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Conserved domains on  [gi|83775806|dbj|BAE65925|]
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unnamed protein product [Aspergillus oryzae RIB40]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143139)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase similar to alcohol dehydrogenase that catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones; 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 4-248 5.76e-88

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: 261.85  E-value: 5.76e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAA----ASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:cd05323   2 VAIITGGASGIGLATAKLLLKKG-AKVAILDRNENPGAAAElqaiNPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRVDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGIAEDTAMFFAshptgIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRSpeKTKGNRHLIIMSSIGGLYPCAHTPV 159
Cdd:cd05323  81 LINNAGILDEKSYLFA-----GKLPPPWEKTIDVNLTGVINTTYLALHYMDKN--KGGKGGVIVNIGSVAGLYPAPQFPV 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806 160 YSATKHGLVGFTRSVGKRL-LDEGVKVNTVCPGVVLTPLMTTELQA---FFPEKIVMKMSDVTNVVLKLIsgtEVTDSNG 235
Cdd:cd05323 154 YSASKHGVVGFTRSLADLLeYKTGVRVNAICPGFTNTPLLPDLVAKeaeMLPSAPTQSPEVVAKAIVYLI---EDDEKNG 230

                       250
                ....*....|...
gi 83775806 236 TSVPSDQLHSRAI 248
Cdd:cd05323 231 AIWIVDGGKLIEI 243
 
Name Accession Description Interval E-value
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 4-248 5.76e-88

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: 261.85  E-value: 5.76e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAA----ASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:cd05323   2 VAIITGGASGIGLATAKLLLKKG-AKVAILDRNENPGAAAElqaiNPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRVDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGIAEDTAMFFAshptgIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRSpeKTKGNRHLIIMSSIGGLYPCAHTPV 159
Cdd:cd05323  81 LINNAGILDEKSYLFA-----GKLPPPWEKTIDVNLTGVINTTYLALHYMDKN--KGGKGGVIVNIGSVAGLYPAPQFPV 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806 160 YSATKHGLVGFTRSVGKRL-LDEGVKVNTVCPGVVLTPLMTTELQA---FFPEKIVMKMSDVTNVVLKLIsgtEVTDSNG 235
Cdd:cd05323 154 YSASKHGVVGFTRSLADLLeYKTGVRVNAICPGFTNTPLLPDLVAKeaeMLPSAPTQSPEVVAKAIVYLI---EDDEKNG 230

                       250
                ....*....|...
gi 83775806 236 TSVPSDQLHSRAI 248
Cdd:cd05323 231 AIWIVDGGKLIEI 243
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
4-225 7.81e-44

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 149.25  E-value: 7.81e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLRNT----IFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:COG0300   7 TVLITGASSGIGRALARALAARG-ARVVLVARDAERLEALAAELRAAgarvEVVALDVTDPDAVAALAEAVLARFGPIDV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGIAEDTAmfFASHPtgippPPDMTGLTDINFTGAIYTSYLAMHYFRRSpektkGNRHLIIMSSIGGLYPCAHTPV 159
Cdd:COG0300  86 LVNNAGVGGGGP--FEELD-----LEDLRRVFEVNVFGPVRLTRALLPLMRAR-----GRGRIVNVSSVAGLRGLPGMAA 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83775806 160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLmtTELQAFFPEKIVMKMSDVTNVVLKLI 225
Cdd:COG0300 154 YAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPF--TARAGAPAGRPLLSPEEVARAILRAL 217
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 4-202 6.43e-43

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 145.06  E-value: 6.43e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806     4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLRNT----IFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEG-AKVVLVDRSEEKLEAVAKELGALggkaLFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    80 VLANAGIAEDtamffasHPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFrrsPEKTKGNrhLIIMSSIGGLYPCAHTPV 159
Cdd:pfam00106  81 LVNNAGITGL-------GPFSELSDEDWERVIDVNLTGVFNLTRAVLPAM---IKGSGGR--IVNISSVAGLVPYPGGSA 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 83775806   160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTEL 202
Cdd:pfam00106 149 YSASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTD-MTKEL 190
PRK12826 PRK12826
SDR family oxidoreductase;
4-226 9.91e-33

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 120.41  E-value: 9.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRN---TIF-HQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK12826   8 VALVTGAARGIGRAIAVRLAADGA-EVIVVDICGDDAAATAELVEAaggKARaRQVDVRDRAALKAAVAAGVEDFGRLDI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAEDTAMFFAShptgippPPDMTGLTDINFTGAIYTSYLAMHYFRRSpektKGNRhLIIMSSIGGL---YP-CA 155
Cdd:PRK12826  87 LVANAGIFPLTPFAEMD-------DEQWERVIDVNLTGTFLLTQAALPALIRA----GGGR-IVLTSSVAGPrvgYPgLA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83775806  156 HtpvYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAFFPEKIVMKMS--------DVTNVVLKLIS 226
Cdd:PRK12826 155 H---YAASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNLGDAQWAEAIAAAIPlgrlgepeDIAAAVLFLAS 230
PHB_DH TIGR01963
3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain ...
 4-197 1.06e-26

3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain dehydrogenases. Characterized members so far as 3-hydroxybutyrate dehydrogenases and are found in species that accumulate ester polmers called polyhydroxyalkanoic acids (PHAs) under certain conditions. Several members of the family are from species not known to accumulate PHAs, including Oceanobacillus iheyensis and Bacillus subtilis. However, polymer formation is not required for there be a role for 3-hydroxybutyrate dehydrogenase; it may be members of this family have the same function in those species.


Pssm-ID: 211705 [Multi-domain]  Cd Length: 255  Bit Score: 104.37  E-value: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806     4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:TIGR01963   3 TALVTGAASGIGLAIARALAAAGA-NVVVNDFGEEGAEAAAKVAGdaggSVIYLPADVTKEDEIADMIAAAAAEFGGLDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    80 VLANAGIaedtamffaSHPTGIP--PPPDMTGLTDINFTGAIYTSYLAMhyfrrSPEKTKGNRHLIIMSSIGGLYPCAHT 157
Cdd:TIGR01963  82 LVNNAGI---------QHVAPIEefPPEDWDRIIAVMLTSAFHTIRAAL-----PHMKKQGWGRIINIASAHGLVASPFK 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 83775806   158 PVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:TIGR01963 148 SAYVAAKHGLIGLTKVLALEVAEHGITVNAICPGYVRTPL 187
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 6-92 2.32e-04

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 40.93  E-value: 2.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806      6 LITGGTSGMGLDVAQELDKTGLWKVHIIGSNANRGEEAAASLR-------NTIFHQVDVTKYEQQGAAFDKIFNEEKRLD 78
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARRLVLLSRSGPDAPGAAALLAeleaagaRVTVVACDVADRDALAAVLAAIPAVEGPLT 83

                           90
                   ....*....|....
gi 83775806     79 FVLANAGIAEDTAM 92
Cdd:smart00822  84 GVIHAAGVLDDGVL 97
 
Name Accession Description Interval E-value
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 4-248 5.76e-88

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: 261.85  E-value: 5.76e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAA----ASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:cd05323   2 VAIITGGASGIGLATAKLLLKKG-AKVAILDRNENPGAAAElqaiNPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRVDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGIAEDTAMFFAshptgIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRSpeKTKGNRHLIIMSSIGGLYPCAHTPV 159
Cdd:cd05323  81 LINNAGILDEKSYLFA-----GKLPPPWEKTIDVNLTGVINTTYLALHYMDKN--KGGKGGVIVNIGSVAGLYPAPQFPV 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806 160 YSATKHGLVGFTRSVGKRL-LDEGVKVNTVCPGVVLTPLMTTELQA---FFPEKIVMKMSDVTNVVLKLIsgtEVTDSNG 235
Cdd:cd05323 154 YSASKHGVVGFTRSLADLLeYKTGVRVNAICPGFTNTPLLPDLVAKeaeMLPSAPTQSPEVVAKAIVYLI---EDDEKNG 230

                       250
                ....*....|...
gi 83775806 236 TSVPSDQLHSRAI 248
Cdd:cd05323 231 AIWIVDGGKLIEI 243
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 5-241 1.21e-46

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: 155.90  E-value: 1.21e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   5 ALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAA---ASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVL 81
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREG-AKVVLADRNEEALAELAaieALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  82 ANAGIAEDTAMFFAShptgippPPDMTGLTDINFTGAIYTSYLAMHYFRRSpektkGNRHLIIMSSIGGLYPCAHTPVYS 161
Cdd:cd05233  80 NNAGIARPGPLEELT-------DEDWDRVLDVNLTGVFLLTRAALPHMKKQ-----GGGRIVNISSVAGLRPLPGQAAYA 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806 162 ATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTT--------ELQAFFPEKIVMKMSDVTNVVLKLISGtEVTDS 233
Cdd:cd05233 148 ASKAALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKlgpeeaekELAAAIPLGRLGTPEEVAEAVVFLASD-EASYI 226


                ....*...
gi 83775806 234 NGTSVPSD 241
Cdd:cd05233 227 TGQVIPVD 234
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
4-225 7.81e-44

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 149.25  E-value: 7.81e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLRNT----IFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:COG0300   7 TVLITGASSGIGRALARALAARG-ARVVLVARDAERLEALAAELRAAgarvEVVALDVTDPDAVAALAEAVLARFGPIDV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGIAEDTAmfFASHPtgippPPDMTGLTDINFTGAIYTSYLAMHYFRRSpektkGNRHLIIMSSIGGLYPCAHTPV 159
Cdd:COG0300  86 LVNNAGVGGGGP--FEELD-----LEDLRRVFEVNVFGPVRLTRALLPLMRAR-----GRGRIVNVSSVAGLRGLPGMAA 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83775806 160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLmtTELQAFFPEKIVMKMSDVTNVVLKLI 225
Cdd:COG0300 154 YAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPF--TARAGAPAGRPLLSPEEVARAILRAL 217
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 4-202 6.43e-43

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 145.06  E-value: 6.43e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806     4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLRNT----IFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEG-AKVVLVDRSEEKLEAVAKELGALggkaLFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    80 VLANAGIAEDtamffasHPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFrrsPEKTKGNrhLIIMSSIGGLYPCAHTPV 159
Cdd:pfam00106  81 LVNNAGITGL-------GPFSELSDEDWERVIDVNLTGVFNLTRAVLPAM---IKGSGGR--IVNISSVAGLVPYPGGSA 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 83775806   160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTEL 202
Cdd:pfam00106 149 YSASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTD-MTKEL 190
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 4-226 1.94e-42

