
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-124 4.59e-03

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 36.69  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   1 MFSAVRSQHSGVDICINNAGMARpDTLLSGSTSGWKDM-FNVNVLALSICTRE-AYQSMKERNiddGHIININSmcGHRV 78
Cdd:PRK12859   86 LLNKVTEQLGYPHILVNNAAYST-NNDFSNLTAEELDKhYMVNVRATTLLSSQfARGFDKKSG---GRIINMTS--GQFQ 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720364755  79 PPQSVIHFYSATKYAVTALTEGLRQELleAQTHIRATCISPGLVET 124
Cdd:PRK12859  160 GPMVGELAYAATKGAIDALTSSLAAEV--AHLGITVNAINPGPTDT 203
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 4-105 5.32e-03

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 36.49  E-value: 5.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364755   4 AVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNiddGHIININSMCGHRVPPqsV 83
Cdd:PRK05872   78 EAVERFGGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR---GYVLQVSSLAAFAAAP--G 152

                          90       100
                  ....*....|....*....|..
gi 1720364755  84 IHFYSATKYAVTALTEGLRQEL 105
Cdd:PRK05872  153 MAAYCASKAGVEAFANALRLEV 174
 
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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