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Conserved domains on  [gi|6322779|ref|NP_012852|]
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Osi1p [Saccharomyces cerevisiae S288C]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143154)

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

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0016491
PubMed:  19011750|19011748|12604210|19027726|20423462
SCOP:  4000029

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 9-253 3.40e-87

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: 258.76  E-value: 3.40e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    9 YFIIGGSRGIGFNLVKILSASTGNTVITSIRGSPSLpknKQVEDLAKIRKNIHIVQLDLTKDesIGNIADEIKKTPFFLG 88
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGNNTVIATCRDPSAA---TELAALGASHSRLHILELDVTDE--IAESAEAVAERLGDAG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   89 IDIFIACSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAFVPLSVSAYGQSK 168
Cdd:cd05325  76 LDVLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGSIGDNTSGGWYSYRASK 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779  169 AALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLDHFKeknidisgvnIITPEESASALIDVFRKILPEDNGKFFN 248
Cdd:cd05325 156 AALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAKNKG----------PITPEESVAGLLKVIDNLNEEDSGKFLD 225


                ....*
gi 6322779  249 YDGSE 253
Cdd:cd05325 226 YDGTE 230
 
Name Accession Description Interval E-value
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 9-253 3.40e-87

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: 258.76  E-value: 3.40e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    9 YFIIGGSRGIGFNLVKILSASTGNTVITSIRGSPSLpknKQVEDLAKIRKNIHIVQLDLTKDesIGNIADEIKKTPFFLG 88
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGNNTVIATCRDPSAA---TELAALGASHSRLHILELDVTDE--IAESAEAVAERLGDAG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   89 IDIFIACSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAFVPLSVSAYGQSK 168
Cdd:cd05325  76 LDVLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGSIGDNTSGGWYSYRASK 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779  169 AALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLDHFKeknidisgvnIITPEESASALIDVFRKILPEDNGKFFN 248
Cdd:cd05325 156 AALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAKNKG----------PITPEESVAGLLKVIDNLNEEDSGKFLD 225


                ....*
gi 6322779  249 YDGSE 253
Cdd:cd05325 226 YDGTE 230
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-237 6.37e-35

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 125.37  E-value: 6.37e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    1 MNTSSRiTYFIIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLpkNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEI 80
Cdd:COG0300   1 MSLTGK-TVLITGASSGIGRALARAL-AARGARVVLVARDAERL--EALAAELRAAGARVEVVALDVTDPDAVAALAEAV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   81 KKTpfFLGIDIFIACSAVSDsYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINafVPLS 160
Cdd:COG0300  77 LAR--FGPIDVLVNNAGVGG-GGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRG--LPGM 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322779  161 vSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGqygldhfkEKNIDISGVNIITPEESASALIDVFRK 237
Cdd:COG0300 152 -AAYAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFT--------ARAGAPAGRPLLSPEEVARAILRALER 219
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 10-203 9.10e-28

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 105.00  E-value: 9.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     10 FIIGGSRGIGFNLVKILSASTGNTVITSIRGSPSlpkNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGI 89
Cdd:pfam00106   4 LVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKL---EAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVER--LGRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     90 DIFIACSAVSDSYyKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGsinaFVPL-SVSAYGQSK 168
Cdd:pfam00106  79 DILVNNAGITGLG-PFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAG----LVPYpGGSAYSASK 153

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 6322779    169 AALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQ 203
Cdd:pfam00106 154 AAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTK 188
PRK06953 PRK06953
SDR family oxidoreductase;
8-253 2.57e-25

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 99.38  E-value: 2.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     8 TYFIIGGSRGIGFNLVKILSAStGNTVITSIRGSpslpknkqvEDLAKIRK-NIHIVQLDLTKDESIGNIADEIKKTpff 86
Cdd:PRK06953   3 TVLIVGASRGIGREFVRQYRAD-GWRVIATARDA---------AALAALQAlGAEALALDVADPASVAGLAWKLDGE--- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    87 lGIDIFIACSAVSDSYYKVLETPKSVWLNH-YSTNALGPILALQKVYPLLllKKTRKIF-FISSVAGSINAFVPLSVSAY 164
Cdd:PRK06953  70 -ALDAAVYVAGVYGPRTEGVEPITREDFDAvMHTNVLGPMQLLPILLPLV--EAAGGVLaVLSSRMGSIGDATGTTGWLY 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   165 GQSKAALNYAVKTLSFELKpeGFTVVAFHPGMVSTDMGQYGLDhfkeknidisgvniITPEESASALIDVFRKILPEDNG 244
Cdd:PRK06953 147 RASKAALNDALRAASLQAR--HATCIALHPGWVRTDMGGAQAA--------------LDPAQSVAGMRRVIAQATRRDNG 210


                 ....*....
gi 6322779   245 KFFNYDGSE 253
Cdd:PRK06953 211 RFFQYDGVE 219
 
Name Accession Description Interval E-value
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 9-253 3.40e-87

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: 258.76  E-value: 3.40e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    9 YFIIGGSRGIGFNLVKILSASTGNTVITSIRGSPSLpknKQVEDLAKIRKNIHIVQLDLTKDesIGNIADEIKKTPFFLG 88
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGNNTVIATCRDPSAA---TELAALGASHSRLHILELDVTDE--IAESAEAVAERLGDAG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   89 IDIFIACSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAFVPLSVSAYGQSK 168
Cdd:cd05325  76 LDVLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGSIGDNTSGGWYSYRASK 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779  169 AALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLDHFKeknidisgvnIITPEESASALIDVFRKILPEDNGKFFN 248
Cdd:cd05325 156 AALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAKNKG----------PITPEESVAGLLKVIDNLNEEDSGKFLD 225


                ....*
gi 6322779  249 YDGSE 253
Cdd:cd05325 226 YDGTE 230
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-237 6.37e-35

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 125.37  E-value: 6.37e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    1 MNTSSRiTYFIIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLpkNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEI 80
Cdd:COG0300   1 MSLTGK-TVLITGASSGIGRALARAL-AARGARVVLVARDAERL--EALAAELRAAGARVEVVALDVTDPDAVAALAEAV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   81 KKTpfFLGIDIFIACSAVSDsYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINafVPLS 160
Cdd:COG0300  77 LAR--FGPIDVLVNNAGVGG-GGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRG--LPGM 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322779  161 vSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGqygldhfkEKNIDISGVNIITPEESASALIDVFRK 237
Cdd:COG0300 152 -AAYAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFT--------ARAGAPAGRPLLSPEEVARAILRALER 219
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 10-232 2.62e-34

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


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 123.16  E-value: 2.62e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   10 FIIGGSRGIGFNLVKILSASTGNTVITSIRGSpslpKNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGI 89
Cdd:cd05233   2 LVTGASSGIGRAIARRLAREGAKVVLADRNEE----ALAELAAIEALGGNAVAVQADVSDEEDVEALVEEALEE--FGRL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   90 DIFIACSAVSdSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAFvplSVSAYGQSKA 169
Cdd:cd05233  76 DILVNNAGIA-RPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLP---GQAAYAASKA 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322779  170 ALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLDHFKEKNID--ISGVNIITPEESASALI 232
Cdd:cd05233 152 ALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAaaIPLGRLGTPEEVAEAVV 216
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-230 2.02e-29

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: 111.03  E-value: 2.02e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    1 MNTSSRITYFIIGGSRGIGFNLVKILSASTGNTVITSIRGSPSlpkNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEI 80
Cdd:COG1028   1 MTRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEAL---EAAAAELRAAGGRALAVAADVTDEAAVEALVAAA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   81 KKTpfFLGIDIFIACSAVSDsYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAFvplS 160
Cdd:COG1028  78 VAA--FGRLDILVNNAGITP-PGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSP---G 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322779  161 VSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM--GQYGLDHFKEKNIDISGVN-IITPEESASA 230
Cdd:COG1028 152 QAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMtrALLGAEEVREALAARIPLGrLGTPEEVAAA 224
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 10-248 1.29e-28

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 108.09  E-value: 1.29e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   10 FIIGGSRGIGFNLVKILSASTGNTVITSIRgspSLPKNKQ-VEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLG 88
Cdd:cd05324   4 LVTGANRGIGFEIVRQLAKSGPGTVILTAR---DVERGQAaVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEK--YGG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   89 IDIFIACSAVSdsyYKVLETPKS---VWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINafvplsvSAYG 165
Cdd:cd05324  79 LDILVNNAGIA---FKGFDDSTPtreQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLT-------SAYG 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779  166 QSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQygldHFKEKnidisgvniiTPEESASALidVFRKILPED--- 242
Cdd:cd05324 149 VSKAALNALTRILAKELKETGIKVNACCPGWVKTDMGG----GKAPK----------TPEEGAETP--VYLALLPPDgep 212


                ....*.
gi 6322779  243 NGKFFN 248
Cdd:cd05324 213 TGKFFS 218
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 10-203 9.10e-28

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 105.00  E-value: 9.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     10 FIIGGSRGIGFNLVKILSASTGNTVITSIRGSPSlpkNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGI 89
Cdd:pfam00106   4 LVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKL---EAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVER--LGRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     90 DIFIACSAVSDSYyKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGsinaFVPL-SVSAYGQSK 168
Cdd:pfam00106  79 DILVNNAGITGLG-PFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAG----LVPYpGGSAYSASK 153

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 6322779    169 AALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQ 203
Cdd:pfam00106 154 AAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTK 188
PRK06953 PRK06953
SDR family oxidoreductase;
8-253 2.57e-25

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 99.38  E-value: 2.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     8 TYFIIGGSRGIGFNLVKILSAStGNTVITSIRGSpslpknkqvEDLAKIRK-NIHIVQLDLTKDESIGNIADEIKKTpff 86
Cdd:PRK06953   3 TVLIVGASRGIGREFVRQYRAD-GWRVIATARDA---------AALAALQAlGAEALALDVADPASVAGLAWKLDGE--- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    87 lGIDIFIACSAVSDSYYKVLETPKSVWLNH-YSTNALGPILALQKVYPLLllKKTRKIF-FISSVAGSINAFVPLSVSAY 164
Cdd:PRK06953  70 -ALDAAVYVAGVYGPRTEGVEPITREDFDAvMHTNVLGPMQLLPILLPLV--EAAGGVLaVLSSRMGSIGDATGTTGWLY 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   165 GQSKAALNYAVKTLSFELKpeGFTVVAFHPGMVSTDMGQYGLDhfkeknidisgvniITPEESASALIDVFRKILPEDNG 244
Cdd:PRK06953 147 RASKAALNDALRAASLQAR--HATCIALHPGWVRTDMGGAQAA--------------LDPAQSVAGMRRVIAQATRRDNG 210


                 ....*....
gi 6322779   245 KFFNYDGSE 253
Cdd:PRK06953 211 RFFQYDGVE 219
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 8-249 2.22e-24

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: 97.36  E-value: 2.22e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIGGSRGIGFNLVKILSASTGNTVITSIrgSPSLPKNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTPFfl 87
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSPSVVVLL--ARSEEPLQELKEELRPGLRVTTVKADLSDAAGVEQLLEAIRKLDG-- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   88 GIDIFIACSAVSDSYYKVLETPKSVWLNHYSTNALGPIL---ALQKVYPLLLLKKTrkIFFISSVAgSINAFVplSVSAY 164
Cdd:cd05367  77 ERDLLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCltsTLLRAFKKRGLKKT--VVNVSSGA-AVNPFK--GWGLY 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779  165 GQSKAALNYAVKTLSFELKpeGFTVVAFHPGMVSTDMGQY-----GLDHFKEKNIDISGVN-IITPEESASALIdvfrKI 238
Cdd:cd05367 152 CSSKAARDMFFRVLAAEEP--DVRVLSYAPGVVDTDMQREiretsADPETRSRFRSLKEKGeLLDPEQSAEKLA----NL 225

                       250
                ....*....|....
gi 6322779  239 LPED---NGKFFNY 249
Cdd:cd05367 226 LEKDkfeSGAHVDY 239
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-234 2.50e-24

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: 97.17  E-value: 2.50e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    1 MNTSSRiTYFIIGGSRGIGFNLVKILsASTGNTVI-TSIRGSPslpknkqVEDLAK-IRKNIHIVQLDLTKDESIGNIAD 78
Cdd:COG4221   1 MSDKGK-VALITGASSGIGAATARAL-AAAGARVVlAARRAER-------LEALAAeLGGRALAVPLDVTDEAAVEAAVA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   79 EIKKTpfFLGIDIFI--ACSAVSDSyykVLETPKSVWLNHYSTNALGPILALQKVYPLLllKKTRK--IFFISSVAGsIN 154
Cdd:COG4221  72 AAVAE--FGRLDVLVnnAGVALLGP---LEELDPEDWDRMIDVNVKGVLYVTRAALPAM--RARGSghIVNISSIAG-LR 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779  155 AFVplSVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLDHFKEKNIDI-SGVNIITPEESASALID 233
Cdd:COG4221 144 PYP--GGAVYAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVyEGLEPLTPEDVAEAVLF 221


                .
gi 6322779  234 V 234
Cdd:COG4221 222 A 222
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 8-252 9.28e-24

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: 95.76  E-value: 9.28e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLpknkqvEDLAKIRK-NIHIVQLDLTKDESIGNIADEIKKtpFF 86
Cdd:cd05374   2 VVLITGCSSGIGLALALAL-AAQGYRVIATARNPDKL------ESLGELLNdNLEVLELDVTDEESIKAAVKEVIE--RF 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   87 LGIDIFIACSAVSdsYYK-VLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINafVPLsVSAYG 165
Cdd:cd05374  73 GRIDVLVNNAGYG--LFGpLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVP--TPF-LGPYC 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779  166 QSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGL------------DHFKEKNIDISGVNIITPeESASALID 233
Cdd:cd05374 148 ASKAALEALSESLRLELAPFGIKVTIIEPGPVRTGFADNAAgsaledpeispyAPERKEIKENAAGVGSNP-GDPEKVAD 226

                       250
                ....*....|....*....
gi 6322779  234 VFRKILPEDNGKFFNYDGS 252
Cdd:cd05374 227 VIVKALTSESPPLRYFLGS 245
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 16-230 2.26e-22

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: 92.11  E-value: 2.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     16 RGIGFNLVKILSASTGNTVITSIrgspSLPKNKQVEDLAKiRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGIDIFIAC 95
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDL----NEALAKRVEELAE-ELGAAVLPCDVTDEEQVEALVAAAVEK--FGRLDILVNN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     96 SAVSDSYYK-VLETPKSVWLNHYSTNALGPILALQKVYPLLllKKTRKIFFISSVAGSINafVPlSVSAYGQSKAALNYA 174
Cdd:pfam13561  79 AGFAPKLKGpFLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERV--VP-NYNAYGAAKAALEAL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322779    175 VKTLSFELKPEGFTVVAFHPGMVSTDMGQyGLDHFkEKNIDISGVNI-----ITPEESASA 230
Cdd:pfam13561 154 TRYLAVELGPRGIRVNAISPGPIKTLAAS-GIPGF-DELLAAAEARAplgrlGTPEEVANA 212
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 1-241 1.12e-20

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 87.52  E-value: 1.12e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    1 MNTSSRiTYFIIGGSRGIGFNLVKILSAStGNTVITSIRgspslpkNKQV-EDLAKIRKNIHIVQLDLTKDESIGNIADE 79
Cdd:COG3967   1 MKLTGN-TILITGGTSGIGLALAKRLHAR-GNTVIITGR-------REEKlEEAAAANPGLHTIVLDVADPASIAALAEQ 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   80 IKKTpfFLGIDIFIACSAVSdSYYKVLETPksvwlNHYS-------TNALGPILALQKVYPLLLLKKTRKIFFISSVAgs 152
Cdd:COG3967  72 VTAE--FPDLNVLINNAGIM-RAEDLLDEA-----EDLAdaereitTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGL-- 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779  153 inAFVPLSVSA-YGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM-GQYGLDHFKeknidisgvniITPEESASA 230
Cdd:COG3967 142 --AFVPLAVTPtYSATKAALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLtGGQGGDPRA-----------MPLDEFADE 208