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: 145.70  E-value: 1.94e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:COG1028   8 VALVTGGSSGIGRAIARALAAEG-ARVVITDRDAEALEAAAAELRaaggRALAVAADVTDEAAVEALVAAAVAAFGRLDI 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGIAEDTamffashptgipPPPDMT-----GLTDINFTGAIYTSYLAMHYFRRSpektkGNRHLIIMSSIGGLYPC 154
Cdd:COG1028  87 LVNNAGITPPG------------PLEELTeedwdRVLDVNLKGPFLLTRAALPHMRER-----GGGRIVNISSIAGLRGS 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806 155 AHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTT-----ELQAFFPEKIVMK----MSDVTNVVLKLI 225
Cdd:COG1028 150 PGQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRAllgaeEVREALAARIPLGrlgtPEEVAAAVLFLA 229


                .
gi 83775806 226 S 226
Cdd:COG1028 230 S 230
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 4-226 8.60e-40

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: 138.39  E-value: 8.60e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASL-RNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLA 82
Cdd:COG4221   7 VALITGASSGIGAATARALAAAG-ARVVLAARRAERLEALAAELgGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDVLVN 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  83 NAGIA-----EDTamffashptgipPPPDMTGLTDINFTGAIYTSYLAMHYFRRSPektKGnrHLIIMSSIGGLYPCAHT 157
Cdd:COG4221  86 NAGVAllgplEEL------------DPEDWDRMIDVNVKGVLYVTRAALPAMRARG---SG--HIVNISSIAGLRPYPGG 148

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83775806 158 PVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTT----ELQAFFPEKIVMKM---SDVTNVVLKLIS 226
Cdd:COG4221 149 AVYAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSvfdgDAEAAAAVYEGLEPltpEDVAEAVLFALT 224
PRK12826 PRK12826
SDR family oxidoreductase;
4-226 9.91e-33

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 120.41  E-value: 9.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRN---TIF-HQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK12826   8 VALVTGAARGIGRAIAVRLAADGA-EVIVVDICGDDAAATAELVEAaggKARaRQVDVRDRAALKAAVAAGVEDFGRLDI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAEDTAMFFAShptgippPPDMTGLTDINFTGAIYTSYLAMHYFRRSpektKGNRhLIIMSSIGGL---YP-CA 155
Cdd:PRK12826  87 LVANAGIFPLTPFAEMD-------DEQWERVIDVNLTGTFLLTQAALPALIRA----GGGR-IVLTSSVAGPrvgYPgLA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83775806  156 HtpvYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAFFPEKIVMKMS--------DVTNVVLKLIS 226
Cdd:PRK12826 155 H---YAASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNLGDAQWAEAIAAAIPlgrlgepeDIAAAVLFLAS 230
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
4-226 2.31e-32

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 119.11  E-value: 2.31e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK05653   7 TALVTGASRGIGRAIALRLAADGA-KVVIYDSNEEAAEALAAELRaaggEARVLVFDVSDEAAVRALIEAAVEAFGALDI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAEDTAMffashptgipppPDMT-----GLTDINFTGAIYTSYLAMHYFRRSpektKGNRhLIIMSSIGGLYPC 154
Cdd:PRK05653  86 LVNNAGITRDALL------------PRMSeedwdRVIDVNLTGTFNVVRAALPPMIKA----RYGR-IVNISSVSGVTGN 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  155 AHTPVYSATKHGLVGFTRS----VGKRlldeGVKVNTVCPGVVLTPlMTTELQAFFPEKIV--------MKMSDVTNVVL 222
Cdd:PRK05653 149 PGQTNYSAAKAGVIGFTKAlaleLASR----GITVNAVAPGFIDTD-MTEGLPEEVKAEILkeiplgrlGQPEEVANAVA 223


                 ....
gi 83775806  223 KLIS 226
Cdd:PRK05653 224 FLAS 227
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-226 4.38e-31

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 115.71  E-value: 4.38e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlWKVHIigsNANRGEEAAASLRNTI--------FHQVDVTKYEQQGAAFDKIFNEEK 75
Cdd:PRK05565   7 VAIVTGASGGIGRAIAELLAKEG-AKVVI---AYDINEEAAQELLEEIkeeggdaiAVKADVSSEEDVENLVEQIVEKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   76 RLDFVLANAGIaedtaMFFAshptgipPPPDMTG-----LTDINFTGAIYTSYLAMHYFRRspektKGNRHLIIMSSIGG 150
Cdd:PRK05565  83 KIDILVNNAGI-----SNFG-------LVTDMTDeewdrVIDVNLTGVMLLTRYALPYMIK-----RKSGVIVNISSIWG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  151 LYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTT----ELQAFFPEKIVMKM---SDVTNVVLK 223
Cdd:PRK05565 146 LIGASCEVLYSASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSfseeDKEGLAEEIPLGRLgkpEEIAKVVLF 225


                 ...
gi 83775806  224 LIS 226
Cdd:PRK05565 226 LAS 228
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 4-231 1.10e-29

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: 111.69  E-value: 1.10e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLAN 83
Cdd:cd08932   2 VALVTGASRGIGIEIARALARDG-YRVSLGLRNPEDLAALSASGGDVEAVPYDARDPEDARALVDALRDRFGRIDVLVHN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  84 AGIAEDTAMFFAShptgippPPDMTGLTDINFTGAIYTSYLAMHYFRRSpektkGNRHLIIMSSIGGLYPCAHTPVYSAT 163
Cdd:cd08932  81 AGIGRPTTLREGS-------DAELEAHFSINVIAPAELTRALLPALREA-----GSGRVVFLNSLSGKRVLAGNAGYSAS 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83775806 164 KHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTE-LQAFFPEKIVMKMSDVTNVVLKLISGTEVT 231
Cdd:cd08932 149 KFALRALAHALRQEGWDHGVRVSAVCPGFVDTPMAQGLtLVGAFPPEEMIQPKDIANLVRMVIELPENI 217
PRK07326 PRK07326
SDR family oxidoreductase;
4-226 1.60e-29

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 111.64  E-value: 1.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTifHQV-----DVTKYEQQGAAFDKIFNEEKRLD 78
Cdd:PRK07326   8 VALITGGSKGIGFAIAEALLAEGY-KVAITARDQKELEEAAAELNNK--GNVlglaaDVRDEADVQRAVDAIVAAFGGLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   79 FVLANAGIAEdtamfFAshPTGIPPPPDMTGLTDINFTGAIYTSYLAMhyfrrsPEKTKGNRHLIIMSSIGGLYPCAHTP 158
Cdd:PRK07326  85 VLIANAGVGH-----FA--PVEELTPEEWRLVIDTNLTGAFYTIKAAV------PALKRGGGYIINISSLAGTNFFAGGA 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83775806  159 VYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAFFPEKIvmKMSDVTNVVLKLIS 226
Cdd:PRK07326 152 AYNASKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATHFNGHTPSEKDAWKI--QPEDIAQLVLDLLK 217
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 4-195 5.46e-29

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


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 109.63  E-value: 5.46e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLWKVHIIGSNANRGEEAAASLRNT----IFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:cd05324   2 VALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEglsvRFHQLDVTDDASIEAAADFVEEKYGGLDI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGIAedtamfFASHPTGIPPPPDMTGLTDINFTGAIYTsylaMHYF----RRSPektkGNRHLIIMSSIGGLypca 155
Cdd:cd05324  82 LVNNAGIA------FKGFDDSTPTREQARETMKTNFFGTVDV----TQALlpllKKSP----AGRIVNVSSGLGSL---- 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 83775806 156 hTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT 195
Cdd:cd05324 144 -TSAYGVSKAALNALTRILAKELKETGIKVNACCPGWVKT 182
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 4-197 3.59e-28

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 108.44  E-value: 3.59e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNT----IFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK12429   6 VALVTGAASGIGLEIALALAKEGA-KVVIADLNDEAAAAAAEALQKAggkaIGVAMDVTDEEAINAGIDYAVETFGGVDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIaedtamffaSHPTGIP--PPPDMTGLTDINFTGAIYTSYLAMHYFRRSpektKGNRhLIIMSSIGGLYPCAHT 157
Cdd:PRK12429  85 LVNNAGI---------QHVAPIEdfPTEKWKKMIAIMLDGAFLTTKAALPIMKAQ----GGGR-IINMASVHGLVGSAGK 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 83775806  158 PVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:PRK12429 151 AAYVSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDTPL 190
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 3-209 4.56e-28

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 108.22  E-value: 4.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    3 LVALITGGTSGMGLDVAQELDKTGLwKVHIIGsnanRGEEAAASLR------NTIFHQVDVTKYEQQGAAFDKIFNEEKR 76
Cdd:PRK12829  12 LRVLVTGGASGIGRAIAEAFAEAGA-RVHVCD----VSEAALAATAarlpgaKVTATVADVADPAQVERVFDTAVERFGG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   77 LDFVLANAGIAEDTAmffashptGIP--PPPDMTGLTDINFTGAIYTSYLAMHYFRRSPEktkgNRHLIIMSSIGGL--Y 152
Cdd:PRK12829  87 LDVLVNNAGIAGPTG--------GIDeiTPEQWEQTLAVNLNGQFYFARAAVPLLKASGH----GGVIIALSSVAGRlgY 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 83775806  153 PcAHTPvYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAFFPEK 209
Cdd:PRK12829 155 P-GRTP-YAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEARAQQL 209
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 4-226 3.28e-27

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: 105.32  E-value: 3.28e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:cd05333   2 VALVTGASRGIGRAIALRLAAEGA-KVAVTDRSEEAAAETVEEIKalggNAAALEADVSDREAVEALVEKVEAEFGPVDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGIAEDTAMFFAShptgippPPDMTGLTDINFTGAIYTSYLAMHYFRRspektKGNRHLIIMSSIGGLYPCAHTPV 159
Cdd:cd05333  81 LVNNAGITRDNLLMRMS-------EEDWDAVINVNLTGVFNVTQAVIRAMIK-----RRSGRIINISSVVGLIGNPGQAN 148

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83775806 160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTELqaffPEKIVMKM------------SDVTNVVLKLIS 226
Cdd:cd05333 149 YAASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTD-MTDAL----PEKVKEKIlkqiplgrlgtpEEVANAVAFLAS 222
PHB_DH TIGR01963
3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain ...
 4-197 1.06e-26

3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain dehydrogenases. Characterized members so far as 3-hydroxybutyrate dehydrogenases and are found in species that accumulate ester polmers called polyhydroxyalkanoic acids (PHAs) under certain conditions. Several members of the family are from species not known to accumulate PHAs, including Oceanobacillus iheyensis and Bacillus subtilis. However, polymer formation is not required for there be a role for 3-hydroxybutyrate dehydrogenase; it may be members of this family have the same function in those species.