                       250
                ....*....|....*
gi 6322779  231 LIDVFRK----ILPE 241
Cdd:COG3967 209 VMAGLETgkyeILVG 223
PRK08177 PRK08177
SDR family oxidoreductase;
8-202 4.30e-19

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 82.77  E-value: 4.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     8 TYFIIGGSRGIGFNLVKILSAStGNTVITSIRGsPSLPKNKQveDLAkirkNIHIVQLDLTKDESIGNIADEIKKTPFfl 87
Cdd:PRK08177   3 TALIIGASRGLGLGLVDRLLER-GWQVTATVRG-PQQDTALQ--ALP----GVHIEKLDMNDPASLDQLLQRLQGQRF-- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    88 giDIFIACSAVSDSYYKVLETPKSVWLNH-YSTNALGPILALQKvypllLLKKTRK----IFFISSVAGSINAFVPLSVS 162
Cdd:PRK08177  73 --DLLFVNAGISGPAHQSAADATAAEIGQlFLTNAIAPIRLARR-----LLGQVRPgqgvLAFMSSQLGSVELPDGGEMP 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 6322779   163 AYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMG 202
Cdd:PRK08177 146 LYKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTDMG 185
PRK09009 PRK09009
SDR family oxidoreductase;
9-253 5.70e-19

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 82.80  E-value: 5.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     9 YFIIGGSRGIGFNLVKILSAS-TGNTVITSIRGSPslPKNKQvedlakirKNIHIVQLDLTKDESIGNIADEIKKtpffl 87
Cdd:PRK09009   3 ILIVGGSGGIGKAMVKQLLERyPDATVHATYRHHK--PDFQH--------DNVQWHALDVTDEAEIKQLSEQFTQ----- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    88 gIDIFIACSAVsdsyykvLETP-----KSV-------WLNHYSTNALgPILALQKVYPLLLLKKTRKIF-FISSVAGSIN 154
Cdd:PRK09009  68 -LDWLINCVGM-------LHTQdkgpeKSLqaldadfFLQNITLNTL-PSLLLAKHFTPKLKQSESAKFaVISAKVGSIS 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   155 AFVPLSVSAYGQSKAALNYAVKTLSFE----LKpeGFTVVAFHPGMVSTDMGQygldHFKEkniDISGVNIITPEESASA 230
Cdd:PRK09009 139 DNRLGGWYSYRASKAALNMFLKTLSIEwqrsLK--HGVVLALHPGTTDTALSK----PFQQ---NVPKGKLFTPEYVAQC 209

                        250       260
                 ....*....|....*....|...
gi 6322779   231 LIDVFRKILPEDNGKFFNYDGSE 253
Cdd:PRK09009 210 LLGIIANATPAQSGSFLAYDGET 232
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 10-233 1.52e-17

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: 78.83  E-value: 1.52e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   10 FIIGGSRGIGFNLVKILSASTGNTVITSiRGSPSLpkNKQVEDLAKIRKN----IHIVQLDLTKDESIGNIADEIkkTPF 85
Cdd:cd08939   5 LITGGSSGIGKALAKELVKEGANVIIVA-RSESKL--EEAVEEIEAEANAsgqkVSYISADLSDYEEVEQAFAQA--VEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   86 FLGIDIFIACSAVSDSYYkVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGsinaFVPL-SVSAY 164
Cdd:cd08939  80 GGPPDLVVNCAGISIPGL-FEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAA----LVGIyGYSAY 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322779  165 GQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMgqygldhFKEKNI-------DISG-VNIITPEESASALID 233
Cdd:cd08939 155 CPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTPG-------FEEENKtkpeetkAIEGsSGPITPEEAARIIVK 224
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 8-204 2.08e-17

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: 79.19  E-value: 2.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIGGSRGIGFNLVKILsASTGNTVITSIRgSPSlpknKQVEDLAKIRK-----NIHIVQLDLTKDESIGNIADEIKK 82
Cdd:cd05327   3 VVVITGANSGIGKETAREL-AKRGAHVIIACR-NEE----KGEEAAAEIKKetgnaKVEVIQLDLSSLASVRQFAEEFLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   83 TpfFLGIDIFIACSAVsdsYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVA---GSINAFVPL 159
Cdd:cd05327  77 R--FPRLDILINNAGI---MAPPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAhraGPIDFNDLD 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 6322779  160 SVS--------AYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQY 204
Cdd:cd05327 152 LENnkeyspykAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRR 204
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 11-201 2.17e-16

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 75.86  E-value: 2.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGFNLVKILSASTGNTVITSIRGSPSLPKNKQVEdlaKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGID 90
Cdd:cd05347  10 VTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIE---KEGVEATAFTCDVSDEEAIKAAVEAIEED--FGKID 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   91 IFIACSAVSdSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAgSINAFVPlsVSAYGQSKAA 170
Cdd:cd05347  85 ILVNNAGII-RRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLL-SELGGPP--VPAYAASKGG 160

                       170       180       190
                ....*....|....*....|....*....|.
gi 6322779  171 LNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:cd05347 161 VAGLTKALATEWARHGIQVNAIAPGYFATEM 191
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 11-212 2.46e-16

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: 75.83  E-value: 2.46e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGFNLVKILSASTGNTVITSIRGSPSLPKNKQVEDlaKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGID 90
Cdd:cd05352  13 VTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAK--KYGVKTKAYKCDVSSQESVEKTFKQIQKD--FGKID 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   91 IFIACSAVSdSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSInAFVPLSVSAYGQSKAA 170
Cdd:cd05352  89 ILIANAGIT-VHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTI-VNRPQPQAAYNASKAA 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 6322779  171 LNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLDHFKEK 212
Cdd:cd05352 167 VIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKK 208
PRK12826 PRK12826
SDR family oxidoreductase;
10-203 4.24e-16

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 75.34  E-value: 4.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    10 FIIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLPKnkQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGI 89
Cdd:PRK12826  10 LVTGAARGIGRAIAVRL-AADGAEVIVVDICGDDAAA--TAELVEAAGGKARARQVDVRDRAALKAAVAAGVED--FGRL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    90 DIFIACSAVSDSYyKVLETPKSVWLNHYSTNALGPILALQKVYPLLllKKTR--KIFFISSVAGSINAFVPLSvsAYGQS 167
Cdd:PRK12826  85 DILVANAGIFPLT-PFAEMDDEQWERVIDVNLTGTFLLTQAALPAL--IRAGggRIVLTSSVAGPRVGYPGLA--HYAAS 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 6322779   168 KAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQ 203
Cdd:PRK12826 160 KAGLVGFTRALALELAARNITVNSVHPGGVDTPMAG 195
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 11-204 5.20e-16

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 74.88  E-value: 5.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILsASTGNTVITSIRgspsLPKNKQVEDLAKIRKN---IHIVQLDLTKDESIGNIADEIKKTpfFL 87
Cdd:PRK05565  10 VTGASGGIGRAIAELL-AKEGAKVVIAYD----INEEAAQELLEEIKEEggdAIAVKADVSSEEDVENLVEQIVEK--FG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    88 GIDIFIACSAVSdSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAfvPLSVsAYGQS 167
Cdd:PRK05565  83 KIDILVNNAGIS-NFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGA--SCEV-LYSAS 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 6322779   168 KAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQY 204
Cdd:PRK05565 159 KGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSS 195
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 1-212 8.16e-16

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 74.46  E-value: 8.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     1 MNTSSRITyFIIGGSRGIGFNLVKILsASTGNTVITSIRGSpSLPKNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEI 80
Cdd:PRK05557   1 MSLEGKVA-LVTGASRGIGRAIAERL-AAQGANVVINYASS-EAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    81 KKTpfFLGIDIFIACSAVS----------DSYYKVLETP-KSVWLnhystnalgpilALQKVYPLLLLKKTRKIFFISSV 149
Cdd:PRK05557  78 KAE--FGGVDILVNNAGITrdnllmrmkeEDWDRVIDTNlTGVFN------------LTKAVARPMMKQRSGRIINISSV 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322779   150 AGSINAFvplSVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLDHFKEK 212
Cdd:PRK05557 144 VGLMGNP---GQANYAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDVKEA 203
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 1-236 1.40e-15

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


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 73.49  E-value: 1.40e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    1 MNTSSRiTYFIIGGSRGIGFNLVKILsASTGNTVITSIRgSPSlpknkQVEDLAKIRKNIHIVQLDLTKDESIGNIADEI 80
Cdd:cd05370   1 MKLTGN-TVLITGGTSGIGLALARKF-LEAGNTVIITGR-REE-----RLAEAKKELPNIHTIVLDVGDAESVEALAEAL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   81 KKTpfFLGIDIFIACSAVSDSY-YKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAgsinAFVPL 159
Cdd:cd05370  73 LSE--YPNLDILINNAGIQRPIdLRDPASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGL----AFVPM 146

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322779  160 SVS-AYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQygldhfKEKNIDISGVNIITPEESASALIDVFR 236
Cdd:cd05370 147 AANpVYCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHE------ERRNPDGGTPRKMPLDEFVDEVVAGLE 218
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 10-230 5.54e-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: 5.54e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   10 FIIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLPKNKQVEDLAKIRKNIhIVQLDLTKDESIGNIADEIKKTpfFLGI 89
Cdd:cd05359   2 LVTGGSRGIGKAIALRL-AERGADVVINYRKSKDAAAEVAAEIEELGGKAV-VVRADVSQPQDVEEMFAAVKER--FGRL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   90 DIFIACSAvSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVaGSINAFVPLSvsAYGQSKA 169
Cdd:cd05359  78 DVLVSNAA-AGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSL-GSIRALPNYL--AVGTAKA 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322779  170 ALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQ--YGLDHFKEKNIDISGVN-IITPEESASA 230
Cdd:cd05359 154 ALEALVRYLAVELGPRGIRVNAVSPGVIDTDALAhfPNREDLLEAAAANTPAGrVGTPQDVADA 217
PRK06914 PRK06914
SDR family oxidoreductase;
10-206 5.67e-15

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 72.75  E-value: 5.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    10 FIIGGSRGIGFnLVKILSASTGNTVITSIRgspSLPKNKQVEDLAK---IRKNIHIVQLDLTKDESIGNIADEIKKtpfF 86
Cdd:PRK06914   7 IVTGASSGFGL-LTTLELAKKGYLVIATMR---NPEKQENLLSQATqlnLQQNIKVQQLDVTDQNSIHNFQLVLKE---I 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    87 LGIDIFI--ACSAVSDSyykVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSInAFVPLsvSAY 164
Cdd:PRK06914  80 GRIDLLVnnAGYANGGF---VEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRV-GFPGL--SPY 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 6322779   165 GQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGL 206
Cdd:PRK06914 154 VSSKYALEGFSESLRLELKPFGIDVALIEPGSYNTNIWEVGK 195
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 11-203 1.06e-14

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: 70.85  E-value: 1.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGFNLVKILsASTGNTVITSIRgSPSLPKNKQVEDlakirKNIHIVQLDLTKDESIGNIADEIKKTpfFLGID 90
Cdd:cd08932   5 VTGASRGIGIEIARAL-ARDGYRVSLGLR-NPEDLAALSASG-----GDVEAVPYDARDPEDARALVDALRDR--FGRID 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   91 IFIACSAVSDSYyKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSInafVPLSVSAYGQSKAA 170
Cdd:cd08932  76 VLVHNAGIGRPT-TLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKR---VLAGNAGYSASKFA 151

                       170       180       190
                ....*....|....*....|....*....|...
gi 6322779  171 LNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQ 203
Cdd:cd08932 152 LRALAHALRQEGWDHGVRVSAVCPGFVDTPMAQ 184
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
11-209 1.22e-14

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 71.29  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILSASTGNTVITSIRGSPslPKNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGID 90
Cdd:PRK08063   9 VTGSSRGIGKAIALRLAEEGYDIAVNYARSRK--AAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEE--FGRLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    91 IFIAcSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVaGSINAFVplSVSAYGQSKAA 170
Cdd:PRK08063  85 VFVN-NAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSL-GSIRYLE--NYTTVGVSKAA 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 6322779   171 LNYAVKTLSFELKPEGFTVVAFHPGMVSTDmgqyGLDHF 209
Cdd:PRK08063 161 LEALTRYLAVELAPKGIAVNAVSGGAVDTD----ALKHF 195
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 11-206 1.51e-14

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: 70.82  E-value: 1.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLPKNKqvEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKtpFFLGID 90
Cdd:cd05350   3 ITGASSGIGRALAREF-AKAGYNVALAARRTDRLDELK--AELLNPNPSVEVEILDVTDEERNQLVIAELEA--ELGGLD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   91 IFIACSAVSDSYyKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINafVPLSVsAYGQSKAA 170
Cdd:cd05350  78 LVIINAGVGKGT-SLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRG--LPGAA-AYSASKAA 153

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 6322779  171 LNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGL 206
Cdd:cd05350 154 LSSLAESLRYDVKKRGIRVTVINPGFIDTPLTANMF 189
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 8-230 2.18e-14

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: 70.56  E-value: 2.18e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLpkNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpFFL 87
Cdd:cd05329   8 TALVTGGTKGIGYAIVEEL-AGLGAEVYTCARNQKEL--DECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASH-FGG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   88 GIDIFIACSAVSDSYYKVLETPKSvWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINafVPlSVSAYGQS 167
Cdd:cd05329  84 KLNILVNNAGTNIRKEAKDYTEED-YSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIA--VP-SGAPYGAT 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322779  168 KAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLDHFKEKNIDISGV---NIITPEESASA 230
Cdd:cd05329 160 KGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKENLDKVIERTplkRFGEPEEVAAL 225
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 10-203 2.74e-14

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: 69.96  E-value: 2.74e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   10 FIIGGSRGIGFNLVKILSASTGNTVITSIRGSPSLPKNKQVEdlaKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGI 89
Cdd:cd05339   3 LITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVR---KAGGKVHYYKCDVSKREEVYEAAKKIKKE--VGDV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   90 DIFIACSAVSdSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINafvPLSVSAYGQSKA 169
Cdd:cd05339  78 TILINNAGVV-SGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLIS---PAGLADYCASKA 153

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 6322779  170 ALNYAVKTLSFELKPEG-----FTVVafHPGMVSTDMGQ 203
Cdd:cd05339 154 AAVGFHESLRLELKAYGkpgikTTLV--CPYFINTGMFQ 190
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 8-200 2.90e-14

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: 70.38  E-value: 2.90e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIGGSRGIGFNLVKILSASTGNTVITSiRGSPSLPKNKqvEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFL 87
Cdd:cd05344   3 VALVTAASSGIGLAIARALAREGARVAICA-RNRENLERAA--SELRAGGAGVLAVVADLTDPEDIDRLVEKAGDA--FG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   88 GIDIFIAcSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGsINAFVPLSVSayGQS 167
Cdd:cd05344  78 RVDILVN-NAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTV-KEPEPNLVLS--NVA 153

                       170       180       190
                ....*....|....*....|....*....|...
gi 6322779  168 KAALNYAVKTLSFELKPEGFTVVAFHPGMVSTD 200
Cdd:cd05344 154 RAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTE 186
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 11-232 5.99e-14

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: 69.54  E-value: 5.99e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGFNLVKILSASTGNTVITSIRgspslpknkqVEDLAKIR--------KNIHIVQLDLTKDESIGNIADEIKK 82
Cdd:cd05332   8 ITGASSGIGEELAYHLARLGARLVLSARR----------EERLEEVKseclelgaPSPHVVPLDMSDLEDAEQVVEEALK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   83 TpfFLGIDIFIACSAVSdSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINafVPLSvS 162
Cdd:cd05332  78 L--FGGLDILINNAGIS-MRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIG--VPFR-T 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322779  163 AYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGL--DHFKEKNIDISGVNIITPEESASALI 232
Cdd:cd05332 152 AYAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNALsgDGSMSAKMDDTTANGMSPEECALEIL 223
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-230 2.04e-13