Pssm-ID: 211705 [Multi-domain]  Cd Length: 255  Bit Score: 104.37  E-value: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806     4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:TIGR01963   3 TALVTGAASGIGLAIARALAAAGA-NVVVNDFGEEGAEAAAKVAGdaggSVIYLPADVTKEDEIADMIAAAAAEFGGLDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    80 VLANAGIaedtamffaSHPTGIP--PPPDMTGLTDINFTGAIYTSYLAMhyfrrSPEKTKGNRHLIIMSSIGGLYPCAHT 157
Cdd:TIGR01963  82 LVNNAGI---------QHVAPIEefPPEDWDRIIAVMLTSAFHTIRAAL-----PHMKKQGWGRIINIASAHGLVASPFK 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 83775806   158 PVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:TIGR01963 148 SAYVAAKHGLIGLTKVLALEVAEHGITVNAICPGYVRTPL 187
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 5-197 7.91e-26

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: 101.64  E-value: 7.91e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   5 ALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLRN----TIFHQVDVTKYEQQGAAFDKIFNEEKRLDFV 80
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAG-YNVALAARRTDRLDELKAELLNpnpsVEVEILDVTDEERNQLVIAELEAELGGLDLV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  81 LANAGIAedtamffASHPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRspektKGNRHLIIMSSIGGLYPCAHTPVY 160
Cdd:cd05350  80 IINAGVG-------KGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRA-----KGRGHLVLISSVAALRGLPGAAAY 147

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 83775806 161 SATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:cd05350 148 SASKAALSSLAESLRYDVKKRGIRVTVINPGFIDTPL 184
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 3-210 1.73e-25

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 101.21  E-value: 1.73e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   3 LVALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLA 82
Cdd:cd05371   3 LVAVVTGGASGLGLATVERLLAQGA-KVVILDLPNSPGETVAKLGDNCRFVPVDVTSEKDVKAALALAKAKFGRLDIVVN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  83 NAGI--AEDTAMFFASHPTgipPPPDMTGLTDINFTGAIYTSYLAMHYFRRSPEKTKGNRHLII-MSSIGGLYPCAHTPV 159
Cdd:cd05371  82 CAGIavAAKTYNKKGQQPH---SLELFQRVINVNLIGTFNVIRLAAGAMGKNEPDQGGERGVIInTASVAAFEGQIGQAA 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 83775806 160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTelqafFPEKI 210
Cdd:cd05371 159 YSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAG-----LPEKV 204
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 4-203 5.85e-25

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


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 99.63  E-value: 5.85e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR--------NTIFHQVDVTKYEQQGAAFDKIFNEEK 75
Cdd:cd08939   3 HVLITGGSSGIGKALAKELVKEGA-NVIIVARSESKLEEAVEEIEaeanasgqKVSYISADLSDYEEVEQAFAQAVEKGG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  76 RLDFVLANAGIAEdtAMFFAshptgippppDMTG-----LTDINFTGAIYtsylAMHY-FRRspEKTKGNRHLIIMSSIG 149
Cdd:cd08939  82 PPDLVVNCAGISI--PGLFE----------DLTAeeferGMDVNYFGSLN----VAHAvLPL--MKEQRPGHIVFVSSQA 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 83775806 150 GLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQ 203
Cdd:cd08939 144 ALVGIYGYSAYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTPGFEEENK 197
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-231 2.24e-24

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 98.02  E-value: 2.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlWKVhIIGSNANR------GEEAAASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRL 77
Cdd:PRK12825   8 VALVTGAARGLGRAIALRLARAG-ADV-VVHYRSDEeaaeelVEAVEALGRRAQAVQADVTDKAALEAAVAAAVERFGRI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   78 DFVLANAGIAEDTAMffashptgipppPDMT-----GLTDINFTGAIYTSYLAMHYFRrspeKTKGNRhLIIMSSIGGLY 152
Cdd:PRK12825  86 DILVNNAGIFEDKPL------------ADMSddewdEVIDVNLSGVFHLLRAVVPPMR----KQRGGR-IVNISSVAGLP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  153 PCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQ-------AFFPEKIVMKMSDVTNVVLKL- 224
Cdd:PRK12825 149 GWPGRSNYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEeareakdAETPLGRSGTPEDIARAVAFLc 228

                        250
                 ....*....|....*
gi 83775806  225 ------ISGT--EVT 231
Cdd:PRK12825 229 sdasdyITGQviEVT 243
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 12-226 2.33e-24

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: 97.89  E-value: 2.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    12 SGMGLDVAQELDKTGlWKVHIIGSN---ANRGEEAAASLRNTIFHqVDVTKYEQQGAAFDKIFNEEKRLDFVLANAGIAe 88
Cdd:pfam13561   6 SGIGWAIARALAEEG-AEVVLTDLNealAKRVEELAEELGAAVLP-CDVTDEEQVEALVAAAVEKFGRLDILVNNAGFA- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    89 dtamffashPTGIPPPPDMTG-----LTDINFTGAIYTSYLAMHYFRRspektKGNrhLIIMSSIGGLYPCAHTPVYSAT 163
Cdd:pfam13561  83 ---------PKLKGPFLDTSRedfdrALDVNLYSLFLLAKAALPLMKE-----GGS--IVNLSSIGAERVVPNYNAYGAA 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83775806   164 KHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTT-----ELQAFFPEKIVMK----MSDVTNVVLKLIS 226
Cdd:pfam13561 147 KAALEALTRYLAVELGPRGIRVNAISPGPIKTLAASGipgfdELLAAAEARAPLGrlgtPEEVANAAAFLAS 218
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 1-226 2.38e-24

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: 98.22  E-value: 2.38e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   1 MVLVALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASL-----RNTIFHQVDVTKYEQQGAAFDKIFNEEK 75
Cdd:cd05366   1 MSKVAIITGAAQGIGRAIAERLAADGF-NIVLADLNLEEAAKSTIQEiseagYNAVAVGADVTDKDDVEALIDQAVEKFG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  76 RLDFVLANAGIAedtamffASHPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRspEKTKGNrhLIIMSSIGGLYPCA 155
Cdd:cd05366  80 SFDVMVNNAGIA-------PITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKK--LGHGGK--IINASSIAGVQGFP 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806 156 HTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTT--------------ELQAFFPEKIVMKM----SDV 217
Cdd:cd05366 149 NLGAYSASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYideevgeiagkpegEGFAEFSSSIPLGRlsepEDV 228


                ....*....
gi 83775806 218 TNVVLKLIS 226
Cdd:cd05366 229 AGLVSFLAS 237
PRK08267 PRK08267
SDR family oxidoreductase;
6-199 3.51e-24

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 98.09  E-value: 3.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    6 LITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASL--RNTIFHQVDVTKYEQQGAAFDKiFNEE--KRLDFVL 81
Cdd:PRK08267   5 FITGAASGIGRATALLFAAEG-WRVGAYDINEAGLAALAAELgaGNAWTGALDVTDRAAWDAALAD-FAAAtgGRLDVLF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   82 ANAGIAEDTAmfFASHPtgippPPDMTGLTDINFTGAIYTSYLAMHYFRRSPektkgNRHLIIMSSIGGLYPCAHTPVYS 161
Cdd:PRK08267  83 NNAGILRGGP--FEDIP-----LEAHDRVIDINVKGVLNGAHAALPYLKATP-----GARVINTSSASAIYGQPGLAVYS 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 83775806  162 ATKHGLVGFTRSvgkrlLD-----EGVKVNTVCPGVVLTPLMT 199
Cdd:PRK08267 151 ATKFAVRGLTEA-----LDlewrrHGIRVADVMPLFVDTAMLD 188
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 4-198 4.30e-24

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: 97.48  E-value: 4.30e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTIFHQV-------DVTKYEQQGAAFDKIFNEEKR 76
Cdd:cd05364   5 VAIITGSSSGIGAGTAILFARLGA-RLALTGRDAERLEETRQSCLQAGVSEKkillvvaDLTEEEGQDRIISTTLAKFGR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  77 LDFVLANAGIA-----EDTAMFFASHptgippppdmtgLTDINFTGAIYTSYLAMHYFRrspeKTKGNrhLIIMSSIGGL 151
Cdd:cd05364  84 LDILVNNAGILakgggEDQDIEEYDK------------VMNLNLRAVIYLTKLAVPHLI----KTKGE--IVNVSSVAGG 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 83775806 152 YPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLM 198
Cdd:cd05364 146 RSFPGVLYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFH 192
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 4-205 4.50e-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: 97.30  E-value: 4.50e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLRNTIFH-QVDVTKYEQQGAAFDKIFNEEKRLDFVLA 82
Cdd:cd05374   2 VVLITGCSSGIGLALALALAAQG-YRVIATARNPDKLESLGELLNDNLEVlELDVTDEESIKAAVKEVIERFGRIDVLVN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  83 NAGI-----AEDTamffashptgipPPPDMTGLTDINFTGAIYTSYLAMHYFRRSPektKGnrHLIIMSSIGGLYPCAHT 157
Cdd:cd05374  81 NAGYglfgpLEET------------SIEEVRELFEVNVFGPLRVTRAFLPLMRKQG---SG--RIVNVSSVAGLVPTPFL 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 83775806 158 PVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAF 205
Cdd:cd05374 144 GPYCASKAALEALSESLRLELAPFGIKVTIIEPGPVRTGFADNAAGSA 191
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 4-226 8.27e-24

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: 96.68  E-value: 8.27e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRN-TIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLA 82
Cdd:cd05341   7 VAIVTGGARGLGLAHARLLVAEGA-KVVLSDILDEEGQAAAAELGDaARFFHLDVTDEDGWTAVVDTAREAFGRLDVLVN 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  83 NAGIA-----EDTAMffashptgipppPDMTGLTDINFTGAIYTSYLAMhyfrrSPEKTKGNRHLIIMSSIGGLYPCAHT 157
Cdd:cd05341  86 NAGILtggtvETTTL------------EEWRRLLDINLTGVFLGTRAVI-----PPMKEAGGGSIINMSSIEGLVGDPAL 148

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83775806 158 PVYSATKHGLVGFTRS--VGKRLLDEGVKVNTVCPGVVLTPLM------TTELQAFFPEKI--VMKMSDVTNVVLKLIS 226
Cdd:cd05341 149 AAYNASKGAVRGLTKSaaLECATQGYGIRVNSVHPGYIYTPMTdelliaQGEMGNYPNTPMgrAGEPDEIAYAVVYLAS 227
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 4-204 1.13e-23

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


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 96.36  E-value: 1.13e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlwkVHIIgSNANRGEEAAASLRNTI---------FHQVDVTKYEQQGAAFDKIFNEE 74
Cdd:cd08940   4 VALVTGSTSGIGLGIARALAAAG---ANIV-LNGFGDAAEIEAVRAGLaakhgvkvlYHGADLSKPAAIEDMVAYAQRQF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  75 KRLDFVLANAGIaedtamffaSHPTGIPP-PPDM-TGLTDINFTGAIYTSYLAMhyfrrSPEKTKGNRHLIIMSSIGGLY 152
Cdd:cd08940  80 GGVDILVNNAGI---------QHVAPIEDfPTEKwDAIIALNLSAVFHTTRLAL-----PHMKKQGWGRIINIASVHGLV 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 83775806 153 PCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQA 204
Cdd:cd08940 146 ASANKSAYVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPLVEKQISA 197
PRK06172 PRK06172
SDR family oxidoreductase;
4-226 1.34e-23