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 67.59  E-value: 2.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    10 FIIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLPKN--KQVEDLAKirkNIHIVQLDLTKDESIGNIADEIKKTpfFL 87
Cdd:PRK12825  10 LVTGAARGLGRAIALRL-ARAGADVVVHYRSDEEAAEElvEAVEALGR---RAQAVQADVTDKAALEAAVAAAVER--FG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    88 GIDIFIACSAVS----------DSYYKVLETpksvwlnhystNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINafv 157
Cdd:PRK12825  84 RIDILVNNAGIFedkpladmsdDEWDEVIDV-----------NLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPG--- 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322779   158 PLSVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQyglDHFKEKNIDISGV----NIITPEESASA 230
Cdd:PRK12825 150 WPGRSNYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKE---ATIEEAREAKDAEtplgRSGTPEDIARA 223
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 8-217 2.27e-13

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: 67.43  E-value: 2.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIGGSRGIGFNLVKILSASTGNTVITSIRGSPSlpknkqVEDL-AKIRKNIHIVQLDLTKDESIGNIADEIKKtpff 86
Cdd:cd05354   5 TVLVTGANRGIGKAFVESLLAHGAKKVYAAVRDPGS------AAHLvAKYGDKVVPLRLDVTDPESIKAAAAQAKD---- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   87 lgIDIFI-------ACSAVSDsyyKVLETPKSvwlnHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAgSINAFVpl 159
Cdd:cd05354  75 --VDVVInnagvlkPATLLEE---GALEALKQ----EMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVA-SLKNFP-- 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6322779  160 SVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQyGLDHFKEKNIDIS 217
Cdd:cd05354 143 AMGTYSASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAA-GAGGPKESPETVA 199
FabG-like PRK07231
SDR family oxidoreductase;
11-201 2.83e-13

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 67.55  E-value: 2.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILSASTGNTVITSIRGSPSLPKNKQVEDLAkirkNIHIVQLDLTKDESIGNIADEIKKTpfFLGID 90
Cdd:PRK07231  10 VTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAGG----RAIAVAADVSDEADVEAAVAAALER--FGSVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    91 IFIACSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGsinafvpLSVS----AYGQ 166
Cdd:PRK07231  84 ILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAG-------LRPRpglgWYNA 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 6322779   167 SKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK07231 157 SKGAVITLTKALAAELGPDKIRVNAVAPVVVETGL 191
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 10-201 6.48e-13

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: 66.34  E-value: 6.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   10 FIIGGSRGIGFNLVKILsASTGNTVITSirgspslpkNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGI 89
Cdd:cd05331   2 IVTGAAQGIGRAVARHL-LQAGATVIAL---------DLPFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAE--HGPI 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   90 DIFIACSAV-----SDsyykvlETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAgsinAFVP-LSVSA 163
Cdd:cd05331  70 DALVNCAGVlrpgaTD------PLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNA----AHVPrISMAA 139

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 6322779  164 YGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:cd05331 140 YGASKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAM 177
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 10-205 9.20e-13

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 66.15  E-value: 9.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    10 FIIGGSRGIGFNLVKILSASTGNTVITSIRGSPslpknkqVEDLA-KIRK---NIHIVQLDLTKDESIGNIADEIKKTpf 85
Cdd:PRK12939  11 LVTGAARGLGAAFAEALAEAGATVAFNDGLAAE-------ARELAaALEAaggRAHAIAADLADPASVQRFFDAAAAA-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    86 FLGIDIFIACSAVSDSYYKVlETPKSVWLNHYSTNALGPILALQKVYPLLL-LKKTRKIFFISSVA--GSINafvplsVS 162
Cdd:PRK12939  82 LGGLDGLVNNAGITNSKSAT-ELDIDTWDAVMNVNVRGTFLMLRAALPHLRdSGRGRIVNLASDTAlwGAPK------LG 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 6322779   163 AYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYG 205
Cdd:PRK12939 155 AYVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEATAYV 197
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 10-201 3.90e-12

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 64.05  E-value: 3.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    10 FIIGGSRGIGFNLVKILsASTGNTVITSIRGSPslPKNKQVEDLAKIRknIHIVQLDLTKDESIGNIADEIKKTpfFLGI 89
Cdd:PRK12828  11 AITGGFGGLGRATAAWL-AARGARVALIGRGAA--PLSQTLPGVPADA--LRIGGIDLVDPQAARRAVDEVNRQ--FGRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    90 DIFIACSAVSdSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAfvpLSVSAYGQSKA 169
Cdd:PRK12828  84 DALVNIAGAF-VWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAG---PGMGAYAAAKA 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 6322779   170 ALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK12828 160 GVARLTEALAAELLDRGITVNAVLPSIIDTPP 191
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 11-203 6.05e-12

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: 63.64  E-value: 6.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGfNLVKILSASTGNTVI-TSIrgspslpkNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKtpfflgI 89
Cdd:cd05368   7 ITAAAQGIG-RAIALAFAREGANVIaTDI--------NEEKLKELERGPGITTRVLDVTDKEQVAALAKEEGR------I 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   90 DIFIACSAVSDSYyKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAfVPlSVSAYGQSKA 169
Cdd:cd05368  72 DVLFNCAGFVHHG-SILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIKG-VP-NRFVYSTTKA 148

                       170       180       190
                ....*....|....*....|....*....|....
gi 6322779  170 ALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQ 203
Cdd:cd05368 149 AVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLE 182
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 10-236 1.09e-11

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: 62.52  E-value: 1.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   10 FIIGGSRGIGFNLVKILSASTGNTVITSirgspslPKNKQVEDLA-KIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLG 88
Cdd:cd08929   4 LVTGASRGIGEATARLLHAEGYRVGICA-------RDEARLAAAAaQELEGVLGLAGDVRDEADVRRAVDAMEEA--FGG 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   89 IDIFIACSAVSdSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSiNAFVplSVSAYGQSK 168
Cdd:cd08929  75 LDALVNNAGVG-VMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGK-NAFK--GGAAYNASK 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322779  169 AALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLDHFKEknidisgvniITPEESASALIDVFR 236
Cdd:cd08929 151 FGLLGLSEAAMLDLREANIRVVNVMPGSVDTGFAGSPEGQAWK----------LAPEDVAQAVLFALE 208
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 11-209 1.32e-11

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: 62.51  E-value: 1.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGFNLVKILSASTGNTVITSIRGSPSlpknkqVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGID 90
Cdd:cd08944   8 VTGAGAGIGAACAARLAREGARVVVADIDGGAA------QAVVAQIAGGALALRVDVTDEQQVAALFERAVEE--FGGLD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   91 IFIACSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAfvpLSVSAYGQSKAA 170
Cdd:cd08944  80 LLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGD---PGYGAYGASKAA 156

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 6322779  171 LNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLDHF 209
Cdd:cd08944 157 IRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGF 195
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
9-234 1.63e-11

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 62.39  E-value: 1.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     9 YFII-GGSRGIGFNLVKILSAStGNTVITSIRGspslpKNKQVEDLAKIRK-NIHIVQLDLTkdeSIGNIADEIKKtpff 86
Cdd:PRK06924   3 YVIItGTSQGLGEAIANQLLEK-GTHVISISRT-----ENKELTKLAEQYNsNLTFHSLDLQ---DVHELETNFNE---- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    87 lgIDIFIACSAVSDSYY----------KVLETPKSVWLN-HYSTNALGPILALQkvyplLLLKKT------RKIFFISSV 149
Cdd:PRK06924  70 --ILSSIQEDNVSSIHLinnagmvapiKPIEKAESEELItNVHLNLLAPMILTS-----TFMKHTkdwkvdKRVINISSG 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   150 AGSINAFvplSVSAYGQSKAALNYAVKTLSFELKPEGFTV--VAFHPGMVSTDMGQYGLDHFKEKNIDISGV-------N 220
Cdd:PRK06924 143 AAKNPYF---GWSAYCSSKAGLDMFTQTVATEQEEEEYPVkiVAFSPGVMDTNMQAQIRSSSKEDFTNLDRFitlkeegK 219

                        250
                 ....*....|....
gi 6322779   221 IITPEESASALIDV 234
Cdd:PRK06924 220 LLSPEYVAKALRNL 233
PRK09291 PRK09291
SDR family oxidoreductase;
3-248 1.93e-11

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 62.32  E-value: 1.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     3 TSSRItyFIIGGSRGIGFNlVKILSASTGNTVITSIRGSPslpknkQVEDL---AKIRK-NIHIVQLDLTKDESIGNIAD 78
Cdd:PRK09291   1 MSKTI--LITGAGSGFGRE-VALRLARKGHNVIAGVQIAP------QVTALraeAARRGlALRVEKLDLTDAIDRAQAAE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    79 eikktpffLGIDIFIACSAVSDSYyKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGsinAFVP 158
Cdd:PRK09291  72 --------WDVDVLLNNAGIGEAG-AVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAG---LITG 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   159 LSVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLDHFK-----EKNIdISGVNIITPEESASA--L 231
Cdd:PRK09291 140 PFTGAYCASKHALEAIAEAMHAELKPFGIQVATVNPGPYLTGFNDTMAETPKrwydpARNF-TDPEDLAFPLEQFDPqeM 218

                        250
                 ....*....|....*..
gi 6322779   232 IDVFRKILPEDNGKFFN 248
Cdd:PRK09291 219 IDAMVEVIPADTGLFRN 235
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 11-201 2.26e-11

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: 61.79  E-value: 2.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGFNLVKILsASTGNTVItsIRGSPSLPKNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKtpFFLGID 90
Cdd:cd05333   5 VTGASRGIGRAIALRL-AAEGAKVA--VTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEA--EFGPVD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   91 IFIACSAVS-DSYykVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAFvplsvsayGQ--- 166
Cdd:cd05333  80 ILVNNAGITrDNL--LMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNP--------GQany 149

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 6322779  167 --SKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:cd05333 150 aaSKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDM 186
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 11-201 6.61e-11

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: 60.78  E-value: 6.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGFNLVKILsASTGNTVItsirgspSLPKNKQVEDLAKIRK-----NIHIVQLDLTKDESIGNIADEIKKTpf 85
Cdd:cd05323   5 ITGGASGIGLATAKLL-LKKGAKVA-------ILDRNENPGAAAELQAinpkvKATFVQCDVTSWEQLAAAFKKAIEK-- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   86 FLGIDIFIACSAVSDS-YYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRK---IFFISSVAGsinaFVPL-S 160
Cdd:cd05323  75 FGRVDILINNAGILDEkSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKGGKggvIVNIGSVAG----LYPApQ 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 6322779  161 VSAYGQSKAALNYAVKTLSFELK-PEGFTVVAFHPGMVSTDM 201
Cdd:cd05323 151 FPVYSASKHGVVGFTRSLADLLEyKTGVRVNAICPGFTNTPL 192
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 1-207 6.83e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 60.50  E-value: 6.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     1 MNTSSRI---TYFIIGGSRGIGFNLVKILSASTGNTVITSIRGSpslpknkqveDLAKIRKNI--HIVQLDLTKDESIGN 75
Cdd:PRK07060   1 MNMAFDFsgkSVLVTGASSGIGRACAVALAQRGARVVAAARNAA----------ALDRLAGETgcEPLRLDVGDDAAIRA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    76 IADEIKktPFflgiDIFIACSAVSdSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTR-KIFFISSVAgsin 154
Cdd:PRK07060  71 ALAAAG--AF----DGLVNCAGIA-SLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRGgSIVNVSSQA---- 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6322779   155 AFVPL-SVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLD 207
Cdd:PRK07060 140 ALVGLpDHLAYCASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPMAAEAWS 193
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 11-201 9.26e-11

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: 60.37  E-value: 9.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGFNLVKILsASTGNTVITSIRGSpslpKNKQVEDLAKIRKN---IHIVQLDLTKDESIGNIADEIKKtpFFL 87
Cdd:cd05362   8 VTGASRGIGRAIAKRL-ARDGASVVVNYASS----KAAAEEVVAEIEAAggkAIAVQADVSDPSQVARLFDAAEK--AFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   88 GIDIFIACSAVSDSYyKVLETPKSVWLNHYSTNALGPILALQKVYPLLllKKTRKIFFISSVAGSinAFVPLSvSAYGQS 167
Cdd:cd05362  81 GVDILVNNAGVMLKK-PIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTA--AYTPNY-GAYAGS 154

                       170       180       190
                ....*....|....*....|....*....|....
gi 6322779  168 KAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:cd05362 155 KAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDM 188
PRK08264 PRK08264
SDR family oxidoreductase;
8-233 1.85e-10

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 59.13  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     8 TYFIIGGSRGIGFNLVKILSASTGNTVITSIRgspslpknkQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKtpffl 87
Cdd:PRK08264   8 VVLVTGANRGIGRAFVEQLLARGAAKVYAAAR---------DPESVTDLGPRVVPLQLDVTDPASVAAAAEAASD----- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    88 gIDIFIACSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLllKKTRK--IFFISSVAGSINafvPLSVSAYG 165
Cdd:PRK08264  74 -VTILVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVL--AANGGgaIVNVLSVLSWVN---FPNLGTYS 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322779   166 QSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQyGLDHFKEknidisgvniiTPEESASALID 233
Cdd:PRK08264 148 ASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAA-GLDAPKA-----------SPADVARQILD 203
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 11-200 3.01e-10

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: 58.93  E-value: 3.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGFNLVKILSASTGNTVItSIRGSPSlPKNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGID 90
Cdd:cd05358   8 VTGASSGIGKAIAIRLATAGANVVV-NYRSKED-AAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKE--FGTLD 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   91 IFIACSAVsDSYYKVLETPKSVWLNHYSTNALGPIL-ALQKVYPLLLLKKTRKIFFISSVagsiNAFVPLSV-SAYGQSK 168
Cdd:cd05358  84 ILVNNAGL-QGDASSHEMTLEDWNKVIDVNLTGQFLcAREAIKRFRKSKIKGKIINMSSV----HEKIPWPGhVNYAASK 158

                       170       180       190
                ....*....|....*....|....*....|..
gi 6322779  169 AALNYAVKTLSFELKPEGFTVVAFHPGMVSTD 200
Cdd:cd05358 159 GGVKMMTKTLAQEYAPKGIRVNAIAPGAINTP 190
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-201 3.53e-10

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 58.55  E-value: 3.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     8 TYFIIGGSRGIGfNLVKILSASTGNTVITSIRGSPSLpkNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpffL 87
Cdd:PRK07666   9 NALITGAGRGIG-RAVAIALAKEGVNVGLLARTEENL--KAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNE---L 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    88 G-IDIFIACSAVSdSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAFVplsVSAYGQ 166
Cdd:PRK07666  83 GsIDILINNAGIS-KFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAV---TSAYSA 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 6322779   167 SKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK07666 159 SKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDM 193
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
10-201 4.38e-10

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 58.25  E-value: 4.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    10 FIIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLPKNKqvEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGI 89
Cdd:PRK05653   9 LVTGASRGIGRAIALRL-AADGAKVVIYDSNEEAAEALA--AELRAAGGEARVLVFDVSDEAAVRALIEAAVEA--FGAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    90 DIFIACSAV-SDSyyKVLETPKSVWLNHYSTNALGPILALQKVypLLLLKKTRK--IFFISSVAGSI-NAFVplsvSAYG 165
Cdd:PRK05653  84 DILVNNAGItRDA--LLPRMSEEDWDRVIDVNLTGTFNVVRAA--LPPMIKARYgrIVNISSVSGVTgNPGQ----TNYS 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 6322779   166 QSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK05653 156 AAKAGVIGFTKALALELASRGITVNAVAPGFIDTDM 191
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 11-232 4.70e-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: 4.70e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLPKNKQvEDLAKIRKNIHIVQLDLTKDESI-GNIADEIKKTPfflgI 89
Cdd:cd05356   6 VTGATDGIGKAYAEEL-AKRGFNVILISRTQEKLDAVAK-EIEEKYGVETKTIAADFSAGDDIyERIEKELEGLD----I 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   90 DIFIACSAVSDSYYKV-LETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINafVPLsVSAYGQSK 168
Cdd:cd05356  80 GILVNNVGISHSIPEYfLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIP--TPL-LATYSASK 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322779  169 AALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMgqygldhfkeKNIDISGVNIITPEESASALI 232
Cdd:cd05356 157 AFLDFFSRALYEEYKSQGIDVQSLLPYLVATKM----------SKIRKSSLFVPSPEQFVRSAL 210
PRK07326 PRK07326
SDR family oxidoreductase;
1-236 4.83e-10

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 58.10  E-value: 4.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     1 MNTSSRITYFIIGGSRGIGFNLVKILSASTGNTVITSiRgspslpKNKQVEDLAKIRK---NIHIVQLDLTKDESIGNIA 77
Cdd:PRK07326   1 MMSLKGKVALITGGSKGIGFAIAEALLAEGYKVAITA-R------DQKELEEAAAELNnkgNVLGLAADVRDEADVQRAV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    78 DEIKKTpfFLGIDIFIACSAVSdSYYKVLETPKSVWLNHYSTNALGPILALQKVYPllLLKKTRK-IFFISSVAGSiNAF 156
Cdd:PRK07326  74 DAIVAA--FGGLDVLIANAGVG-HFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVP--ALKRGGGyIINISSLAGT-NFF 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   157 VplSVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTdmgqygldHFKEKNIDISGVNIITPEESASALIDVFR 236
Cdd:PRK07326 148 A--GGAAYNASKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVAT--------HFNGHTPSEKDAWKIQPEDIAQLVLDLLK 217
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 11-232 6.64e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 57.99  E-value: 6.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILSAStGNTVITSIRGSPslpknkqvEDLAkirKNIHIVQLDLTKDESIGNIADEIKKTpfFLGID 90
Cdd:PRK06523  14 VTGGTKGIGAATVARLLEA-GARVVTTARSRP--------DDLP---EGVEFVAADLTTAEGCAAVARAVLER--LGGVD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    91 IFI----ACSAVSDSYykvLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAfvPLSVSAYGQ 166
Cdd:PRK06523  80 ILVhvlgGSSAPAGGF---AALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPL--PESTTAYAA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322779   167 SKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDmgqyGLDHFKEKNIDISGvniiTPEESASALI 232
Cdd:PRK06523 155 AKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETE----AAVALAERLAEAAG----TDYEGAKQII 212
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 1-230 1.04e-09

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 57.06  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     1 MNTSSRITyFIIGGSRGIGFNLVKILsASTGNTVITSIRGSpSLPKNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEI 80
Cdd:PRK12937   1 MTLSNKVA-IVTGASRGIGAAIARRL-AADGFAVAVNYAGS-AAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    81 KKTpfFLGIDIFIAcSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLllKKTRKIFFISSvagSINAFVPLS 160
Cdd:PRK12937  78 ETA--FGRIDVLVN-NAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLST---SVIALPLPG 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322779   161 VSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLDhfkEKNID-ISGVNII----TPEESASA 230
Cdd:PRK12937 150 YGPYAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATELFFNGKS---AEQIDqLAGLAPLerlgTPEEIAAA 221
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 11-200 1.07e-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: 57.47  E-value: 1.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGFNLVKILSASTGNTVITSIRGSPSLPKNKQVEDLAKIRKNIHIVQLDLtkdESIGNIADEIKKTpfFLGID 90
Cdd:cd08935  10 ITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDR---ASLERAREEIVAQ--FGTVD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   91 IFIACS------AVSDSYYKVLETPKSV-------WLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSvagsINAFV 157
Cdd:cd08935  85 ILINGAggnhpdATTDPEHYEPETEQNFfdldeegWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISS----MNAFS 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 6322779  158 PLS-VSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTD 200
Cdd:cd08935 161 PLTkVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTP 204
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 11-203 1.14e-09

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: 57.10  E-value: 1.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGFNLVKILsASTGNTVITSIRgspslpKNKQVEDLAKIRKNIHIVQLDLTkdesiGNIADEIKKTPFFLgID 90
Cdd:cd05351  12 VTGAGKGIGRATVKAL-AKAGARVVAVSR------TQADLDSLVRECPGIEPVCVDLS-----DWDATEEALGSVGP-VD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   91 IFIACSAVSdSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTR-KIFFISSVAgSINAFVPLSVsaYGQSKA 169
Cdd:cd05351  79 LLVNNAAVA-ILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVPgSIVNVSSQA-SQRALTNHTV--YCSTKA 154

                       170       180       190
                ....*....|....*....|....*....|....
gi 6322779  170 ALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQ 203
Cdd:cd05351 155 ALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGR 188
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 8-228 1.17e-09

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: 56.90  E-value: 1.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIGGSRGIGFNLVKILsASTGNTVITSIRgspslpknkQVEDLAKIRK--------NIHIVQLDLTKDESIGNIADE 79
Cdd:cd05346   2 TVLITGASSGIGEATARRF-AKAGAKLILTGR---------RAERLQELADelgakfpvKVLPLQLDVSDRESIEAALEN 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   80 IKKTpfFLGIDIFIACSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSiNAFVPL 159
Cdd:cd05346  72 LPEE--FRDIDILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGR-YPYAGG 148

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322779  160 SVsaYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTD--MGQYGLDHFKEKNIdISGVNIITPEESA 228
Cdd:cd05346 149 NV--YCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETEfsLVRFHGDKEKADKV-YEGVEPLTPEDIA 216
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 10-242 1.19e-09

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 57.37  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    10 FIIGGSRGIGFNLVKILSASTGNTVITSIRGspslpknkqvEDLAKIRK-----NIHIVQLDLTKDESIGNIADEIKKTp 84
Cdd:PRK12829  15 LVTGGASGIGRAIAEAFAEAGARVHVCDVSE----------AALAATAArlpgaKVTATVADVADPAQVERVFDTAVER- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    85 fFLGIDIFIACSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLL-KKTRKIFFISSVAGSINAfvPLSvSA 163
Cdd:PRK12829  84 -FGGLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKAsGHGGVIIALSSVAGRLGY--PGR-TP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322779   164 YGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMgqygLDHFKEKNIDISGVNIITPEESASALIDVFRKILPED 242
Cdd:PRK12829 160 YAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPR----MRRVIEARAQQLGIGLDEMEQEYLEKISLGRMVEPED 234
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 8-197 1.42e-09

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: 56.63  E-value: 1.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIGGSRGIGFNLVKILSASTGNTVIT----SIRGSPSLPKNKQV--EDLAKIRK---NIHIVQLDLTKDESIGNIAD 78
Cdd:cd05338   5 VAFVTGASRGIGRAIALRLAKAGATVVVAaktaSEGDNGSAKSLPGTieETAEEIEAaggQALPIVVDVRDEDQVRALVE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   79 EIKKTpfFLGIDIFIACSAVSDsYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSinAFVP 158
Cdd:cd05338  85 ATVDQ--FGRLDILVNNAGAIW-LSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSL--RPAR 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 6322779  159 LSVsAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMV 197
Cdd:cd05338 160 GDV-AYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTA 197
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 8-242 1.72e-09

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: 56.62  E-value: 1.72e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIGGSRGIGFNLVKILSASTGNTVITSirgspsLPKNKQVEDLAKIRK----NIHIVQLDLTKDESIGNIADEIKKT 83
Cdd:cd05366   4 VAIITGAAQGIGRAIAERLAADGFNIVLAD------LNLEEAAKSTIQEISeagyNAVAVGADVTDKDDVEALIDQAVEK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   84 pfFLGIDIFIACSAVsDSYYKVLETPKSVWLNHYSTNALGPILALQK-VYPLLLLKKTRKIFFISSVAGsINAFVPLSvs 162
Cdd:cd05366  78 --FGSFDVMVNNAGI-APITPLLTITEEDLKKVYAVNVFGVLFGIQAaARQFKKLGHGGKIINASSIAG-VQGFPNLG-- 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779  163 AYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMgqygLDHFKEKNIDISGVNIITPEESASALIDVFRKILPED 242
Cdd:cd05366 152 AYSASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEM----WDYIDEEVGEIAGKPEGEGFAEFSSSIPLGRLSEPED 227
PRK09242 PRK09242
SDR family oxidoreductase;
8-199 1.84e-09

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 56.68  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     8 TYFIIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLPKNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFL 87
Cdd:PRK09242  11 TALITGASKGIGLAIAREF-LGLGADVLIVARDADALAQARDELAEEFPEREVHGLAADVSDDEDRRAILDWVEDH--WD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    88 GIDIFIAcSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAfvpLSVSAYGQS 167
Cdd:PRK09242  88 GLHILVN-NAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHV---RSGAPYGMT 163

                        170       180       190
                 ....*....|....*....|....*....|..
gi 6322779   168 KAALNYAVKTLSFELKPEGFTVVAFHPGMVST 199
Cdd:PRK09242 164 KAALLQMTRNLAVEWAEDGIRVNAVAPWYIRT 195
PRK06484 PRK06484
short chain dehydrogenase; Validated
 1-201 1.91e-09

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 57.55  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     1 MNTSSRITyFIIGGSRGIGFNLVKILsASTGNTVITSIRgspslPKNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEI 80
Cdd:PRK06484   1 SKAQSRVV-LVTGAAGGIGRAACQRF-ARAGDQVVVADR-----NVERARERADSLGPDHHALAMDVSDEAQIREGFEQL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    81 KKTpfFLGIDIFIACSAVSDSYYK-VLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKT-RKIFFISSVAGSI-NAfv 157
Cdd:PRK06484  74 HRE--FGRIDVLVNNAGVTDPTMTaTLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHgAAIVNVASGAGLVaLP-- 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 6322779   158 plSVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK06484 150 --KRTAYSASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQM 191
PRK06500 PRK06500
SDR family oxidoreductase;
11-230 2.55e-09

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 56.12  E-value: 2.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILSAStGNTVITSIRGSPSLPKNKqvedlAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGID 90
Cdd:PRK06500  11 ITGGTSGIGLETARQFLAE-GARVAITGRDPASLEAAR-----AELGESALVIRADAGDVAAQKALAQALAEA--FGRLD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    91 IFIACSAVSDsYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKktrkiffiSSVA--GSINAFV--PLSvSAYGQ 166
Cdd:PRK06500  83 AVFINAGVAK-FAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANP--------ASIVlnGSINAHIgmPNS-SVYAA 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322779   167 SKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTD-MGQYGLDHFKEKNIDISGVNII------TPEESASA 230
Cdd:PRK06500 153 SKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPlYGKLGLPEATLDAVAAQIQALVplgrfgTPEEIAKA 223
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
10-230 3.88e-09

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 56.78  E-value: 3.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    10 FIIGGSRGIGFNLVKILSASTGNTVITSIRGSPSlpkNKQVEDLAKIRKNIhIVQLDLTKDESIGNIADEIKKTpfFLGI 89
Cdd:PRK08324 426 LVTGAAGGIGKATAKRLAAEGACVVLADLDEEAA---EAAAAELGGPDRAL-GVACDVTDEAAVQAAFEEAALA--FGGV 499

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    90 DIFIACSAVSDSYyKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTR-KIFFISSVagsiNAFVP-LSVSAYGQS 167
Cdd:PRK08324 500 DIVVSNAGIAISG-PIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLGgSIVFIASK----NAVNPgPNFGAYGAA 574

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   168 KAALNYAVKTLSFELKPEGFTVVAFHP------------GMVSTDMGQYGLD------HFKEKNidISGVNiITPEESAS 229
Cdd:PRK08324 575 KAAELHLVRQLALELGPDGIRVNGVNPdavvrgsgiwtgEWIEARAAAYGLSeeeleeFYRARN--LLKRE-VTPEDVAE 651


                 .
gi 6322779   230 A 230
Cdd:PRK08324 652 A 652
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 13-201 4.40e-09

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: 55.53  E-value: 4.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   13 GGSRGIGFNLVKILsASTGNTVitSIRGSPSLPKNKQVEDLAKIRKNI-HIVQLDLTKDESIGNIADEI-KKTPFFLGID 90
Cdd:cd09763  10 GASRGIGRGIALQL-GEAGATV--YITGRTILPQLPGTAEEIEARGGKcIPVRCDHSDDDEVEALFERVaREQQGRLDIL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   91 IFIACSAVSDSYYKV----LETPKSVW--------LNHYSTNALGPilalqkvyPLLLLKKTRKIFFISSVAGSINAFVP 158
Cdd:cd09763  87 VNNAYAAVQLILVGVakpfWEEPPTIWddinnvglRAHYACSVYAA--------PLMVKAGKGLIVIISSTGGLEYLFNV 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 6322779  159 lsvsAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:cd09763 159 ----AYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTEL 197
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 10-212 5.01e-09

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: 55.42  E-value: 5.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   10 FIIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLpkNKQVEDLAKIRKN-IHIVQLDLTKDESIGNIADeiKKTPFFLG 88
Cdd:cd08930   6 LITGAAGLIGKAFCKAL-LSAGARLILADINAPAL--EQLKEELTNLYKNrVIALELDITSKESIKELIE--SYLEKFGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   89 IDIFIACSAVSDSYY--KVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAFV-------PL 159
Cdd:cd08930  81 IDILINNAYPSPKVWgsRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIAPDFriyentqMY 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 6322779  160 SVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLDHFKEK 212
Cdd:cd08930 161 SPVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNNQPSEFLEKYTKK 213
PRK06101 PRK06101
SDR family oxidoreductase;
8-199 1.00e-08

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 54.49  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     8 TYFIIGGSRGIGFNLVKILsASTGNTVITSIRgspslpkNKQV-EDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTPff 86
Cdd:PRK06101   3 AVLITGATSGIGKQLALDY-AKQGWQVIACGR-------NQSVlDELHTQSANIFTLAFDVTDHPGTKAALSQLPFIP-- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    87 lGIDIFIA--CSAVSDSYYKVletpkSVWLNHYSTNALGPILALQKVYPLLllKKTRKIFFISSVAGSINafVPlSVSAY 164
Cdd:PRK06101  73 -ELWIFNAgdCEYMDDGKVDA-----TLMARVFNVNVLGVANCIEGIQPHL--SCGHRVVIVGSIASELA--LP-RAEAY 141

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 6322779   165 GQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVST 199
Cdd:PRK06101 142 GASKAAVAYFARTLQLDLRPKGIEVVTVFPGFVAT 176
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 11-201 1.17e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 54.65  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILsASTGNTVITSIRgspSLPKNKQVedLAKIRK-----NIHIVQLDLTKDESIGNIADEIKKTpf 85
Cdd:PRK06197  21 VTGANTGLGYETAAAL-AAKGAHVVLAVR---NLDKGKAA--AARITAatpgaDVTLQELDLTSLASVRAAADALRAA-- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    86 FLGIDIFIACSAVsdsyykvLETPKSVWLN----HYSTNALGPiLALQKvypLLL--LKKTR--KIFFISSVAGSINA-- 155
Cdd:PRK06197  93 YPRIDLLINNAGV-------MYTPKQTTADgfelQFGTNHLGH-FALTG---LLLdrLLPVPgsRVVTVSSGGHRIRAai 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6322779   156 -FVPLS-------VSAYGQSKAALNYAVKTLSFELKPEGFT--VVAFHPGMVSTDM 201
Cdd:PRK06197 162 hFDDLQwerrynrVAAYGQSKLANLLFTYELQRRLAAAGATtiAVAAHPGVSNTEL 217
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 11-200 1.21e-08