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 96.36  E-value: 1.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK06172   9 VALVTGGAAGIGRATALAFAREGA-KVVVADRDAAGGEETVALIReaggEALFVACDVTRDAEVKALVEQTIAAYGRLDY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAedtamffashpTGIPPPPDMT-----GLTDINFTGAiytsYLAMHYfrRSPEKTK-GNRHLIIMSSIGGLYP 153
Cdd:PRK06172  88 AFNNAGIE-----------IEQGRLAEGSeaefdAIMGVNVKGV----WLCMKY--QIPLMLAqGGGAIVNTASVAGLGA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  154 CAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLM--TTELQAFFPEKI--------VMKMSDVTNVVLK 223
Cdd:PRK06172 151 APKMSIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFrrAYEADPRKAEFAaamhpvgrIGKVEEVASAVLY 230


                 ...
gi 83775806  224 LIS 226
Cdd:PRK06172 231 LCS 233
FabG-like PRK07231
SDR family oxidoreductase;
4-208 1.39e-23

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 96.05  E-value: 1.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR---NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFV 80
Cdd:PRK07231   7 VAIVTGASSGIGEGIARRFAAEGA-RVVVTDRNEEAAERVAAEILaggRAIAVAADVSDEADVEAAVAAALERFGSVDIL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   81 LANAGIaedtamffaSHPTGipPPPDMT-----GLTDINFTGAIYTSYLAMHYFRRspektkgnRH---LIIMSSIGGLY 152
Cdd:PRK07231  86 VNNAGT---------THRNG--PLLDVDeaefdRIFAVNVKSPYLWTQAAVPAMRG--------EGggaIVNVASTAGLR 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 83775806  153 PCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAFFPE 208
Cdd:PRK07231 147 PRPGLGWYNASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFMGEPTPE 202
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 4-211 1.63e-23

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 95.65  E-value: 1.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIG-SNANRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKRLD 78
Cdd:PRK05557   7 VALVTGASRGIGRAIAERLAAQGA-NVVINYaSSEAGAEALVAEIGalggKALAVQGDVSDAESVERAVDEAKAEFGGVD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   79 FVLANAGIAEDTAMFfashptgippppDMT-----GLTDINFTGAIYTSYLAMHYFRRSpektKGNRhlII-MSSIGGLY 152
Cdd:PRK05557  86 ILVNNAGITRDNLLM------------RMKeedwdRVIDTNLTGVFNLTKAVARPMMKQ----RSGR--IInISSVVGLM 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 83775806  153 PCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTELQAFFPEKIV 211
Cdd:PRK05557 148 GNPGQANYAASKAGVIGFTKSLARELASRGITVNAVAPGFIETD-MTDALPEDVKEAIL 205
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 4-197 1.92e-23

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: 95.91  E-value: 1.92e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIigsNANRGEEAAASLRNTI--------FHQVDVTKYEQQGAAFDKIFNEEK 75
Cdd:cd05358   5 VALVTGASSGIGKAIAIRLATAGA-NVVV---NYRSKEDAAEEVVEEIkavggkaiAVQADVSKEEDVVALFQSAIKEFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  76 RLDFVLANAGIAEDTamffashPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRSpeKTKGNrhLIIMSSIGGLYPCA 155
Cdd:cd05358  81 TLDILVNNAGLQGDA-------SSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKS--KIKGK--IINMSSVHEKIPWP 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 83775806 156 HTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:cd05358 150 GHVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPI 191
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 4-252 3.90e-23

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 95.35  E-value: 3.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNT----IFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK13394   9 TAVVTGAASGIGKEIALELARAGA-AVAIADLNQDGANAVADEINKAggkaIGVAMDVTNEDAVNAGIDKVAERFGSVDI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAedtamffASHPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRSpekTKGNRhLIIMSSIGGLYPCAHTPV 159
Cdd:PRK13394  88 LVSNAGIQ-------IVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKD---DRGGV-VIYMGSVHSHEASPLKSA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAFFPEKIVMKMSDVTNVVL-KLISG--TEVTDSNGT 236
Cdd:PRK13394 157 YVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQIPEQAKELGISEEEVVKKVMLgKTVDGvfTTVEDVAQT 236

                        250       260
                 ....*....|....*....|.
gi 83775806  237 -----SVPSDQLHSRAILISG 252
Cdd:PRK13394 237 vlflsSFPSAALTGQSFVVSH 257
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
1-198 3.62e-22

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 92.48  E-value: 3.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    1 MVLVALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKR 76
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDG-FKVAIVDYNEETAQAAADKLSkdggKAIAVKADVSDRDQVFAAVRQVVDTFGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   77 LDFVLANAGIAEDTamffashPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRSPEKTKgnrhLIIMSSIGGLYPCAH 156
Cdd:PRK08643  80 LNVVVNNAGVAPTT-------PIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHGGK----IINATSQAGVVGNPE 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 83775806  157 TPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLM 198
Cdd:PRK08643 149 LAVYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKTPMM 190
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 4-213 4.29e-22

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: 92.01  E-value: 4.29e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRN-----TIFHQVDVTKYEQQGAAFDKIFNEEKRLD 78
Cdd:cd05352  10 VAIVTGGSRGIGLAIARALAEAGA-DVAIIYNSAPRAEEKAEELAKkygvkTKAYKCDVSSQESVEKTFKQIQKDFGKID 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  79 FVLANAGIAEDTamffashPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRrspEKTKGNrhLIIMSSIGGLYP--CAH 156
Cdd:cd05352  89 ILIANAGITVHK-------PALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFK---KQGKGS--LIITASMSGTIVnrPQP 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806 157 TPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL---MTTELQAFFPEKIVMK 213
Cdd:cd05352 157 QAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLtdfVDKELRKKWESYIPLK 216
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 1-226 4.81e-22

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 92.09  E-value: 4.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    1 MVLVALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTI--------FHQVDVTKYEQQGAAFDKIFN 72
Cdd:PRK12827   5 DSRRVLITGGSGGLGRAIAVRLAADGA-DVIVLDIHPMRGRAEADAVAAGIeaaggkalGLAFDVRDFAATRAALDAGVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   73 EEKRLDFVLANAGIAEDTAMffashptgipppPDMTG-----LTDINFTGAIYTSY-LAMHYFRrspekTKGNRHLIIMS 146
Cdd:PRK12827  84 EFGRLDILVNNAGIATDAAF------------AELSIeewddVIDVNLDGFFNVTQaALPPMIR-----ARRGGRIVNIA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  147 SIGGLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL-----MTTELQAFFPEKIVMKMSDVTNVV 221
Cdd:PRK12827 147 SVAGVRGNRGQVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMadnaaPTEHLLNPVPVQRLGEPDEVAALV 226


                 ....*
gi 83775806  222 LKLIS 226
Cdd:PRK12827 227 AFLVS 231
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 4-204 5.66e-22

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


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 91.65  E-value: 5.66e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASL----RNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:cd05347   7 VALVTGASRGIGFGIASGLAEAGA-NIVINSRNEEKAEEAQQLIekegVEATAFTCDVSDEEAIKAAVEAIEEDFGKIDI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGIAEdtamffaSHPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRspektKGNRHLI----IMSSIGGLYpca 155
Cdd:cd05347  86 LVNNAGIIR-------RHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIK-----QGHGKIInicsLLSELGGPP--- 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 83775806 156 hTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTELQA 204
Cdd:cd05347 151 -VPAYAASKGGVAGLTKALATEWARHGIQVNAIAPGYFATE-MTEAVVA 197
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 7-221 5.69e-22

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


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 91.36  E-value: 5.69e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   7 ITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASL--RNTIFHQVDVTKYEQQGAAFDKIFNEE-KRLDFVLAN 83
Cdd:cd08931   5 ITGAASGIGRETALLFARNG-WFVGLYDIDEDGLAALAAELgaENVVAGALDVTDRAAWAAALADFAAATgGRLDALFNN 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  84 AGIAEdtamffaSHPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRSPektkGNRhLIIMSSIGGLYPCAHTPVYSAT 163
Cdd:cd08931  84 AGVGR-------GGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATP----GAR-VINTASSSAIYGQPDLAVYSAT 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83775806 164 KHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAFFPEK---IVMKMSDVTNVV 221
Cdd:cd08931 152 KFAVRGLTEALDVEWARHGIRVADVWPWFVDTPILTKGETGAAPKKglgRVLPVSDVAKVV 212
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 4-209 1.32e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 90.94  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLrNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLAN 83
Cdd:PRK06057   9 VAVITGGGSGIGLATARRLAAEGA-TVVVGDIDPEAGKAAADEV-GGLFVPTDVTDEDAVNALFDTAAETYGSVDIAFNN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   84 AGIAedtamffashptgiPPPPDM---TGL------TDINFTGAIYTSYLAMHYFRRspektKGNRHLIIMSSIGGLYPC 154
Cdd:PRK06057  87 AGIS--------------PPEDDSilnTGLdawqrvQDVNLTSVYLCCKAALPHMVR-----QGKGSIINTASFVAVMGS 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 83775806  155 AHTPV-YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMtTELQAFFPEK 209
Cdd:PRK06057 148 ATSQIsYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLL-QELFAKDPER 202
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 6-225 1.61e-21

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: 90.22  E-value: 1.61e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   6 LITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLANAG 85
Cdd:COG3967   9 LITGGTSGIGLALAKRLHARGN-TVIITGRREEKLEEAAAANPGLHTIVLDVADPASIAALAEQVTAEFPDLNVLINNAG 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  86 IaedtaMFFASHPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRSPEKTkgnrhlII-MSSIGGLYPCAHTPVYSATK 164
Cdd:COG3967  88 I-----MRAEDLLDEAEDLADAEREITTNLLGPIRLTAAFLPHLKAQPEAA------IVnVSSGLAFVPLAVTPTYSATK 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83775806 165 HGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTelQAFFPEKivMKMSDVTNVVLKLI 225
Cdd:COG3967 157 AALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTGG--QGGDPRA--MPLDEFADEVMAGL 213
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 5-195 2.24e-21

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


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 90.03  E-value: 2.24e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   5 ALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLRN---TIFH--QVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:cd05346   3 VLITGASSGIGEATARRFAKAG-AKLILTGRRAERLQELADELGAkfpVKVLplQLDVSDRESIEAALENLPEEFRDIDI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGIAEDTAmffashPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFrrspeKTKGNRHLIIMSSIGGLYPCAHTPV 159
Cdd:cd05346  82 LVNNAGLALGLD------PAQEADLEDWETMIDTNVKGLLNVTRLILPIM-----IARNQGHIINLGSIAGRYPYAGGNV 150

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 83775806 160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT 195
Cdd:cd05346 151 YCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVET 186
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 4-197 3.20e-21

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: 89.52  E-value: 3.20e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTIFH----QVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:cd08934   5 VALVTGASSGIGEATARALAAEGA-AVAIAARRVDRLEALADELEAEGGKalvlELDVTDEQQVDAAVERTVEALGRLDI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGIaedtaMFFAshPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYfrrspEKTKGNRHLIIMSSIGGLYPCAHTPV 159
Cdd:cd08934  84 LVNNAGI-----MLLG--PVEDADTTDWTRMIDTNLLGLMYTTHAALPH-----HLLRNKGTIVNISSVAGRVAVRNSAV 151

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 83775806 160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:cd08934 152 YNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTEL 189
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 5-203 6.00e-21

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: 89.04  E-value: 6.00e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   5 ALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTIFH----QVDVTKYEQQGAAFDKIFNE-EKRLDF 79
Cdd:cd05329   9 ALVTGGTKGIGYAIVEELAGLGA-EVYTCARNQKELDECLTEWREKGFKvegsVCDVSSRSERQELMDTVASHfGGKLNI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAG--IAEDTAMFfashptgipPPPDMTGLTDINFTGAIYTSYLAMHYFRRSpektkGNRHLIIMSSIGGLYPCAHT 157
Cdd:cd05329  88 LVNNAGtnIRKEAKDY---------TEEDYSLIMSTNFEAAYHLSRLAHPLLKAS-----GNGNIVFISSVAGVIAVPSG 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 83775806 158 PVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQ 203
Cdd:cd05329 154 APYGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQ 199
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 4-229 2.02e-20

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: 87.30  E-value: 2.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTG----LWKVHIIGSNANRGEEAAASLRNTIFhQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGakvvILDINEKGAEETANNVRKAGGKVHYY-KCDVSKREEVYEAAKKIKKEVGDVTI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGIAedtamfFASHPTGIPPPpDMTGLTDINFTGAIYT--SYL-AMHyfrrspEKTKGnrHLIIMSSIGGLYPCAH 156
Cdd:cd05339  80 LINNAGVV------SGKKLLELPDE-EIEKTFEVNTLAHFWTtkAFLpDML------ERNHG--HIVTIASVAGLISPAG 144

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83775806 157 TPVYSATKHGLVGFTRSVG---KRLLDEGVKVNTVCPGVVLTPL---MTTELQAFFPekivmkMSDVTNVVLKLISGTE 229
Cdd:cd05339 145 LADYCASKAAAVGFHESLRlelKAYGKPGIKTTLVCPYFINTGMfqgVKTPRPLLAP------ILEPEYVAEKIVRAIL 217
PRK06484 PRK06484
short chain dehydrogenase; Validated
 4-196 4.34e-20

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 89.52  E-value: 4.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNAnrgeEAAASLRNT-----IFHQVDVTKYEQQGAAFDKIFNEEKRLD 78
Cdd:PRK06484 271 VVAITGGARGIGRAVADRFAAAG-DRLLIIDRDA----EGAKKLAEAlgdehLSVQADITDEAAVESAFAQIQARWGRLD 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   79 FVLANAGIAEDTAmffashPTGIPPPPDMTGLTDINFTGAIYTSylamhyfRRSPEKTKGNRHLIIMSSIGGLYPCAHTP 158
Cdd:PRK06484 346 VLVNNAGIAEVFK------PSLEQSAEDFTRVYDVNLSGAFACA-------RAAARLMSQGGVIVNLGSIASLLALPPRN 412

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 83775806  159 VYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTP 196
Cdd:PRK06484 413 AYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIETP 450
PRK06124 PRK06124
SDR family oxidoreductase;
4-195 1.42e-19

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 85.53  E-value: 1.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLWkVHIIGSNANRGEEAAASLRNT-------IFhqvDVTKYEQQGAAFDKIFNEEKR 76
Cdd:PRK06124  13 VALVTGSARGLGFEIARALAGAGAH-VLVNGRNAATLEAAVAALRAAggaaealAF---DIADEEAVAAAFARIDAEHGR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   77 LDFVLANAGiAEDtamffaSHPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRSpektKGNRhLIIMSSIGGLYPCAH 156
Cdd:PRK06124  89 LDILVNNVG-ARD------RRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQ----GYGR-IIAITSIAGQVARAG 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 83775806  157 TPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT 195
Cdd:PRK06124 157 DAVYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFAT 195
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 4-241 1.76e-19

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 84.85  E-value: 1.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTIFH--QVDVTKYEQQGAAFDKIFNEEKRLDFVL 81
Cdd:PRK12828   9 VVAITGGFGGLGRATAAWLAARGA-RVALIGRGAAPLSQTLPGVPADALRigGIDLVDPQAARRAVDEVNRQFGRLDALV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   82 ANAGIaedtamfFASHPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRSPektkGNRhLIIMSSIGGLYPCAHTPVYS 161
Cdd:PRK12828  88 NIAGA-------FVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASG----GGR-IVNIGAGAALKAGPGMGAYA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  162 ATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELqaffPEKIV---MKMSDVTNVVLKLISgTEVTDSNGTSV 238
Cdd:PRK12828 156 AAKAGVARLTEALAAELLDRGITVNAVLPSIIDTPPNRADM----PDADFsrwVTPEQIAAVIAFLLS-DEAQAITGASI 230


                 ...
gi 83775806  239 PSD 241
Cdd:PRK12828 231 PVD 233
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
1-213 2.66e-19

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 84.43  E-value: 2.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    1 MVLVALITGGTSGMGLDVAQELDKTGLWKVHIIGSNANR-----GEEAAASLRNTIFhQVDVTKYEQQGAAFDKIFNEEK 75
Cdd:PRK12824   1 MKKIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCakdwfEEYGFTEDQVRLK-ELDVTDTEECAEALAEIEEEEG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   76 RLDFVLANAGIAEDTAMFFASHPtgippppDMTGLTDINFTGAIYTSYLAMhyfrrSPEKTKGNRHLIIMSSIGGLYPCA 155
Cdd:PRK12824  80 PVDILVNNAGITRDSVFKRMSHQ-------EWNDVINTNLNSVFNVTQPLF-----AAMCEQGYGRIINISSVNGLKGQF 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83775806  156 HTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL---MTTELQAFFPEKIVMK 213
Cdd:PRK12824 148 GQTNYSAAKAGMIGFTKALASEGARYGITVNCIAPGYIATPMveqMGPEVLQSIVNQIPMK 208
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 4-214 3.01e-19

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 84.29  E-value: 3.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIigsNANRGEEAAASLRNTIFH--------QVDVTKYEQQGAAFDKIFNEEK 75
Cdd:PRK12935   8 VAIVTGGAKGIGKAITVALAQEGA-KVVI---NYNSSKEAAENLVNELGKeghdvyavQADVSKVEDANRLVEEAVNHFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   76 RLDFVLANAGIAEDTAMFFASHPtgippppDMTGLTDINFTGAIYTSYLAMHYFRRSpektKGNRHLIIMSSIGGLYPCA 155
Cdd:PRK12935  84 KVDILVNNAGITRDRTFKKLNRE-------DWERVIDVNLSSVFNTTSAVLPYITEA----EEGRIISISSIIGQAGGFG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 83775806  156 HTPvYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTELQAFFPEKIVMKM 214
Cdd:PRK12935 153 QTN-YSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTE-MVAEVPEEVRQKIVAKI 209
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 4-199 5.00e-19

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


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 83.66  E-value: 5.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASL--RNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVL 81
Cdd:cd05326   6 VAIITGGASGIGEATARLFAKHGA-RVVIADIDDDAGQAVAAELgdPDISFVHCDVTVEADVRAAVDTAVARFGRLDIMF 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  82 ANAGIAEdtamffashptgiPPPPDM--TGLTDINFTGAI--YTSYLAMHYFRRS--PEKtKGNrhLIIMSSIGGLYPCA 155
Cdd:cd05326  85 NNAGVLG-------------APCYSIleTSLEEFERVLDVnvYGAFLGTKHAARVmiPAK-KGS--IVSVASVAGVVGGL 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 83775806 156 HTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMT 199
Cdd:cd05326 149 GPHAYTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLT 192
PRK08219 PRK08219
SDR family oxidoreductase;
1-205 6.46e-19

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 83.06  E-value: 6.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    1 MVLVALITGGTSGMGLDVAQELDKTglWKVHIIGSNANRGEEAAASLRNTIFHQVDVTKYEQQGAAFDKIfneeKRLDFV 80
Cdd:PRK08219   2 ERPTALITGASRGIGAAIARELAPT--HTLLLGGRPAERLDELAAELPGATPFPVDLTDPEAIAAAVEQL----GRLDVL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   81 LANAGIAEDTamffashPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRSpektKGnrHLIIMSSIGGLYPCAHTPVY 160
Cdd:PRK08219  76 VHNAGVADLG-------PVAESTVDEWRATLEVNVVAPAELTRLLLPALRAA----HG--HVVFINSGAGLRANPGWGSY 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 83775806  161 SATKHGLVGFTRSVgkRLLDEG-VKVNTVCPGVVLTPlMTTELQAF 205
Cdd:PRK08219 143 AASKFALRALADAL--REEEPGnVRVTSVHPGRTDTD-MQRGLVAQ 185
AcAcCoA_reduct TIGR01829
acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the ...
 4-211 6.62e-19

acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the family short-chain-alcohol dehydrogenases. Note that, despite the precision implied by the enzyme name, the reaction of EC 1.1.1.36 is defined more generally as (R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH. Members of this family may act in the biosynthesis of poly-beta-hydroxybutyrate (e.g. Rhizobium meliloti) and related poly-beta-hydroxyalkanoates. Note that the member of this family from Azospirillum brasilense, designated NodG, appears to lack acetoacetyl-CoA reductase activity and to act instead in the production of nodulation factor. This family is downgraded to subfamily for this NodG. Other proteins designated NodG, as from Rhizobium, belong to related but distinct protein families.