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 54.00  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKiLSASTGNTVITSIRGSPSLPKNKQveDLAKIrKNIHIVQLDLTKDESIGNIADEIKKtpFFLGID 90
Cdd:PRK05786  10 IIGVSEGLGYAVAY-FALKEGAQVCINSRNENKLKRMKK--TLSKY-GNIHYVVGDVSSTESARNVIEKAAK--VLNAID 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    91 --IFIACSAVSDSyykvLETPKSvwLNHYSTNAL-GPILALQKVYPLLllKKTRKIFFISSVAGSINAFvPLSVSaYGQS 167
Cdd:PRK05786  84 glVVTVGGYVEDT----VEEFSG--LEEMLTNHIkIPLYAVNASLRFL--KEGSSIVLVSSMSGIYKAS-PDQLS-YAVA 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 6322779   168 KAALNYAVKTLSFELKPEGFTVVAFHPGMVSTD 200
Cdd:PRK05786 154 KAGLAKAVEILASELLGRGIRVNGIAPTTISGD 186
PRK05867 PRK05867
SDR family oxidoreductase;
10-201 1.35e-08

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 54.27  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    10 FIIGGSRGIGfNLVKILSASTGNTVITSIRGSPSLpkNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIkkTPFFLGI 89
Cdd:PRK05867  13 LITGASTGIG-KRVALAYVEAGAQVAIAARHLDAL--EKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQV--TAELGGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    90 DIFIaCSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLK-KTRKIFFISSVAGSInAFVPLSVSAYGQSK 168
Cdd:PRK05867  88 DIAV-CNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQgQGGVIINTASMSGHI-INVPQQVSHYCASK 165

                        170       180       190
                 ....*....|....*....|....*....|...
gi 6322779   169 AALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK05867 166 AAVIHLTKAMAVELAPHKIRVNSVSPGYILTEL 198
PRK05693 PRK05693
SDR family oxidoreductase;
8-203 1.56e-08

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 54.03  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     8 TYFIIGGSRGIGFNLVKILSAsTGNTVITSIRgspslpKNKQVEDLAKirKNIHIVQLDLTKDESIGNIADEIKKTpfFL 87
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKA-AGYEVWATAR------KAEDVEALAA--AGFTAVQLDVNDGAALARLAEELEAE--HG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    88 GIDIFIAcSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRkIFFISSVAGsinAFVPLSVSAYGQS 167
Cdd:PRK05693  72 GLDVLIN-NAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSRGL-VVNIGSVSG---VLVTPFAGAYCAS 146

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 6322779   168 KAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQ 203
Cdd:PRK05693 147 KAAVHALSDALRLELAPFGVQVMEVQPGAIASQFAS 182
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 11-200 1.65e-08

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


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 53.73  E-value: 1.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGFNLVKILSASTGNTVITSIRGSPSlpkNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGID 90
Cdd:cd05365   4 VTGGAAGIGKAIAGTLAKAGASVVIADLKSEGA---EAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQ--FGGIT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   91 IFIacSAVSDSYYKVLETPKSV--WLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAFvplSVSAYGQSK 168
Cdd:cd05365  79 ILV--NNAGGGGPKPFDMPMTEedFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNV---RIAAYGSSK 153

                       170       180       190
                ....*....|....*....|....*....|..
gi 6322779  169 AALNYAVKTLSFELKPEGFTVVAFHPGMVSTD 200
Cdd:cd05365 154 AAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTD 185
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 8-202 2.13e-08

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 53.48  E-value: 2.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     8 TYFIIGGSRGIGFNLVKILSASTGNTVITSIrgSPSLPKNKqvedlakirkNIHIVQLDLTKDESIGNIADEIKKTpfFL 87
Cdd:PRK06171  11 IIIVTGGSSGIGLAIVKELLANGANVVNADI--HGGDGQHE----------NYQFVPTDVSSAEEVNHTVAEIIEK--FG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    88 GIDIFIACSAVSdsYYKVLETPK----------SVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAfv 157
Cdd:PRK06171  77 RIDGLVNNAGIN--IPRLLVDEKdpagkyelneAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGS-- 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 6322779   158 pLSVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPG-MVSTDMG 202
Cdd:PRK06171 153 -EGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGiLEATGLR 197
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 11-231 2.63e-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: 53.16  E-value: 2.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGFNLVKILSASTGNTVITSIRGSPSlpknKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGID 90
Cdd:cd08943   6 VTGGASGIGLAIAKRLAAEGAAVVVADIDPEIA----EKVAEAAQGGPRALGVQCDVTSEAQVQSAFEQAVLE--FGGLD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   91 IFIACSAVSDSYyKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKT--RKIFFIS--SVAGSINAfvplsvSAYGQ 166
Cdd:cd08943  80 IVVSNAGIATSS-PIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIggNIVFNASknAVAPGPNA------AAYSA 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322779  167 SKAALNYAVKTLSFELKPEGFTVVAFHP-----GMVSTDMG-------QYGL--DHFKEKNidISGVNiITPEESASAL 231
Cdd:cd08943 153 AKAAEAHLARCLALEGGEDGIRVNTVNPdavfrGSKIWEGVwraarakAYGLleEEYRTRN--LLKRE-VLPEDVAEAV 228
PRK12743 PRK12743
SDR family oxidoreductase;
61-207 2.95e-08

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 53.11  E-value: 2.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    61 HIVQLDLTKDESIGNIADEIKKTpfFLGIDIFIACSAVSDSYyKVLETPKSVWLNHYSTNALGPILALQKVyPLLLLKKT 140
Cdd:PRK12743  55 EIRQLDLSDLPEGAQALDKLIQR--LGRIDVLVNNAGAMTKA-PFLDMDFDEWRKIFTVDVDGAFLCSQIA-ARHMVKQG 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322779   141 R--KIFFISSVagsiNAFVPLSV-SAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM-GQYGLD 207
Cdd:PRK12743 131 QggRIINITSV----HEHTPLPGaSAYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIATPMnGMDDSD 197
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 88-231 3.50e-08

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: 52.93  E-value: 3.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   88 GIDIFIACSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAgsinAFVPL-SVSAYGQ 166
Cdd:cd08936  87 GVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVA----AFHPFpGLGPYNV 162

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322779  167 SKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTD------MGQYGLDHFKEKnIDISgvNIITPEESASAL 231
Cdd:cd08936 163 SKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSfssalwMDKAVEESMKET-LRIR--RLGQPEDCAGIV 230
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 8-232 3.85e-08

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: 52.87  E-value: 3.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIGGSRGIGFNLVK-ILSAstGNTVITSIRGSPSLpkNKQVEDLAKIrKNIHIVQLDLTKDESIGNIADEIKKTPFF 86
Cdd:cd08942   8 IVLVTGGSRGIGRMIAQgFLEA--GARVIISARKAEAC--ADAAEELSAY-GECIAIPADLSSEEGIEALVARVAERSDR 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   87 LgiDIFI-----ACSAVSDSYykvletPKSVWLNHYSTNALGPILALQKVYPLLLLKKT----RKIFFISSVAGSINAFv 157
Cdd:cd08942  83 L--DVLVnnagaTWGAPLEAF------PESGWDKVMDINVKSVFFLTQALLPLLRAAATaenpARVINIGSIAGIVVSG- 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322779  158 pLSVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLDH---FKEKNIDISGVNIITPEESASALI 232
Cdd:cd08942 154 -LENYSYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLLNDpaaLEAEEKSIPLGRWGRPEDMAGLAI 230
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 10-201 3.98e-08

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 52.80  E-value: 3.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    10 FIIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLPKNKQ--VEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFL 87
Cdd:PRK12827  10 LITGGSGGLGRAIAVRL-AADGADVIVLDIHPMRGRAEADavAAGIEAAGGKALGLAFDVRDFAATRAALDAGVEE--FG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    88 GIDIFIACSAVSDsYYKVLETPKSVWLNHYSTNALGPILALQKV-YPLLLLKKTRKIFFISSVAGSI--NAFVPlsvsaY 164
Cdd:PRK12827  87 RLDILVNNAGIAT-DAAFAELSIEEWDDVIDVNLDGFFNVTQAAlPPMIRARRGGRIVNIASVAGVRgnRGQVN-----Y 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 6322779   165 GQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK12827 161 AASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPM 197
PRK06949 PRK06949
SDR family oxidoreductase;
1-204 4.14e-08

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 52.84  E-value: 4.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     1 MNTSSRITyFIIGGSRGIGFNLVKILSASTGNTVITSIRgspslpknkqVEDLAKIRKNI-------HIVQLDLTKDESI 73
Cdd:PRK06949   5 INLEGKVA-LVTGASSGLGARFAQVLAQAGAKVVLASRR----------VERLKELRAEIeaeggaaHVVSLDVTDYQSI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    74 -GNIAD-EIKKTPfflgIDIFIACSAVSDSYYKVLETPKSvWLNHYSTNALGPILALQKVYPLLLL--------KKTRKI 143
Cdd:PRK06949  74 kAAVAHaETEAGT----IDILVNNSGVSTTQKLVDVTPAD-FDFVFDTNTRGAFFVAQEVAKRMIArakgagntKPGGRI 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322779   144 FFISSVAGsinAFVPLSVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQY 204
Cdd:PRK06949 149 INIASVAG---LRVLPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHH 206
PRK08219 PRK08219
SDR family oxidoreductase;
4-230 4.54e-08

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 52.24  E-value: 4.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     4 SSRITYFIIGGSRGIGFNLVKILSasTGNTVITSIRGSPSLPKnkqvedLAKIRKNIHIVQLDLTKDESIGNIADEIKKt 83
Cdd:PRK08219   1 MERPTALITGASRGIGAAIARELA--PTHTLLLGGRPAERLDE------LAAELPGATPFPVDLTDPEAIAAAVEQLGR- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    84 pfflgIDIFIACSAVSDsYYKVLETPKSVWLNHYSTNALGPIlALQkvypLLLLKKTR----KIFFISSVAGsINAFVpl 159
Cdd:PRK08219  72 -----LDVLVHNAGVAD-LGPVAESTVDEWRATLEVNVVAPA-ELT----RLLLPALRaahgHVVFINSGAG-LRANP-- 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322779   160 SVSAYGQSKAALNYAVKTLSFElKPEGFTVVAFHPGMVSTDMgQYGLDHFKEKNIDisGVNIITPEESASA 230
Cdd:PRK08219 138 GWGSYAASKFALRALADALREE-EPGNVRVTSVHPGRTDTDM-QRGLVAQEGGEYD--PERYLRPETVAKA 204
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 10-201 4.59e-08

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: 52.54  E-value: 4.59e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   10 FIIGGSRGIGFNLVKILSASTGNTVITSIRgspslpknkqVEDLAKIRKNI-------HIVQLDLTkDESIGNIAdeIKK 82
Cdd:cd08934   7 LVTGASSGIGEATARALAAEGAAVAIAARR----------VDRLEALADELeaeggkaLVLELDVT-DEQQVDAA--VER 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   83 TPFFLG-IDIFIACSAVSdSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINafVPLSV 161
Cdd:cd08934  74 TVEALGrLDILVNNAGIM-LLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVA--VRNSA 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 6322779  162 sAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:cd08934 151 -VYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTEL 189
PRK06182 PRK06182
short chain dehydrogenase; Validated
 10-211 4.78e-08

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 52.65  E-value: 4.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    10 FIIGGSRGIGFNLVKILSAStGNTVITSIRgspSLPKnkqVEDLAKIrkNIHIVQLDLTKDESIGNIADEI-KKTPfflG 88
Cdd:PRK06182   7 LVTGASSGIGKATARRLAAQ-GYTVYGAAR---RVDK---MEDLASL--GVHPLSLDVTDEASIKAAVDTIiAEEG---R 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    89 IDIFIAcSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSInaFVPLSvSAYGQSK 168
Cdd:PRK06182  75 IDVLVN-NAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKI--YTPLG-AWYHATK 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 6322779   169 AALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLDHFKE 211
Cdd:PRK06182 151 FALEGFSDALRLEVAPFGIDVVVIEPGGIKTEWGDIAADHLLK 193
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 11-201 5.26e-08

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 52.31  E-value: 5.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLPKNkQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGID 90
Cdd:PRK12935  11 VTGGAKGIGKAITVAL-AQEGAKVVINYNSSKEAAEN-LVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNH--FGKVD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    91 IFIACSAVS-DSYYKVLEtpKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAFvplSVSAYGQSKA 169
Cdd:PRK12935  87 ILVNNAGITrDRTFKKLN--REDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGF---GQTNYSAAKA 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 6322779   170 ALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK12935 162 GMLGFTKSLALELAKTNVTVNAICPGFIDTEM 193
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 11-203 5.31e-08

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: 52.39  E-value: 5.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGFNLVKILSASTGNTVITSIRGSpslpKNKQVedLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGID 90
Cdd:cd05341  10 VTGGARGLGLAHARLLVAEGAKVVLSDILDE----EGQAA--AAELGDAARFFHLDVTDEDGWTAVVDTAREA--FGRLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   91 IFIACSAVSDSYYkVLETPKSVWLNHYSTNALGPILALQKVYPllLLKKTRK--IFFISSVAGsinaFVPL-SVSAYGQS 167
Cdd:cd05341  82 VLVNNAGILTGGT-VETTTLEEWRRLLDINLTGVFLGTRAVIP--PMKEAGGgsIINMSSIEG----LVGDpALAAYNAS 154

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 6322779  168 KAALNYAVKTLSFELKPEGFT--VVAFHPGMVSTDMGQ 203
Cdd:cd05341 155 KGAVRGLTKSAALECATQGYGirVNSVHPGYIYTPMTD 192
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 10-204 1.06e-07

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: 51.51  E-value: 1.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   10 FIIGGSRGIGFNLVKILSaSTGNTVITSIrgspsLPKN-KQVEDLAKI-RKNIHIVQLDLTKDESIGNIADEIK-KTP-- 84
Cdd:cd09805   4 LITGCDSGFGNLLAKKLD-SLGFTVLAGC-----LTKNgPGAKELRRVcSDRLRTLQLDVTKPEQIKRAAQWVKeHVGek 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   85 --FFL----GIDIFIACSAVS--DSYYKVLETpksvwlnhystNALGPILALQKVYPLLllKKTR-KIFFISSVAGSINA 155
Cdd:cd09805  78 glWGLvnnaGILGFGGDEELLpmDDYRKCMEV-----------NLFGTVEVTKAFLPLL--RRAKgRVVNVSSMGGRVPF 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 6322779  156 FVplsVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQY 204
Cdd:cd09805 145 PA---GGAYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGN 190
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 11-205 1.14e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 51.20  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILSASTGNTVItsirgspsLPKNKQVEDLAK--IRKNIHIVQLDLTKDESIGNIADEIKKTpfFLG 88
Cdd:PRK06841  20 VTGGASGIGHAIAELFAAKGARVAL--------LDRSEDVAEVAAqlLGGNAKGLVCDVSDSQSVEAAVAAVISA--FGR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    89 IDIFIACSAVSdSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINafVPLSVsAYGQSK 168
Cdd:PRK06841  90 IDILVNSAGVA-LLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVA--LERHV-AYCASK 165

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 6322779   169 AALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYG 205
Cdd:PRK06841 166 AGVVGMTKVLALEWGPYGITVNAISPTVVLTELGKKA 202
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-201 1.31e-07

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 51.12  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     8 TYFIIGGSRGIGFNLVKILSAStGNTVItsirgspSLPKNKQvedlAKIRKNIHIVQLDLTKDesIGNIADEIKKtpffl 87
Cdd:PRK06550   7 TVLITGAASGIGLAQARAFLAQ-GAQVY-------GVDKQDK----PDLSGNFHFLQLDLSDD--LEPLFDWVPS----- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    88 gIDIFIACSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAFvplSVSAYGQS 167
Cdd:PRK06550  68 -VDILCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGG---GGAAYTAS 143

                        170       180       190
                 ....*....|....*....|....*....|....
gi 6322779   168 KAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK06550 144 KHALAGFTKQLALDYAKDGIQVFGIAPGAVKTPM 177
PRK06484 PRK06484
short chain dehydrogenase; Validated
 11-199 1.53e-07

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 51.77  E-value: 1.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLPKnkqvedLAKIRKNIHIV-QLDLTKDESIGNIADEIKKTpfFLGI 89
Cdd:PRK06484 274 ITGGARGIGRAVADRF-AAAGDRLLIIDRDAEGAKK------LAEALGDEHLSvQADITDEAAVESAFAQIQAR--WGRL 344

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    90 DIFIACSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVypLLLLKKTRKIFFIssvaGSINAFVPLSVS-AYGQSK 168
Cdd:PRK06484 345 DVLVNNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAA--ARLMSQGGVIVNL----GSIASLLALPPRnAYCASK 418

                        170       180       190
                 ....*....|....*....|....*....|.
gi 6322779   169 AALNYAVKTLSFELKPEGFTVVAFHPGMVST 199
Cdd:PRK06484 419 AAVTMLSRSLACEWAPAGIRVNTVAPGYIET 449
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-201 2.34e-07

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 50.35  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     6 RITYFIIGGSRGIGFNLVKILSASTGNTVITSIRGSPSLpkNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKtpF 85
Cdd:PRK12745   2 RPVALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEEL--AATQQELRALGVEVIFFPADVADLSAHEAMLDAAQA--A 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    86 FLGIDIFIACSAVS-----DsyykVLE-TPKSvWLNHYSTNALGPILALQKVYPLLLLKKT------RKIFFISSV---A 150
Cdd:PRK12745  78 WGRIDCLVNNAGVGvkvrgD----LLDlTPES-FDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphRSIVFVSSVnaiM 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6322779   151 GSINAfvplsvSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK12745 153 VSPNR------GEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDM 197
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
8-197 2.36e-07

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 50.75  E-value: 2.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIGGSRGIGFNLVKILSAStGNTVITSIRGSPSLPKNKQVEdlakirkNIHIVQLDLTKDESIgniadeikkTPFFL 87
Cdd:COG0451   1 RILVTGGAGFIGSHLARRLLAR-GHEVVGLDRSPPGAANLAALP-------GVEFVRGDLRDPEAL---------AAALA 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   88 GIDIFIACSAVSDSYYkvlETPKSVWlnhySTNALGPILALQkvypLLLLKKTRKIFFISSVA--GsiNAFVPLS----- 160
Cdd:COG0451  64 GVDAVVHLAAPAGVGE---EDPDETL----EVNVEGTLNLLE----AARAAGVKRFVYASSSSvyG--DGEGPIDedtpl 130

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 6322779  161 --VSAYGQSKAALNYAVKTLSfelKPEGFTVVAFHPGMV 197
Cdd:COG0451 131 rpVSPYGASKLAAELLARAYA---RRYGLPVTILRPGNV 166
PRK06181 PRK06181
SDR family oxidoreductase;
11-234 3.28e-07

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 49.98  E-value: 3.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILSASTGNTVITSIRGSpslpknkQVEDLAKIRKNIH----IVQLDLTKDES-IGNIADEIKKtpf 85
Cdd:PRK06181   6 ITGASEGIGRALAVRLARAGAQLVLAARNET-------RLASLAQELADHGgealVVPTDVSDAEAcERLIEAAVAR--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    86 FLGIDIFIACSAVS-DSYYKVLETPkSVWLNHYSTNALGPILALQKVYPLLllKKTR-KIFFISSVAGSINafVPlSVSA 163
Cdd:PRK06181  76 FGGIDILVNNAGITmWSRFDELTDL-SVFERVMRVNYLGAVYCTHAALPHL--KASRgQIVVVSSLAGLTG--VP-TRSG 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322779   164 YGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLDH----FKEKNIDISGvnIITPEESASALIDV 234
Cdd:PRK06181 150 YAASKHALHGFFDSLRIELADDGVAVTVVCPGFVATDIRKRALDGdgkpLGKSPMQESK--IMSAEECAEAILPA 222
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 11-232 3.73e-07

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 49.72  E-value: 3.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILSASTGNTVITSIRGSPSLpkNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGID 90
Cdd:PRK06077  11 VTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEM--NETLKMVKENGGEGIGVLADVSTREGCETLAKATIDR--YGVAD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    91 IFIACSAVSdSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLllKKTRKIFFISSVAGsINAFVPLSVsaYGQSKAA 170
Cdd:PRK06077  87 ILVNNAGLG-LFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAG-IRPAYGLSI--YGAMKAA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322779   171 LNYAVKTLSFELKPEgFTVVAFHPGMVSTDMGQ--YGLDHFKE----KNIDISGvNIITPEESASALI 232
Cdd:PRK06077 161 VINLTKYLALELAPK-IRVNAIAPGFVKTKLGEslFKVLGMSEkefaEKFTLMG-KILDPEEVAEFVA 226
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 11-202 7.37e-07

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: 48.95  E-value: 7.37e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGFNlVKILSASTGNTVITSIRGSPSLPKNKQ-VEDLAKIRKNIHIVQLDLTKDESIGNIADE-IKKtpfFLG 88
Cdd:cd05364   8 ITGSSSGIGAG-TAILFARLGARLALTGRDAERLEETRQsCLQAGVSEKKILLVVADLTEEEGQDRIISTtLAK---FGR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   89 IDIFI--ACSAVSDS--------YYKVLetpksvwlnhySTNALGPILALQKVYPLLLLKKTrKIFFISSVAGSIN-AFV 157
Cdd:cd05364  84 LDILVnnAGILAKGGgedqdieeYDKVM-----------NLNLRAVIYLTKLAVPHLIKTKG-EIVNVSSVAGGRSfPGV 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 6322779  158 PlsvsAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMG 202
Cdd:cd05364 152 L----YYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFH 192
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
8-201 8.37e-07

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 49.03  E-value: 8.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     8 TYFIIGGSRGIGFNLVKILSASTGNTVITSIrgSPSlpknkqVEDLAK-IRKNIH---IVQLDLTKDESIGNIADEIKKT 83
Cdd:PRK08226   8 TALITGALQGIGEGIARVFARHGANLILLDI--SPE------IEKLADeLCGRGHrctAVVADVRDPASVAAAIKRAKEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    84 pfFLGIDIFIaCSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAfvPLSVSA 163
Cdd:PRK08226  80 --EGRIDILV-NNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGDMVA--DPGETA 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 6322779   164 YGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK08226 155 YALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPM 192
PRK08589 PRK08589
SDR family oxidoreductase;
11-199 1.10e-06

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 48.62  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILsASTGNTVItsirgspSLPKNKQVEDLA-KIRKN---IHIVQLDLTKDESIGNIADEIKKTpfF 86
Cdd:PRK08589  11 ITGASTGIGQASAIAL-AQEGAYVL-------AVDIAEAVSETVdKIKSNggkAKAYHVDISDEQQVKDFASEIKEQ--F 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    87 LGIDIFIACSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLlKKTRKIFFISSVAGSInafVPLSVSAYGQ 166
Cdd:PRK08589  81 GRVDVLFNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMM-EQGGSIINTSSFSGQA---ADLYRSGYNA 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 6322779   167 SKAALNYAVKTLSFELKPEGFTVVAFHPGMVST 199
Cdd:PRK08589 157 AKGAVINFTKSIAIEYGRDGIRANAIAPGTIET 189
PRK07774 PRK07774
SDR family oxidoreductase;
8-200 1.21e-06

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 48.20  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     8 TYFIIGGSRGIGFNLVKILSASTGNTVITSIRGSPSLPKNKQVedLAKIRKNIHiVQLDLTKDESIGNIADEIKKTpfFL 87
Cdd:PRK07774   8 VAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQI--VADGGTAIA-VQVDVSDPDSAKAMADATVSA--FG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    88 GIDIFIACSAVSDSY--YKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAgsinAFVPLSVsaYG 165
Cdd:PRK07774  83 GIDYLVNNAAIYGGMklDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTA----AWLYSNF--YG 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 6322779   166 QSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTD 200
Cdd:PRK07774 157 LAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTE 191
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 8-204 1.29e-06

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 48.23  E-value: 1.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIGGSRGIGFNLVKILsASTGNTVITSIRGspslpKNKQVEDLAKIRK---NIHIV--QLDLTKDESIGNIADEIKK 82
Cdd:cd09807   3 TVIITGANTGIGKETAREL-ARRGARVIMACRD-----MAKCEEAAAEIRRdtlNHEVIvrHLDLASLKSIRAFAAEFLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   83 TPFFLgiDIFIACSAVsdsyykvLETPKSV----WLNHYSTNALGPILAlqkVYPLL-LLKKT--RKIFFISSVA---GS 152
Cdd:cd09807  77 EEDRL--DVLINNAGV-------MRCPYSKtedgFEMQFGVNHLGHFLL---TNLLLdLLKKSapSRIVNVSSLAhkaGK 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6322779  153 INaFVPL-------SVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQY 204
Cdd:cd09807 145 IN-FDDLnseksynTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELGRH 202
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 8-201 1.65e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 47.87  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     8 TYFIIGGSRGIGFNLVKILSASTGNTVITSiRGSPSLPKNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIkkTPFFL 87
Cdd:PRK05875   9 TYLVTGGGSGIGKGVAAGLVAAGAAVMIVG-RNPDKLAAAAEEIEALKGAGAVRYEPADVTDEDQVARAVDAA--TAWHG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    88 GIDIFIACSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSiNA---FvplsvSAY 164
Cdd:PRK05875  86 RLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAAS-NThrwF-----GAY 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 6322779   165 GQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK05875 160 GVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDL 196
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 10-200 1.74e-06

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 47.93  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    10 FIIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLPKNKQvedlaKIRK----NIHIVQLDLTKDESIGNIADEIKKtpf 85
Cdd:PRK08339  12 FTTASSKGIGFGVARVL-ARAGADVILLSRNEENLKKARE-----KIKSesnvDVSYIVADLTKREDLERTVKELKN--- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    86 fLGI-DIFIACSAVSDSYYkVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAgsINAFVPlSVSAY 164
Cdd:PRK08339  83 -IGEpDIFFFSTGGPKPGY-FMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVA--IKEPIP-NIALS 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 6322779   165 GQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTD 200
Cdd:PRK08339 158 NVVRISMAGLVRTLAKELGPKGITVNGIMPGIIRTD 193
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
11-201 2.54e-06

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 47.33  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILSASTGNTVITSIRGSPSlpknkqVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGID 90
Cdd:PRK07067  11 LTGAASGIGEAVAERYLAEGARVVIADIKPARA------RLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVER--FGGID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    91 IFIACSAVSDSYyKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLK-KTRKIFFISSVAGSINAfvPLsVSAYGQSKA 169
Cdd:PRK07067  83 ILFNNAALFDMA-PILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQgRGGKIINMASQAGRRGE--AL-VSHYCATKA 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 6322779   170 ALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK07067 159 AVISYTQSAALALIRHGINVNAIAPGVVDTPM 190
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 8-201 3.04e-06

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 47.25  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     8 TYFIIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLpkNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFL 87
Cdd:PRK08213  14 TALVTGGSRGLGLQIAEAL-GEAGARVVLSARKAEEL--EEAAAHLEALGIDALWIAADVADEADIERLAEETLER--FG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    88 GIDIFIACSAVSDSyYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLK-KTRKIFFISSVAGsINAFVP--LSVSAY 164
Cdd:PRK08213  89 HVDILVNNAGATWG-APAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRSMIPrGYGRIINVASVAG-LGGNPPevMDTIAY 166

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 6322779   165 GQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK08213 167 NTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKM 203
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 13-195 4.22e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 46.54  E-value: 4.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    13 GGSRGIGFNLVKILSASTGNTVITSIrgspSLPKNKQVEdlAKIRKNIHIVQLDLTKDESIGN-IADEIKKtpfFLGIDI 91
Cdd:PRK08265  13 GGATLIGAAVARALVAAGARVAIVDI----DADNGAAVA--ASLGERARFIATDITDDAAIERaVATVVAR---FGRVDI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    92 FI--ACSAVSDSyykvLETPKSVWLNHYSTNALGPILALQKVYPLLllkktrkiffiSSVAGSINAFVplSVSA------ 163
Cdd:PRK08265  84 LVnlACTYLDDG----LASSRADWLAALDVNLVSAAMLAQAAHPHL-----------ARGGGAIVNFT--SISAkfaqtg 146

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 6322779   164 ---YGQSKAALNYAVKTLSFELKPEGFTVVAFHPG 195
Cdd:PRK08265 147 rwlYPASKAAIRQLTRSMAMDLAPDGIRVNSVSPG 181
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 10-202 5.73e-06

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: 46.04  E-value: 5.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   10 FIIGGSRGIGFNLVKILSASTGNTVITSIRgspsLPKNKQ-VEDLAKIRKN-IHIVQLDLTKDESIGNIADEIKKTpfFL 87
Cdd:cd05369   7 FITGGGTGIGKAIAKAFAELGASVAIAGRK----PEVLEAaAEEISSATGGrAHPIQCDVRDPEAVEAAVDETLKE--FG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   88 GIDIFIACSA---VSDSyykvlE--TPKSvWLNHYSTNALGPILALQKVYPLLLLKKTR-KIFFISS-VAGSINAFVPLS 160
Cdd:cd05369  81 KIDILINNAAgnfLAPA-----EslSPNG-FKTVIDIDLNGTFNTTKAVGKRLIEAKHGgSILNISAtYAYTGSPFQVHS 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 6322779  161 VSAygqsKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMG 202
Cdd:cd05369 155 AAA----KAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTEG 192
PRK07856 PRK07856
SDR family oxidoreductase;
13-205 6.10e-06

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 46.08  E-value: 6.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    13 GGSRGIGFNLVKILSAStGNTVITSIRGSPSLPKNKQVedlakirkniHIVQLDLTKDESIGNIADEIKKTpfFLGIDIF 92
Cdd:PRK07856  13 GGTRGIGAGIARAFLAA-GATVVVCGRRAPETVDGRPA----------EFHAADVRDPDQVAALVDAIVER--HGRLDVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    93 I----------ACSAVSDSYYKVLETpksvwlnhystNALGPILALQKVYPLLLLKKTR-KIFFISSVAGSINAfvPLSv 161
Cdd:PRK07856  80 VnnaggspyalAAEASPRFHEKIVEL-----------NLLAPLLVAQAANAVMQQQPGGgSIVNIGSVSGRRPS--PGT- 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 6322779   162 SAYGQSKAALNYAVKTLSFELKPEgFTVVAFHPGMVSTDMGQ--YG 205
Cdd:PRK07856 146 AAYGAAKAGLLNLTRSLAVEWAPK-VRVNAVVVGLVRTEQSElhYG 190
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 11-202 1.06e-05

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 45.55  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSR--GIGFNLVKILSASTGNTVITSIRG-SPSLP----KNKQVEDLAKIRKN---IHIVQLDLTKDESIGNIADEI 80
Cdd:PRK12859  11 VTGVSRldGIGAAICKELAEAGADIFFTYWTAyDKEMPwgvdQDEQIQLQEELLKNgvkVSSMELDLTQNDAPKELLNKV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    81 KKTpffLGI-DIFI--ACSAVSDSYykvlETPKSVWLN-HYSTNALGPILALQKVYPLLLLKKTRKIffISSVAGSINAF 156
Cdd:PRK12859  91 TEQ---LGYpHILVnnAAYSTNNDF----SNLTAEELDkHYMVNVRATTLLSSQFARGFDKKSGGRI--INMTSGQFQGP 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 6322779   157 VPlSVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGmvSTDMG 202
Cdd:PRK12859 162 MV-GELAYAATKGAIDALTSSLAAEVAHLGITVNAINPG--PTDTG 204
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 8-201 1.07e-05