Pssm-ID: 273823 [Multi-domain]  Cd Length: 242  Bit Score: 83.25  E-value: 6.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806     4 VALITGGTSGMGLDVAQELDKTGlwkvHIIGSNANRGEEAAASLRNT--------IFHQVDVTKYEQQGAAFDKIFNEEK 75
Cdd:TIGR01829   2 IALVTGGMGGIGTAICQRLAKDG----YRVAANCGPNEERAEAWLQEqgalgfdfRVVEGDVSSFESCKAAVAKVEAELG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    76 RLDFVLANAGIAEDTamFFASHPtgippPPDMTGLTDINFTGAIYTSYLAMHYFRRspektKGNRHLIIMSSIGGLYPCA 155
Cdd:TIGR01829  78 PVDVLVNNAGITRDA--TFKKMT-----YEQWDAVIDTNLNSVFNVTQPVIDGMRE-----RGWGRIINISSVNGQKGQF 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 83775806   156 HTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTELQAFFPEKIV 211
Cdd:TIGR01829 146 GQTNYSAAKAGMIGFTKALAQEGATKGVTVNTISPGYIATD-MVMAMREDVLNSIV 200
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 5-198 1.56e-18

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: 81.97  E-value: 1.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   5 ALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLANA 84
Cdd:cd05370   8 VLITGGTSGIGLALARKFLEAGN-TVIITGRREERLAEAKKELPNIHTIVLDVGDAESVEALAEALLSEYPNLDILINNA 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  85 GIA-----EDTAMFFASHPTGIppppdmtgltDINFTGAIYTSYLAMHYFRRSPEKTkgnrhLIIMSSIGGLYPCAHTPV 159
Cdd:cd05370  87 GIQrpidlRDPASDLDKADTEI----------DTNLIGPIRLIKAFLPHLKKQPEAT-----IVNVSSGLAFVPMAANPV 151

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 83775806 160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLM 198
Cdd:cd05370 152 YCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELH 190
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 4-201 1.82e-18

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: 82.25  E-value: 1.82e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLRNT-----IFHQVDVTKYEQQGAAFDKIFNEEKRLD 78
Cdd:cd05369   5 VAFITGGGTGIGKAIAKAFAELG-ASVAIAGRKPEVLEAAAEEISSAtggraHPIQCDVRDPEAVEAAVDETLKEFGKID 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  79 FVLANAG---IAEDTAMFFASHPTGIppppdmtgltDINFTGAIYTSYLAMHYFRRSpeKTKGNrhLIIMSSIGGLYPCA 155
Cdd:cd05369  84 ILINNAAgnfLAPAESLSPNGFKTVI----------DIDLNGTFNTTKAVGKRLIEA--KHGGS--ILNISATYAYTGSP 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 83775806 156 -HTPVySATKHGLVGFTRSVGKRLLDEGVKVNTVCPGvvltPLMTTE 201
Cdd:cd05369 150 fQVHS-AAAKAGVDALTRSLAVEWGPYGIRVNAIAPG----PIPTTE 191
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 4-225 3.45e-18

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 81.91  E-value: 3.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLAN 83
Cdd:PRK07825   7 VVAITGGARGIGLATARALAALGA-RVAIGDLDEALAKETAAELGLVVGGPLDVTDPASFAAFLDAVEADLGPIDVLVNN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   84 AGIaedtaMffashPTG--IPPPPDMTGLT-DINFTGAIYTSYLAMhyfRRSPEKTKGnrHLIIMSSIGGLYPCAHTPVY 160
Cdd:PRK07825  86 AGV-----M-----PVGpfLDEPDAVTRRIlDVNVYGVILGSKLAA---PRMVPRGRG--HVVNVASLAGKIPVPGMATY 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83775806  161 SATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVltplmTTELQAFFPEKIVMKM---SDVTNVVLKLI 225
Cdd:PRK07825 151 CASKHAVVGFTDAARLELRGTGVHVSVVLPSFV-----NTELIAGTGGAKGFKNvepEDVAAAIVGTV 213
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 4-197 4.47e-18

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


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 81.43  E-value: 4.47e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:cd08945   5 VALVTGATSGIGLAIARRLGKEGL-RVFVCARGEEGLATTVKELReagvEADGRTCDVRSVPEIEALVAAAVARYGPIDV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGiaedtamffasHPTGipppPDMTGLTDINFTGAIYTSYLAMhyFRRSPE-------KTKGNRHLIIMSSIGGLY 152
Cdd:cd08945  84 LVNNAG-----------RSGG----GATAELADELWLDVVETNLTGV--FRVTKEvlkaggmLERGTGRIINIASTGGKQ 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 83775806 153 PCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:cd08945 147 GVVHAAPYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPM 191
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 4-204 7.89e-18

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: 80.40  E-value: 7.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNT----IFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:cd05344   3 VALVTAASSGIGLAIARALAREGA-RVAICARNRENLERAASELRAGgagvLAVVADLTDPEDIDRLVEKAGDAFGRVDI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGIaedtamffashptgiPPPPDMTGLTD--------INFTGAIYTSYLAMHYFRRspektKGNRHLIIMSSIGGL 151
Cdd:cd05344  82 LVNNAGG---------------PPPGPFAELTDedwleafdLKLLSVIRIVRAVLPGMKE-----RGWGRIVNISSLTVK 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 83775806 152 YPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQA 204
Cdd:cd05344 142 EPEPNLVLSNVARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTERVRRLLEA 194
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 4-206 2.36e-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: 79.58  E-value: 2.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLR------NTIFHQVDVTKYEQQGAAFDKIFNEEKRL 77
Cdd:cd05327   3 VVVITGANSGIGKETARELAKRG-AHVIIACRNEEKGEEAAAEIKketgnaKVEVIQLDLSSLASVRQFAEEFLARFPRL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  78 DFVLANAGIaedtamffashptGIPPppdmTGLTDINFTGAIYTSYLAmHY---------FRRSPEKtkgnRhLIIMSSI 148
Cdd:cd05327  82 DILINNAGI-------------MAPP----RRLTKDGFELQFAVNYLG-HFlltnlllpvLKASAPS----R-IVNVSSI 138

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83775806 149 G-----------------GLYPcahTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAFF 206
Cdd:cd05327 139 AhragpidfndldlennkEYSP---YKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNGSFFL 210
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 4-226 2.96e-17

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: 78.86  E-value: 2.96e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLWKVHIIGSNANRGEEAAASLRN----TIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:cd05362   5 VALVTGASRGIGRAIAKRLARDGASVVVNYASSKAAAEEVVAEIEAaggkAIAVQADVSDPSQVARLFDAAEKAFGGVDI 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAG------IAEDTAMFFAShptgippppdmtgLTDINFTGAIYTSylamhyfRRSPEKTKGNRHLIIMSSIGGLYP 153
Cdd:cd05362  85 LVNNAGvmlkkpIAETSEEEFDR-------------MFTVNTKGAFFVL-------QEAAKRLRDGGRIINISSSLTAAY 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806 154 CAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAFFPEKIVmKMS---------DVTNVVLKL 224
Cdd:cd05362 145 TPNYGAYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYAGKTEEAVEGYA-KMSplgrlgepeDIAPVVAFL 223


                ..
gi 83775806 225 IS 226
Cdd:cd05362 224 AS 225
PRK06500 PRK06500
SDR family oxidoreductase;
5-198 4.70e-17

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 78.46  E-value: 4.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASL-RNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLAN 83
Cdd:PRK06500   9 ALITGGTSGIGLETARQFLAEGA-RVAITGRDPASLEAARAELgESALVIRADAGDVAAQKALAQALAEAFGRLDAVFIN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   84 AGIAE-------DTAMFFASHptgippppdmtgltDINFTGAIYTSYLAMHYFRRSPEktkgnrhLIIMSSIGGLYPCAH 156
Cdd:PRK06500  88 AGVAKfapledwDEAMFDRSF--------------NTNVKGPYFLIQALLPLLANPAS-------IVLNGSINAHIGMPN 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 83775806  157 TPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLM 198
Cdd:PRK06500 147 SSVYAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPLY 188
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 4-226 4.92e-17

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 78.09  E-value: 4.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK12939   9 RALVTGAARGLGAAFAEALAEAGA-TVAFNDGLAAEARELAAALEaaggRAHAIAADLADPASVQRFFDAAAAALGGLDG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAEDTAMFFAShptgippPPDMTGLTDINFTGAIYTSYLAMHYFRRSpektkGNRHLIIMSSIGGLYPCAHTPV 159
Cdd:PRK12939  88 LVNNAGITNSKSATELD-------IDTWDAVMNVNVRGTFLMLRAALPHLRDS-----GRGRIVNLASDTALWGAPKLGA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGvvltpLMTTELQAFFPE----KIVMKMS---------DVTNVVLKLIS 226
Cdd:PRK12939 156 YVASKGAVIGMTRSLARELGGRGITVNAIAPG-----LTATEATAYVPAderhAYYLKGRalerlqvpdDVAGAVLFLLS 230
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 4-241 5.59e-17

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


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 78.33  E-value: 5.59e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNT------IFHQVDVTKYEQQGAAFDKIFNEEKRL 77
Cdd:cd05330   5 VVLITGGGSGLGLATAVRLAKEGA-KLSLVDLNEEGLEAAKAALLEIapdaevLLIKADVSDEAQVEAYVDATVEQFGRI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  78 DFVLANAGIAEDTAmffashPTGIPPPPDMTGLTDINFTGAiytsYLAMHYFRRSPEKTKGNRhLIIMSSIGGLYPCAHT 157
Cdd:cd05330  84 DGFFNNAGIEGKQN------LTEDFGADEFDKVVSINLRGV----FYGLEKVLKVMREQGSGM-IVNTASVGGIRGVGNQ 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806 158 PVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAFFPE---------------KIVMKMSDVTNVVL 222
Cdd:cd05330 153 SGYAAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSLKQLGPEnpeeageefvsvnpmKRFGEPEEVAAVVA 232

                       250
                ....*....|....*....
gi 83775806 223 KLISGtEVTDSNGTSVPSD 241
Cdd:cd05330 233 FLLSD-DAGYVNAAVVPID 250
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-226 6.44e-17

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 77.90  E-value: 6.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlWKVHIigsNANRGEEAAASLRNT---IFhQVDVTKYEQQGAAFDKIFNEEKRLDFV 80
Cdd:PRK06463   9 VALITGGTRGIGRAIAEAFLREG-AKVAV---LYNSAENEAKELREKgvfTI-KCDVGNRDQVKKSKEVVEKEFGRVDVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   81 LANAGIAedTAMFFASHPTgipppPDMTGLTDINFTGAIYTSYLAMHYFRRSPektkgNRHLIIMSSIGGLYPCAH-TPV 159
Cdd:PRK06463  84 VNNAGIM--YLMPFEEFDE-----EKYNKMIKINLNGAIYTTYEFLPLLKLSK-----NGAIVNIASNAGIGTAAEgTTF 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83775806  160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLM--------TTELQAFFPEKIVMKMS----DVTNVVLKLIS 226
Cdd:PRK06463 152 YAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTlsgksqeeAEKLRELFRNKTVLKTTgkpeDIANIVLFLAS 230
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 3-197 1.81e-16

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: 77.11  E-value: 1.81e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   3 LVALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRN----TIFHQVDVTKYEQQGAAFDKIFNEEKRLD 78
Cdd:cd08935   6 KVAVITGGTGVLGGAMARALAQAGA-KVAALGRNQEKGDKVAKEITAlggrAIALAADVLDRASLERAREEIVAQFGTVD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  79 FVLANAGiaedtamffASHPTGIPPPP-----------DMTG-----LTDINFTGAIYTSylaMHYFRRSPEKTKGNrhL 142
Cdd:cd08935  85 ILINGAG---------GNHPDATTDPEhyepeteqnffDLDEegwefVFDLNLNGSFLPS---QVFGKDMLEQKGGS--I 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 83775806 143 IIMSSIGGLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:cd08935 151 INISSMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQ 205
PRK06484 PRK06484
short chain dehydrogenase; Validated
 4-203 2.00e-16