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 45.26  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     8 TYFIIGGSRGIGFNLVKILsASTGNTVI---TSIRGSPSLPknkqvedlakirknIHIVQLDLTKDESIGNIADEIKKTp 84
Cdd:PRK08220  10 TVWVTGAAQGIGYAVALAF-VEAGAKVIgfdQAFLTQEDYP--------------FATFVLDVSDAAAVAQVCQRLLAE- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    85 fFLGIDIFIACSAVsdsyykvL------ETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAgsinAFVP 158
Cdd:PRK08220  74 -TGPLDVLVNAAGI-------LrmgatdSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNA----AHVP 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 6322779   159 -LSVSAYGQSKAALNYAVKTLSFELKPEGF--TVVAfhPGMVSTDM 201
Cdd:PRK08220 142 rIGMAAYGASKAALTSLAKCVGLELAPYGVrcNVVS--PGSTDTDM 185
PRK05650 PRK05650
SDR family oxidoreductase;
61-202 1.35e-05

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 45.42  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    61 HIVQLDLTKDESIGNIADEIKKTpfFLGIDIFIACSAVSdSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKT 140
Cdd:PRK05650  52 FYQRCDVRDYSQLTALAQACEEK--WGGIDVIVNNAGVA-SGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKS 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322779   141 RKIFFISSVAGSINAfvPLSVSaYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMG 202
Cdd:PRK05650 129 GRIVNIASMAGLMQG--PAMSS-YNVAKAGVVALSETLLVELADDEIGVHVVCPSFFQTNLL 187
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 11-200 1.39e-05

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 45.22  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILSASTGNTVITSIRGSPSlpkNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADeiKKTPFFLGID 90
Cdd:PRK06113  16 ITGAGAGIGKEIAITFATAGASVVVSDINADAA---NHVVDEIQQLGGQAFACRCDITSEQELSALAD--FALSKLGKVD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    91 IFIACSAVSDSyyKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSiNAFVplSVSAYGQSKAA 170
Cdd:PRK06113  91 ILVNNAGGGGP--KPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAE-NKNI--NMTSYASSKAA 165

                        170       180       190
                 ....*....|....*....|....*....|
gi 6322779   171 LNYAVKTLSFELKPEGFTVVAFHPGMVSTD 200
Cdd:PRK06113 166 ASHLVRNMAFDLGEKNIRVNGIAPGAILTD 195
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 6-201 1.40e-05

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: 45.15  E-value: 1.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    6 RITYFIIGGSRGIGFNLVKILSAstGNTVITSIRGSPSLPKNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpf 85
Cdd:cd05337   1 RPVAIVTGASRGIGRAIATELAA--RGFDIAINDLPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWED-- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   86 FLGIDIFIACSAVSDSYYK-VLETPKSVWLNHYSTNALGPILALQKV------YPLLLLKKTRKIFFISSvagsINAF-V 157
Cdd:cd05337  77 FGRLDCLVNNAGIAVRPRGdLLDLTEDSFDRLIAINLRGPFFLTQAVarrmveQPDRFDGPHRSIIFVTS----INAYlV 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 6322779  158 PLSVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:cd05337 153 SPNRGEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDM 196
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
11-248 1.79e-05

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 44.76  E-value: 1.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILSAStGNTVITSIRGSPSLPKNKQvEDLAKIRKNIHIVQLDLTKDESIGNIADEI---KKTpffl 87
Cdd:PRK12824   7 VTGAKRGIGSAIARELLND-GYRVIATYFSGNDCAKDWF-EEYGFTEDQVRLKELDVTDTEECAEALAEIeeeEGP---- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    88 gIDIFIACSAVS-DSYYKvlETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAFvplSVSAYGQ 166
Cdd:PRK12824  81 -VDILVNNAGITrDSVFK--RMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQF---GQTNYSA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   167 SKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM-GQYG---LDHFKEkniDISGVNIITPEESASALidvfrKILPED 242
Cdd:PRK12824 155 AKAGMIGFTKALASEGARYGITVNCIAPGYIATPMvEQMGpevLQSIVN---QIPMKRLGTPEEIAAAV-----AFLVSE 226


                 ....*.
gi 6322779   243 NGKFFN 248
Cdd:PRK12824 227 AAGFIT 232
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 10-201 2.03e-05

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 44.68  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    10 FIIGGSRGIGFNLVKILsASTGNTVITSIRGSpslpKNKQVEDLAKIRKN------IHIVQLDLTKDESIGNIAD-EIKK 82
Cdd:PRK12747   8 LVTGASRGIGRAIAKRL-ANDGALVAIHYGNR----KEEAEETVYEIQSNggsafsIGANLESLHGVEALYSSLDnELQN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    83 TPFFLGIDIFIACSAVSDSYYkVLETPKSVWLNHYSTNALGPILALQKVYPLLllKKTRKIFFISSVAGSINafVPLSVs 162
Cdd:PRK12747  83 RTGSTKFDILINNAGIGPGAF-IEETTEQFFDRMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRIS--LPDFI- 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 6322779   163 AYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK12747 157 AYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDM 195
PRK06398 PRK06398
aldose dehydrogenase; Validated
 11-201 2.63e-05

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 44.44  E-value: 2.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLPKNKQVEdlakirknihivqLDLTKDESIGNIADEIKKTpfFLGID 90
Cdd:PRK06398  11 VTGGSQGIGKAVVNRL-KEEGSNVINFDIKEPSYNDVDYFK-------------VDVSNKEQVIKGIDYVISK--YGRID 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    91 IFIACSAVsDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSInafVPLSVSAYGQSKAA 170
Cdd:PRK06398  75 ILVNNAGI-ESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFA---VTRNAAAYVTSKHA 150

                        170       180       190
                 ....*....|....*....|....*....|.
gi 6322779   171 LNYAVKTLSFELKPEgFTVVAFHPGMVSTDM 201
Cdd:PRK06398 151 VLGLTRSIAVDYAPT-IRCVAVCPGSIRTPL 180
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 8-208 2.90e-05

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 44.26  E-value: 2.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     8 TYFIIGGSRGIGFNL-VKILSAstGNTVITSIRGSPSLpknkqvEDLA-KIRKNIHIVQLDLT-KDESIGNIADEIKKtp 84
Cdd:PRK08263   5 VWFITGASRGFGRAWtEAALER--GDRVVATARDTATL------ADLAeKYGDRLLPLALDVTdRAAVFAAVETAVEH-- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    85 fFLGIDIfiacsAVSDSYYKVL----ETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGsINAFvPlS 160
Cdd:PRK08263  75 -FGRLDI-----VVNNAGYGLFgmieEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGG-ISAF-P-M 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 6322779   161 VSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLDH 208
Cdd:PRK08263 146 SGIYHASKWALEGMSEALAQEVAEFGIKVTLVEPGGYSTDWAGTSAKR 193
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 11-201 2.94e-05

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 44.00  E-value: 2.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILsASTGNTVITSIRGSPSlpKNKQVEdlakiRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGID 90
Cdd:PRK06463  12 ITGGTRGIGRAIAEAF-LREGAKVAVLYNSAEN--EAKELR-----EKGVFTIKCDVGNRDQVKKSKEVVEKE--FGRVD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    91 IFIACSAV----------SDSYYKVLetpksvwlnhySTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAFVplS 160
Cdd:PRK06463  82 VLVNNAGImylmpfeefdEEKYNKMI-----------KINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIGTAAE--G 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 6322779   161 VSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK06463 149 TTFYAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDM 189
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 8-241 9.40e-05

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 43.12  E-value: 9.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIGGSRGIGFNLVKILSASTGNTVITSIRGSPSLPKNKQVEDLAKIRKN---IHIVQLDLTKDESIGNIADEIKKTp 84
Cdd:cd08953 207 VYLVTGGAGGIGRALARALARRYGARLVLLGRSPLPPEEEWKAQTLAALEALgarVLYISADVTDAAAVRRLLEKVRER- 285

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   85 fFLGIDIFIACSAVSDSYYKVLETPKSVwlnhysTNALGP----ILALQKVyplllLKKTRKIFFI--SSVAGSI----- 153
Cdd:cd08953 286 -YGAIDGVIHAAGVLRDALLAQKTAEDF------EAVLAPkvdgLLNLAQA-----LADEPLDFFVlfSSVSAFFggagq 353

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779  154 ------NAFvplsVSAYGQSKAALNYAVKTLSFELKPEGFTvvafhpGMVSTDMGQYGLDHfkeknidiSGVNIITPEES 227
Cdd:cd08953 354 adyaaaNAF----LDAFAAYLRQRGPQGRVLSINWPAWREG------GMAADLGARELLAR--------AGLLPIEPEEG 415

                       250
                ....*....|....
gi 6322779  228 ASALIDVFRKILPE 241
Cdd:cd08953 416 LQALEQALSSDLPQ 429
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 48-195 1.01e-04

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 42.64  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    48 KQVEDLAkiRKNIHIVQlDLTKDESIGNIADEIKKTpfFLGIDIFIAcSAVSDSYYKVLE-TPKSVWLNHYSTNALGPIL 126
Cdd:PRK07890  47 AEIDDLG--RRALAVPT-DITDEDQCANLVALALER--FGRVDALVN-NAFRVPSMKPLAdADFAHWRAVIELNVLGTLR 120

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   127 ALQKVYPLLLlKKTRKIFFISSVAgsinAFVP-LSVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPG 195
Cdd:PRK07890 121 LTQAFTPALA-ESGGSIVMINSMV----LRHSqPKYGAYKMAKGALLAASQSLATELGPQGIRVNSVAPG 185
PRK12742 PRK12742
SDR family oxidoreductase;
1-201 1.15e-04

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 42.44  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     1 MNTSSRITYFIIGGSRGIGFNLVKILsASTGNTVITSIRGSPSlpknkQVEDLAKiRKNIHIVQLDLT-KDESIGNIADE 79
Cdd:PRK12742   1 MGAFTGKKVLVLGGSRGIGAAIVRRF-VTDGANVRFTYAGSKD-----AAERLAQ-ETGATAVQTDSAdRDAVIDVVRKS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    80 IKktpfflgIDIFIACSAVSdSYYKVLETPKSVWLNHYSTNALGPILAlqKVYPLLLLKKTRKIFFISSVAGSINAFVPL 159
Cdd:PRK12742  74 GA-------LDILVVNAGIA-VFGDALELDADDIDRLFKINIHAPYHA--SVEAARQMPEGGRIIIIGSVNGDRMPVAGM 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 6322779   160 SvsAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK12742 144 A--AYAASKSALQGMARGLARDFGPRGITINVVQPGPIDTDA 183
PRK07577 PRK07577
SDR family oxidoreductase;
3-201 1.54e-04

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 42.02  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     3 TSSRiTYFIIGGSRGIGFNLVKILSASTGNTVITSIRGSPSLPKNKQVEDLAKIRKNIHIVQlDLTKDESIGNIADEIkk 82
Cdd:PRK07577   1 MSSR-TVLVTGATKGIGLALSLRLANLGHQVIGIARSAIDDFPGELFACDLADIEQTAATLA-QINEIHPVDAIVNNV-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    83 tpfflGIDIFIACSAVS-DSYYKVletpksvwlnhYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAgsinAFVPLSV 161
Cdd:PRK07577  77 -----GIALPQPLGKIDlAALQDV-----------YDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRA----IFGALDR 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 6322779   162 SAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK07577 137 TSYSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETEL 176
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 10-255 1.89e-04

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 41.57  E-value: 1.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   10 FIIGGSRGIGFNLVKILSAStGNTVITsirgspsLPKNkqVEDLAKIRK----NIHIVQLDLTKDESIGNIADEIKKTpf 85
Cdd:cd05348   8 LITGGGSGLGRALVERFVAE-GAKVAV-------LDRS--AEKVAELRAdfgdAVVGVEGDVRSLADNERAVARCVER-- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   86 FLGIDIFIACSAVSDSYYKVLETPK----SVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAFVPLsv 161
Cdd:cd05348  76 FGKLDCFIGNAGIWDYSTSLVDIPEekldEAFDELFHINVKGYILGAKAALPALYATEGSVIFTVSNAGFYPGGGGPL-- 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779  162 saYGQSKAALNYAVKTLSFELKPEgFTVVAFHP-GMVSTDMGQYGLDhFKEKNID-------ISGVNII----TPEESAS 229
Cdd:cd05348 154 --YTASKHAVVGLVKQLAYELAPH-IRVNGVAPgGMVTDLRGPASLG-QGETSIStpplddmLKSILPLgfapEPEDYTG 229

                       250       260       270
                ....*....|....*....|....*....|
gi 6322779  230 ALIDVFRKilpEDN----GKFFNYDGSEGV 255
Cdd:cd05348 230 AYVFLASR---GDNrpatGTVINYDGGMGV 256
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 105-203 2.06e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 41.45  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   105 VLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAFvPlSVSAYGQSKAALNYAVKTLSFELKP 184
Cdd:PRK07478 100 VAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHTAGF-P-GMAAYAASKAGLIGLTQVLAAEYGA 177

                         90
                 ....*....|....*....
gi 6322779   185 EGFTVVAFHPGMVSTDMGQ 203
Cdd:PRK07478 178 QGIRVNALLPGGTDTPMGR 196
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
11-199 2.12e-04

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 41.64  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILSASTGNTVITSiRGSPSLPKNKQVEDLAKirkNIHIVQLDLTKDESIGNIADEIKKTpfFLGID 90
Cdd:PRK06935  20 VTGGNTGLGQGYAVALAKAGADIIITT-HGTNWDETRRLIEKEGR---KVTFVQVDLTKPESAEKVVKEALEE--FGKID 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    91 IFIAcSAVSDSYYKVLETPKSVWLNHYSTNaLGPILAL-QKVYPLLLLKKTRKIFFISSV---AGSInaFVPlsvsAYGQ 166
Cdd:PRK06935  94 ILVN-NAGTIRRAPLLEYKDEDWNAVMDIN-LNSVYHLsQAVAKVMAKQGSGKIINIASMlsfQGGK--FVP----AYTA 165

                        170       180       190
                 ....*....|....*....|....*....|...
gi 6322779   167 SKAALNYAVKTLSFELKPEGFTVVAFHPGMVST 199
Cdd:PRK06935 166 SKHGVAGLTKAFANELAAYNIQVNAIAPGYIKT 198
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 8-201 2.67e-04

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: 41.45  E-value: 2.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIGGSRGIGFNLVKILSASTGNTVITSIRgspslPKNKQVEdLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFL 87
Cdd:cd05363   5 TALITGSARGIGRAFAQAYVREGARVAIADIN-----LEAARAT-AAEIGPAACAISLDVTDQASIDRCVAALVDR--WG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   88 GIDIFIACSAVSDsYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLK-KTRKIFFISSVAGSINAFVplsVSAYGQ 166
Cdd:cd05363  77 SIDILVNNAALFD-LAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMASQAGRRGEAL---VGVYCA 152

                       170       180       190
                ....*....|....*....|....*....|....*
gi 6322779  167 SKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:cd05363 153 TKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGEH 187
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 11-201 2.68e-04

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: 41.02  E-value: 2.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGfNLVKILSASTGNTVITSIRGSPSLPK-NKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFLGI 89
Cdd:cd05340   9 VTGASDGIG-REAALTYARYGATVILLGRNEEKLRQvADHINEEGGRQPQWFILDLLTCTSENCQQLAQRIAVN--YPRL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   90 DIFIACSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSINAfvpLSVSAYGQSKA 169
Cdd:cd05340  86 DGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGR---ANWGAYAVSKF 162

                       170       180       190
                ....*....|....*....|....*....|..
gi 6322779  170 ALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:cd05340 163 ATEGL*QVLADEYQQRNLRVNCINPGGTRTAM 194
PRK07035 PRK07035
SDR family oxidoreductase;
10-199 3.16e-04

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 41.15  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    10 FIIGGSRGIGFNLVKILsASTGNTVITSIRgspSLPKNKQVEDlaKIRKN--------IHIVQLdltkdESIGNIADEIK 81
Cdd:PRK07035  12 LVTGASRGIGEAIAKLL-AQQGAHVIVSSR---KLDGCQAVAD--AIVAAggkaealaCHIGEM-----EQIDALFAHIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    82 KTpfFLGIDIFIACSAVSDSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLllkKTRKIFFISSVAgSINAFVPLSV 161
Cdd:PRK07035  81 ER--HGRLDILVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLM---KEQGGGSIVNVA-SVNGVSPGDF 154

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 6322779   162 SA-YGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVST 199
Cdd:PRK07035 155 QGiYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDT 193
PRK07023 PRK07023
SDR family oxidoreductase;
114-233 3.59e-04

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 40.77  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   114 LNHYSTNALGPILALQKVYPLLL----LKKT-----RKIFFISSVAGSiNAFVPLSVsaYGQSKAALNYAVKTLSFElKP 184
Cdd:PRK07023  94 LATLDAAAIARAVGLNVAAPLMLtaalAQAAsdaaeRRILHISSGAAR-NAYAGWSV--YCATKAALDHHARAVALD-AN 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6322779   185 EGFTVVAFHPGMVSTDMG----QYGLDHF--KEKNIDI--SGvNIITPEESASALID 233
Cdd:PRK07023 170 RALRIVSLAPGVVDTGMQatirATDEERFpmRERFRELkaSG-ALSTPEDAARRLIA 225
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 8-201 4.34e-04

human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human HSDL2 and related protens. 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. 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: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 40.51  E-value: 4.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIGGSRGIGFNLVKILSASTGNTVIT--SIRGSPSLPKN-----KQVEDLAKirKNIHIVqLDLtKDESigNIADEI 80
Cdd:cd09762   5 TLFITGASRGIGKAIALKAARDGANVVIAakTAEPHPKLPGTiytaaEEIEAAGG--KALPCI-VDI-RDED--QVRAAV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   81 KKT-PFFLGIDIFI-ACSAVSDSyyKVLETP-KSVWLNHySTNALGPILALQKVYPLLLLKKTRKIFFISSvagsinafv 157
Cdd:cd09762  79 EKAvEKFGGIDILVnNASAISLT--GTLDTPmKRYDLMM-GVNTRGTYLCSKACLPYLKKSKNPHILNLSP--------- 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 6322779  158 PLSV--------SAYGQSKAALNYAVKTLSFELKPEGFTVVAFHP-GMVSTDM 201
Cdd:cd09762 147 PLNLnpkwfknhTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWPrTAIATAA 199
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 11-214 4.73e-04

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: 40.34  E-value: 4.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   11 IIGGSRGIGFNLVKILsASTGNTVITSIRGSpSLPKNKQVEDLAKIRKNIHIVQLDLTkdeSIGNIADEIKKTPFFLG-I 89
Cdd:cd05357   5 VTGAAKRIGRAIAEAL-AAEGYRVVVHYNRS-EAEAQRLKDELNALRNSAVLVQADLS---DFAACADLVAAAFRAFGrC 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   90 DIFIacSAVSdSYY--KVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSvagsINAFVPLS-VSAYGQ 166
Cdd:cd05357  80 DVLV--NNAS-AFYptPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIID----AMTDRPLTgYFAYCM 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 6322779  167 SKAALNYAVKTLSFELKPEgFTVVAFHPGMV--STDMGQYGLDHFKEKNI 214
Cdd:cd05357 153 SKAALEGLTRSAALELAPN-IRVNGIAPGLIllPEDMDAEYRENALRKVP 201
PRK07454 PRK07454
SDR family oxidoreductase;
1-199 6.13e-04

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 39.94  E-value: 6.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     1 MNTSSRITYFIIGGSRGIGfNLVKILSASTGNTVITSIRgspSLPKNKQV-EDLAKIRKNIHIVQLDLTKDESIGN-IAD 78
Cdd:PRK07454   1 MSLNSMPRALITGASSGIG-KATALAFAKAGWDLALVAR---SQDALEALaAELRSTGVKAAAYSIDLSNPEAIAPgIAE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    79 EIKKtpfFLGIDIFI--ACSAVSDSyykVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSiNAF 156
Cdd:PRK07454  77 LLEQ---FGCPDVLInnAGMAYTGP---LLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAAR-NAF 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 6322779   157 vPlSVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVST 199
Cdd:PRK07454 150 -P-QWGAYCVSKAALAAFTKCLAEEERSHGIRVCTITLGAVNT 190
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 8-199 1.26e-03

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: 39.36  E-value: 1.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLPKNKqvedLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpfFL 87
Cdd:cd05349   2 VVLVTGASRGLGAAIARSF-AREGARVVVNYYRSTESAEAV----AAEAGERAIAIQADVRDRDQVQAMIEEAKNH--FG 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   88 GIDIfIACSAVSDSYYKVLETPKS---VW---LNHYSTNALGPILALQKVYPLLLLKKTRKIFFISSvagsiNAF----V 157
Cdd:cd05349  75 PVDT-IVNNALIDFPFDPDQRKTFdtiDWedyQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGT-----NLFqnpvV 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 6322779  158 PLSvsAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVST 199
Cdd:cd05349 149 PYH--DYTTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKV 188
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
142-208 1.27e-03

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 39.32  E-value: 1.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322779   142 KIFFISSVAGSI-NAfvplSVSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMgQYGLDH 208
Cdd:PRK08643 133 KIINATSQAGVVgNP----ELAVYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKTPM-MFDIAH 195
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 8-201 1.43e-03

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 39.12  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIGGSRGIGFNLVKILsASTGNTVITSIRGSPSlpKNKQVEDLAK--IRKNIHIVQLDLTKDESIGNIADEIKKTPf 85
Cdd:cd09809   3 VIIITGANSGIGFETARSF-ALHGAHVILACRNMSR--ASAAVSRILEewHKARVEAMTLDLASLRSVQRFAEAFKAKN- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   86 fLGIDIFIACSAVSDSYYKV----LETPksvwlnhYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAgsiNAFVPLSV 161
Cdd:cd09809  79 -SPLHVLVCNAAVFALPWTLtedgLETT-------FQVNHLGHFYLVQLLEDVLRRSAPARVIVVSSES---HRFTDLPD 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322779  162 S--------------------AYGQSKAALNYAVKTLSFELKPEGFTVVAFHPG-MVSTDM 201
Cdd:cd09809 148 ScgnldfsllsppkkkywsmlAYNRAKLCNILFSNELHRRLSPRGITSNSLHPGnMMYSSI 208
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 11-199 1.88e-03

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 38.52  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSR--GIGFNLVKILsASTGNTV-----ITSIRGSPSLPKNKQVEDLAKIRKN----IHIVQLDLTKDESIGNIADE 79
Cdd:PRK12748  10 VTGASRlnGIGAAVCRRL-AAKGIDIfftywSPYDKTMPWGMHDKEPVLLKEEIESygvrCEHMEIDLSQPYAPNRVFYA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    80 IKKTPFFLGIDIFIACSAVSDSYYKVleTPKSVWLnHYSTNALGPIL---ALQKVYPLLllKKTRKIFFISsvaGSINAF 156
Cdd:PRK12748  89 VSERLGDPSILINNAAYSTHTRLEEL--TAEQLDK-HYAVNVRATMLlssAFAKQYDGK--AGGRIINLTS---GQSLGP 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 6322779   157 VPLSVsAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVST 199
Cdd:PRK12748 161 MPDEL-AYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDT 202
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 124-194 1.97e-03

haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. Haloalcohol dehalogenase show low sequence similarity to short-chain dehydrogenases/reductases (SDRs). Like the SDRs, haloalcohol dehalogenases have a conserved catalytic triad (Ser-Tyr-Lys/Arg), and form a Rossmann fold. However, the normal classical SDR NAD(P)-binding motif (TGXXGXG) and NAD-binding function is replaced with a halide binding site, allowing the enzyme to catalyze a dehalogenation reaction. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in 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: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 38.71  E-value: 1.97e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322779  124 PILALQKVYPLLLLKKTRKIFFISSVAGsinaFVPLS-VSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHP 194
Cdd:cd05361 108 PFALLQAAIAQMKKAGGGSIIFITSAVP----KKPLAyNSLYGPARAAAVALAESLAKELSRDNILVYAIGP 175
PRK07201 PRK07201
SDR family oxidoreductase;
11-233 2.27e-03

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 39.16  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILsASTGNTVITSIRGspslpknkqVEDLAKIRKNI-------HIVQLDLTKDESIGNIADEIKKT 83
Cdd:PRK07201 376 ITGASSGIGRATAIKV-AEAGATVFLVARN---------GEALDELVAEIrakggtaHAYTCDLTDSAAVDHTVKDILAE 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    84 pfFLGIDIFIACS------AVSDSYYKVLETPKSVWLNHYStnALGPILALqkvYPLLLLKKTRKIFFISSVAGSINA-- 155
Cdd:PRK07201 446 --HGHVDYLVNNAgrsirrSVENSTDRFHDYERTMAVNYFG--AVRLILGL---LPHMRERRFGHVVNVSSIGVQTNApr 518

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   156 FvplsvSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM----GQYGldhfkeknidisGVNIITPEESASAL 231
Cdd:PRK07201 519 F-----SAYVASKAALDAFSDVAASETLSDGITFTTIHMPLVRTPMiaptKRYN------------NVPTISPEEAADMV 581


                 ..
gi 6322779   232 ID 233
Cdd:PRK07201 582 VR 583
PRK12746 PRK12746
SDR family oxidoreductase;
10-213 2.97e-03

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 38.09  E-value: 2.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    10 FIIGGSRGIGFNLVKILSASTGNTVITSIRgspslpkNKQVED--LAKIRKN---IHIVQLDLTKDESIGNIADEIK-KT 83
Cdd:PRK12746  10 LVTGASRGIGRAIAMRLANDGALVAIHYGR-------NKQAADetIREIESNggkAFLIEADLNSIDGVKKLVEQLKnEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    84 PFFLG---IDIFIACSAVSdSYYKVLETPKSVWLNHYSTNALGPILALQKVYPLLllKKTRKIFFISSV------AGSIn 154
Cdd:PRK12746  83 QIRVGtseIDILVNNAGIG-TQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL--RAEGRVINISSAevrlgfTGSI- 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6322779   155 afvplsvsAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVSTDMGQYGLDHFKEKN 213
Cdd:PRK12746 159 --------AYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLLDDPEIRN 209
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 11-201 3.19e-03

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 38.01  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    11 IIGGSRGIGFNLVKILsASTGNTVITSIRGSPSLpkNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKtpFFLGID 90
Cdd:PRK05876  11 ITGGASGIGLATGTEF-ARRGARVVLGDVDKPGL--RQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFR--LLGHVD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    91 IFIACSAVSDSYyKVLETPKSVWLNHYSTNALGPILALQKVYPLLLLKKTR-KIFFISSVAGsinaFVP-LSVSAYGQSK 168
Cdd:PRK05876  86 VVFSNAGIVVGG-PIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTGgHVVFTASFAG----LVPnAGLGAYGVAK 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 6322779   169 AALNYAVKTLSFELKPEGFTVVAFHPGMVSTDM 201
Cdd:PRK05876 161 YGVVGLAETLAREVTADGIGVSVLCPMVVETNL 193
PRK07832 PRK07832
SDR family oxidoreductase;
113-238 3.59e-03

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 38.10  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   113 WLNHYSTNALGPILALQK-VYPLLLLKKTRKIFFISSVAGSINafVPLSvSAYGQSKAALNYAVKTLSFELKPEGFTVVA 191
Cdd:PRK07832 102 WRRMVDVNLMGPIHVIETfVPPMVAAGRGGHLVNVSSAAGLVA--LPWH-AAYSASKFGLRGLSEVLRFDLARHGIGVSV 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 6322779   192 FHPGMVSTDMgqygldhfkEKNIDISGVNiiTPEESASALIDVFRKI 238
Cdd:PRK07832 179 VVPGAVKTPL---------VNTVEIAGVD--REDPRVQKWVDRFRGH 214
PRK07102 PRK07102
SDR family oxidoreductase;
119-238 4.54e-03

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 37.60  E-value: 4.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   119 TNALGPILALQKVYPLLLLKKTRKIFFISSVAG----SINAFvplsvsaYGQSKAALNYAVKTLSFELKPEGFTVVAFHP 194
Cdd:PRK07102 106 TNFEGPIALLTLLANRFEARGSGTIVGISSVAGdrgrASNYV-------YGSAKAALTAFLSGLRNRLFKSGVHVLTVKP 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 6322779   195 GMVSTDMGQygldhfkekNIDISGVNIITPEESASaliDVFRKI 238
Cdd:PRK07102 179 GFVRTPMTA---------GLKLPGPLTAQPEEVAK---DIFRAI 210
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 8-199 5.46e-03

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: 37.44  E-value: 5.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIGGSRGIGFNLVKILSASTGNT--VITSIRgspSLPKNKQVEDLAKIR--KNIHIVQLDLTKDESIGNIADEIKKT 83
Cdd:cd09806   2 VVLITGCSSGIGLHLAVRLASDPSKRfkVYATMR---DLKKKGRLWEAAGALagGTLETLQLDVCDSKSVAAAVERVTER 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   84 PfflgIDIFIACSAVS----------DSYYKVLEtpksvwlnhysTNALGPILALQKVYPLLLLKKTRKIFFISSVAGSI 153
Cdd:cd09806  79 H----VDVLVCNAGVGllgplealseDAMASVFD-----------VNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQ 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 6322779  154 NafVPLSvSAYGQSKAALNYAVKTLSFELKPEGFTVVAFHPGMVST 199
Cdd:cd09806 144 G--LPFN-DVYCASKFALEGLCESLAVQLLPFNVHLSLIECGPVHT 186
PRK09186 PRK09186
flagellin modification protein A; Provisional
 8-195 6.07e-03

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 37.28  E-value: 6.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     8 TYFIIGGSRGIGFNLVKILSASTGNTVITSIRGSPSLPKNKQVEDLAKIRKNIhIVQLDLTKDESIGNIADEIkkTPFFL 87
Cdd:PRK09186   6 TILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSKKLS-LVELDITDQESLEEFLSKS--AEKYG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    88 GIDIFIACS-AVSDSYYKVLE--TPKSVWLNhYSTNALGPILALQKVYPLLLLKKTRKIFFISSVAGsINA--------- 155
Cdd:PRK09186  83 KIDGAVNCAyPRNKDYGKKFFdvSLDDFNEN-LSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYG-VVApkfeiyegt 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 6322779   156 --FVPLSVSAYgqsKAALNYAVKTLSFELKPEGFTVVAFHPG 195
Cdd:PRK09186 161 smTSPVEYAAI---KAGIIHLTKYLAKYFKDSNIRVNCVSPG 199
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 8-186 7.32e-03

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


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 36.79  E-value: 7.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779    8 TYFIIG--GSRGIGFNLVKILSASTGNTVITsirGSPSLPKNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEIKKTpf 85
Cdd:cd05372   3 RILITGiaNDRSIAWGIAKALHEAGAELAFT---YQPEALRKRVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKD-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779   86 FLGIDIFIACSAVSDSYYKV---LETPKSVWLNHYSTNAlgpilalqkvYPLLLLkkTRKIFFISSVAGSInafVPLS-- 160
Cdd:cd05372  78 WGKLDGLVHSIAFAPKVQLKgpfLDTSRKGFLKALDISA----------YSLVSL--AKAALPIMNPGGSI---VTLSyl 142

                       170       180       190
                ....*....|....*....|....*....|....
gi 6322779  161 -----VSAY---GQSKAALNYAVKTLSFELKPEG 186
Cdd:cd05372 143 gservVPGYnvmGVAKAALESSVRYLAYELGRKG 176
PRK07806 PRK07806
SDR family oxidoreductase;
1-93 8.01e-03

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 36.62  E-value: 8.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322779     1 MNTSSRITYFIIGGSRGIGFNLVKILSASTGNTVITSIRGSPSlpKNKQVEDLAKIRKNIHIVQLDLTKDESIGNIADEI 80
Cdd:PRK07806   1 MGDLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPR--ANKVVAEIEAAGGRASAVGADLTDEESVAALMDTA 78

                         90
                 ....*....|...
gi 6322779    81 KKTpfFLGIDIFI 93
Cdd:PRK07806  79 REE--FGGLDALV 89
 
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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