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 78.74  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASL-RNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLA 82
Cdd:PRK06484   7 VVLVTGAAGGIGRAACQRFARAG-DQVVVADRNVERARERADSLgPDHHALAMDVSDEAQIREGFEQLHREFGRIDVLVN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   83 NAGIAEDTAmffasHPTGIPPPPDMTGLTDINFTGAiytsYLAMHYFRRSPEKTKGNRHLIIMSSIGGLYPCAHTPVYSA 162
Cdd:PRK06484  86 NAGVTDPTM-----TATLDTTLEEFARLQAINLTGA----YLVAREALRLMIEQGHGAAIVNVASGAGLVALPKRTAYSA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 83775806  163 TKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTELQ 203
Cdd:PRK06484 157 SKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQ-MVAELE 196
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 4-227 2.03e-16

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: 76.73  E-value: 2.03e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwkvhIIGSNANRGEEAAASL--------RNTIFHQVDVTKYEQQGAAFDKIFNEEK 75
Cdd:cd05337   3 VAIVTGASRGIGRAIATELAARGF----DIAINDLPDDDQATEVvaevlaagRRAIYFQADIGELSDHEALLDQAWEDFG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  76 RLDFVLANAGIAedtamffashptgIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRS--------PEKTKG-NRHLIIMS 146
Cdd:cd05337  79 RLDCLVNNAGIA-------------VRPRGDLLDLTEDSFDRLIAINLRGPFFLTQAvarrmveqPDRFDGpHRSIIFVT 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806 147 SIGGLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTELQAFFPEKIVMKM---------SDV 217
Cdd:cd05337 146 SINAYLVSPNRGEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTD-MTAPVKEKYDELIAAGLvpirrwgqpEDI 224

                       250
                ....*....|
gi 83775806 218 TNVVLKLISG 227
Cdd:cd05337 225 AKAVRTLASG 234
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 4-196 2.33e-16

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 77.65  E-value: 2.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLRNT----IFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK07109  10 VVVITGASAGVGRATARAFARRG-AKVVLLARGEEGLEALAAEIRAAggeaLAVVADVADAEAVQAAADRAEEELGPIDT 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAedtamFFASHPTgiPPPPDMTGLTDINFTGAIYTSYLAMHYFRRspektKGNRHLIIMSSIGGLYPCAHTPV 159
Cdd:PRK07109  89 WVNNAMVT-----VFGPFED--VTPEEFRRVTEVTYLGVVHGTLAALRHMRP-----RDRGAIIQVGSALAYRSIPLQSA 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 83775806  160 YSATKHGLVGFTRSVGKRLLDEG--VKVNTVCPGVVLTP 196
Cdd:PRK07109 157 YCAAKHAIRGFTDSLRCELLHDGspVSVTMVQPPAVNTP 195
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 4-226 2.33e-16

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


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 76.27  E-value: 2.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGE-EAAASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLA 82
Cdd:cd05345   7 VAIVTGAGSGFGEGIARRFAQEGA-RVVIADINADGAErVAADIGEAAIAIQADVTKRADVEAMVEAALSKFGRLDILVN 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  83 NAGIaedtamffaSHPtgippPPDMTGLTDINF-------TGAIYTSYLAMhyfrrSPEKTKGNRHLII-MSSIGGLYPC 154
Cdd:cd05345  86 NAGI---------THR-----NKPMLEVDEEEFdrvfavnVKSIYLSAQAL-----VPHMEEQGGGVIInIASTAGLRPR 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806 155 AHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL-------MTTELQAFFPEKIVM----KMSDVTNVVLK 223
Cdd:cd05345 147 PGLTWYNASKGWVVTATKAMAVELAPRNIRVNCLCPVAGETPLlsmfmgeDTPENRAKFRATIPLgrlsTPDDIANAALY 226


                ...
gi 83775806 224 LIS 226
Cdd:cd05345 227 LAS 229
PRK06181 PRK06181
SDR family oxidoreductase;
4-195 4.15e-16

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 75.79  E-value: 4.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRN----TIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK06181   3 VVIITGASEGIGRALAVRLARAGA-QLVLAARNETRLASLAQELADhggeALVVPTDVSDAEACERLIEAAVARFGGIDI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAEDTAmfFAShptgIPPPPDMTGLTDINFTGAIYTSYLAMHYFRrspeKTKGnrHLIIMSSIGGLYPCAHTPV 159
Cdd:PRK06181  82 LVNNAGITMWSR--FDE----LTDLSVFERVMRVNYLGAVYCTHAALPHLK----ASRG--QIVVVSSLAGLTGVPTRSG 149

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 83775806  160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT 195
Cdd:PRK06181 150 YAASKHALHGFFDSLRIELADDGVAVTVVCPGFVAT 185
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 4-195 7.81e-16

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: 74.93  E-value: 7.81e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRN------TIFHqVDVTKYEQQGAAFDKIFNEEKRL 77
Cdd:cd05332   5 VVIITGASSGIGEELAYHLARLGA-RLVLSARREERLEEVKSECLElgapspHVVP-LDMSDLEDAEQVVEEALKLFGGL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  78 DFVLANAGI-----AEDTAMffashptgippppDMT-GLTDINFTGAIYTSYLAMHYFRrspEKTKGnrHLIIMSSIGGL 151
Cdd:cd05332  83 DILINNAGIsmrslFHDTSI-------------DVDrKIMEVNYFGPVALTKAALPHLI---ERSQG--SIVVVSSIAGK 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 83775806 152 YPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT 195
Cdd:cd05332 145 IGVPFRTAYAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDT 188
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 4-197 1.09e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 74.94  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlWKVhiIGSNANRGeeAAASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLAN 83
Cdd:PRK06179   6 VALVTGASSGIGRATAEKLARAG-YRV--FGTSRNPA--RAAPIPGVELLELDVTDDASVQAAVDEVIARAGRIDVLVNN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   84 AGI-----AEDTAMFFASHptgippppdmtgLTDINFTGAIYTSYLAMHYFRRspektKGNRHLIIMSSIGGLYPCAHTP 158
Cdd:PRK06179  81 AGVglagaAEESSIAQAQA------------LFDTNVFGILRMTRAVLPHMRA-----QGSGRIINISSVLGFLPAPYMA 143

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 83775806  159 VYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:PRK06179 144 LYAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNF 182
PRK05650 PRK05650
SDR family oxidoreductase;
6-200 1.35e-15

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 74.69  E-value: 1.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    6 LITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLRNTI----FHQVDVTKYEQQGAAFDKIfnEEK--RLDF 79
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREG-WRLALADVNEEGGEETLKLLREAGgdgfYQRCDVRDYSQLTALAQAC--EEKwgGIDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAedTAMFFASHPTGippppDMTGLTDINFTGAIYTSYLAMHYFRRSpektkGNRHLIIMSSIGGLYPCAHTPV 159
Cdd:PRK05650  81 IVNNAGVA--SGGFFEELSLE-----DWDWQIAINLMGVVKGCKAFLPLFKRQ-----KSGRIVNIASMAGLMQGPAMSS 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 83775806  160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTT 200
Cdd:PRK05650 149 YNVAKAGVVALSETLLVELADDEIGVHVVCPSFFQTNLLDS 189
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 4-196 1.51e-15

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


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 73.96  E-value: 1.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNT----IFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:cd05360   2 VVVITGASSGIGRATALAFAERGA-KVVLAARSAEALHELAREVRELggeaIAVVADVADAAQVERAADTAVERFGRIDT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGIA-----EDTamffashptgipPPPDMTGLTDINFTGAIYTSYLAMHYFRRspektKGNRHLIIMSSIGGLypc 154
Cdd:cd05360  81 WVNNAGVAvfgrfEDV------------TPEEFRRVFDVNYLGHVYGTLAALPHLRR-----RGGGALINVGSLLGY--- 140

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 83775806 155 AHTPV---YSATKHGLVGFTRSVGKRLLDEG--VKVNTVCPGVVLTP 196
Cdd:cd05360 141 RSAPLqaaYSASKHAVRGFTESLRAELAHDGapISVTLVQPTAMNTP 187
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 4-226 2.06e-15

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 73.70  E-value: 2.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRN----TIF-HQVDVTKYEQQGAAFDKIFNEEKRLD 78
Cdd:cd05343   8 VALVTGASVGIGAAVARALVQHGM-KVVGCARRVDKIEALAAECQSagypTLFpYQCDLSNEEQILSMFSAIRTQHQGVD 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  79 FVLANAGIAEDTAMFfashpTGipPPPDMTGLTDINftgAIYTSYLAMHYFRRSPEKTKGNRHLIIMSSIGG--LYPCAH 156
Cdd:cd05343  87 VCINNAGLARPEPLL-----SG--KTEGWKEMFDVN---VLALSICTREAYQSMKERNVDDGHIININSMSGhrVPPVSV 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83775806 157 TPVYSATKHGLVGFTRSVGK--RLLDEGVKVNTVCPGVVLTPLMTT------ELQAFFPEKI-VMKMSDVTNVVLKLIS 226
Cdd:cd05343 157 FHFYAATKHAVTALTEGLRQelREAKTHIRATSISPGLVETEFAFKlhdndpEKAAATYESIpCLKPEDVANAVLYVLS 235
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 4-194 2.52e-15

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: 73.52  E-value: 2.52e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlwKVHIIGS-NANRGEEAAASLRNT-----IFHQVDVTKYEQQGAAFDKIFNEEKRL 77
Cdd:cd08930   4 IILITGAAGLIGKAFCKALLSAG--ARLILADiNAPALEQLKEELTNLyknrvIALELDITSKESIKELIESYLEKFGRI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  78 DFVLANAGIaedTAMFFASHPTGIPPPPDMTGLtDINFTGAIYTSYLAMHYFRRSpekTKGNrhLIIMSSIGGL------ 151
Cdd:cd08930  82 DILINNAYP---SPKVWGSRFEEFPYEQWNEVL-NVNLGGAFLCSQAFIKLFKKQ---GKGS--IINIASIYGViapdfr 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 83775806 152 -YPCAHT--PV-YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVL 194
Cdd:cd08930 153 iYENTQMysPVeYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGIL 199
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 5-195 3.24e-15

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: 73.02  E-value: 3.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   5 ALITGGTSGMGLDVAQELDKTGLWKVHIIgsnanRGEEAAASL---------RNTIFHQVDVTKYEQqgaAFDKIFNEEK 75
Cdd:cd05356   4 AVVTGATDGIGKAYAEELAKRGFNVILIS-----RTQEKLDAVakeieekygVETKTIAADFSAGDD---IYERIEKELE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  76 RLD--FVLANAGIAEDTAMFFASHPTGippppDMTGLTDINFTGAIYTSYLAMHYFRrspEKTKGnrhLII-MSSIGGLY 152
Cdd:cd05356  76 GLDigILVNNVGISHSIPEYFLETPED-----ELQDIINVNVMATLKMTRLILPGMV---KRKKG---AIVnISSFAGLI 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 83775806 153 PCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT 195
Cdd:cd05356 145 PTPLLATYSASKAFLDFFSRALYEEYKSQGIDVQSLLPYLVAT 187
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-224 3.26e-15

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 73.18  E-value: 3.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlwkVHI--IGSNANRGEEAAASLRNT----IFHQVDVTKYEQQGAAFDKIFNEEKRL 77
Cdd:PRK07666   9 NALITGAGRGIGRAVAIALAKEG---VNVglLARTEENLKAVAEEVEAYgvkvVIATADVSDYEEVTAAIEQLKNELGSI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   78 DFVLANAGIAEdtamfFASHPTgiPPPPDMTGLTDINFTGAIYTSYLAMHYFRrspEKTKGnrHLIIMSSIGGLYPCAHT 157
Cdd:PRK07666  86 DILINNAGISK-----FGKFLE--LDPAEWEKIIQVNLMGVYYATRAVLPSMI---ERQSG--DIINISSTAGQKGAAVT 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83775806  158 PVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTE-LQAFFPEKiVMKMSDVTNVV---LKL 224
Cdd:PRK07666 154 SAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDLgLTDGNPDK-VMQPEDLAEFIvaqLKL 223
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
4-211 4.16e-15

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 72.74  E-value: 4.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLWKVHIIGSNANRG----EEAAASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK12938   5 IAYVTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRRvkwlEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVGEIDV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAEDTAMFFASHPtgippppDMTGLTDINFTGAIYTSYLAMHYFrrspeKTKGNRHLIIMSSIGGLYPCAHTPV 159
Cdd:PRK12938  85 LVNNAGITRDVVFRKMTRE-------DWTAVIDTNLTSLFNVTKQVIDGM-----VERGWGRIINISSVNGQKGQFGQTN 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 83775806  160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTELQAFFPEKIV 211
Cdd:PRK12938 153 YSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTD-MVKAIRPDVLEKIV 203
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 4-201 6.16e-15

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 72.74  E-value: 6.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEaaaslRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLAN 83
Cdd:PRK06171  11 IIIVTGGSSGIGLAIVKELLANGA-NVVNADIHGGDGQH-----ENYQFVPTDVSSAEEVNHTVAEIIEKFGRIDGLVNN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   84 AGIAEDTAMFFASHPTG--IPPPPDMTGLTDINFTGAIYTSYLAMHYFrrspekTKGNRHLII-MSSIGGLYPCAHTPVY 160
Cdd:PRK06171  85 AGINIPRLLVDEKDPAGkyELNEAAFDKMFNINQKGVFLMSQAVARQM------VKQHDGVIVnMSSEAGLEGSEGQSCY 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 83775806  161 SATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVV-LTPLMTTE 201
Cdd:PRK06171 159 AATKAALNSFTRSWAKELGKHNIRVVGVAPGILeATGLRTPE 200
PLN02253 PLN02253
xanthoxin dehydrogenase
 4-197 1.00e-14

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 72.16  E-value: 1.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASL---RNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFV 80
Cdd:PLN02253  20 VALVTGGATGIGESIVRLFHKHGA-KVCIVDLQDDLGQNVCDSLggePNVCFFHCDVTVEDDVSRAVDFTVDKFGTLDIM 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   81 LANAGIaedtamffashpTGiPPPPDMTGLT--------DINFTGAiytsYLAMHYFRRS--PEKtKGNrhlIIM----- 145
Cdd:PLN02253  99 VNNAGL------------TG-PPCPDIRNVElsefekvfDVNVKGV----FLGMKHAARImiPLK-KGS---IVSlcsva 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 83775806  146 SSIGGLYPCAhtpvYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:PLN02253 158 SAIGGLGPHA----YTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTAL 205
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 4-197 1.00e-14

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


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 72.18  E-value: 1.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIigsnANRGEEAAASLR---------NTIFHQVDVTKYEQQGAAFDKIFNEE 74
Cdd:cd08933  11 VVIVTGGSRGIGRGIVRAFVENGA-KVVF----CARGEAAGQALEselnragpgSCKFVPCDVTKEEDIKTLISVTVERF 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  75 KRLDFVLANAGIaedtamffasHPTgiPPPPDMTG------LTDINFTGAIYTSYLAMHYFRrspeKTKGNrhLIIMSSI 148
Cdd:cd08933  86 GRIDCLVNNAGW----------HPP--HQTTDETSaqefrdLLNLNLISYFLASKYALPHLR----KSQGN--IINLSSL 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 83775806 149 GGLYPCAHTPVYSATKHGLVGFTRSVGkrlLDE---GVKVNTVCPGVVLTPL 197
Cdd:cd08933 148 VGSIGQKQAAPYVATKGAITAMTKALA---VDEsryGVRVNCISPGNIWTPL 196
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 4-201 1.02e-14

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: 72.04  E-value: 1.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlwkVHIIGS--NANRGEEAAASLRN---TIFHQVDVTKYEQQGAAFDKIFNEEKRLD 78
Cdd:cd08943   3 VALVTGGASGIGLAIAKRLAAEG---AAVVVAdiDPEIAEKVAEAAQGgprALGVQCDVTSEAQVQSAFEQAVLEFGGLD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  79 FVLANAGIAedtamffASHPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRspEKTKGNrhLIIMSSIGGLYPCAHTP 158
Cdd:cd08943  80 IVVSNAGIA-------TSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKS--QGIGGN--IVFNASKNAVAPGPNAA 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 83775806 159 VYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTE 201
Cdd:cd08943 149 AYSAAKAAEAHLARCLALEGGEDGIRVNTVNPDAVFRGSKIWE 191
PRK06398 PRK06398
aldose dehydrogenase; Validated
 4-198 1.20e-14

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 71.79  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlwkVHIIGSNANRGEEAAASlrntiFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLAN 83
Cdd:PRK06398   8 VAIVTGGSQGIGKAVVNRLKEEG---SNVINFDIKEPSYNDVD-----YFKVDVSNKEQVIKGIDYVISKYGRIDILVNN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   84 AGIAEdtamFFASHPTgipPPPDMTGLTDINFTGAIYTSYLAMHYFRRSpektkGNRHLIIMSSIGGLYPCAHTPVYSAT 163
Cdd:PRK06398  80 AGIES----YGAIHAV---EEDEWDRIINVNVNGIFLMSKYTIPYMLKQ-----DKGVIINIASVQSFAVTRNAAAYVTS 147

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 83775806  164 KHGLVGFTRSVGkrlLDEG--VKVNTVCPGVVLTPLM 198
Cdd:PRK06398 148 KHAVLGLTRSIA---VDYAptIRCVAVCPGSIRTPLL 181
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 4-226 1.23e-14

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 71.60  E-value: 1.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLR------NTIFHQVDVTKYEQQGAAFDKIFNEEKRL 77
Cdd:PRK12384   4 VAVVIGGGQTLGAFLCHGLAEEG-YRVAVADINSEKAANVAQEINaeygegMAYGFGADATSEQSVLALSRGVDEIFGRV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   78 DFVLANAGIAedTAMFFASHPTGippppDMTGLTDINFTGaiYtsYLAMHYFRRS--PEKTKGNrhLIIMSSIGGLYPCA 155
Cdd:PRK12384  83 DLLVYNAGIA--KAAFITDFQLG-----DFDRSLQVNLVG--Y--FLCAREFSRLmiRDGIQGR--IIQINSKSGKVGSK 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  156 HTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLM---------------TTELQAFFPEKIVMK----MSD 216
Cdd:PRK12384 150 HNSGYSAAKFGGVGLTQSLALDLAEYGITVHSLMLGNLLKSPMfqsllpqyakklgikPDEVEQYYIDKVPLKrgcdYQD 229

                        250
                 ....*....|
gi 83775806  217 VTNVVLKLIS 226
Cdd:PRK12384 230 VLNMLLFYAS 239
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 4-227 1.28e-14

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 71.58  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASL-RNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLA 82
Cdd:PRK08265   8 VAIVTGGATLIGAAVARALVAAGA-RVAIVDIDADNGAAVAASLgERARFIATDITDDAAIERAVATVVARFGRVDILVN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   83 NA------GIAEDTAMFFAShptgippppdmtglTDINFTGAiytsylAMHYFRRSPEKTKGNRHLIIMSSIGGLYPCAH 156
Cdd:PRK08265  87 LActylddGLASSRADWLAA--------------LDVNLVSA------AMLAQAAHPHLARGGGAIVNFTSISAKFAQTG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  157 TPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLM----------TTELQA-FFPEKIVMKMSDVTNVVLKLI 225
Cdd:PRK08265 147 RWLYPASKAAIRQLTRSMAMDLAPDGIRVNSVSPGWTWSRVMdelsggdrakADRVAApFHLLGRVGDPEEVAQVVAFLC 226


                 ..
gi 83775806  226 SG 227
Cdd:PRK08265 227 SD 228
PRK06914 PRK06914
SDR family oxidoreductase;
4-205 1.43e-14

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 71.98  E-value: 1.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwkvHIIGSNanRGEEAAASLRNTI----------FHQVDVTKyEQQGAAFDKIFNE 73
Cdd:PRK06914   5 IAIVTGASSGFGLLTTLELAKKGY---LVIATM--RNPEKQENLLSQAtqlnlqqnikVQQLDVTD-QNSIHNFQLVLKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   74 EKRLDFVLANAGIA-----EDTAM------FfashptgippppdmtgltDINFTGAIYTSYLAMHYFRrspeKTKGNrHL 142
Cdd:PRK06914  79 IGRIDLLVNNAGYAnggfvEEIPVeeyrkqF------------------ETNVFGAISVTQAVLPYMR----KQKSG-KI 135

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83775806  143 IIMSSIGGL--YPcAHTPvYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAF 205
Cdd:PRK06914 136 INISSISGRvgFP-GLSP-YVSSKYALEGFSESLRLELKPFGIDVALIEPGSYNTNIWEVGKQLA 198
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
4-206 1.92e-14

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 71.21  E-value: 1.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR-NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLA 82
Cdd:PRK07067   8 VALLTGAASGIGEAVAERYLAEGA-RVVIADIKPARARLAALEIGpAAIAVSLDVTRQDSIDRIVAAAVERFGGIDILFN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   83 NAGIAEdtamffashptgIPPPPDMT-----GLTDINFTGAIYTSYLAMhyfRRSPEKTKGNRhLIIMSSIGGLYPCAHT 157
Cdd:PRK07067  87 NAALFD------------MAPILDISrdsydRLFAVNVKGLFFLMQAVA---RHMVEQGRGGK-IINMASQAGRRGEALV 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 83775806  158 PVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTELQAFF 206
Cdd:PRK07067 151 SHYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTP-MWDQVDALF 198
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 4-202 2.37e-14

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: 70.88  E-value: 2.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAA-SLRNTIFH---------------QVDVTKYEQQGAAF 67
Cdd:cd05338   5 VAFVTGASRGIGRAIALRLAKAG-ATVVVAAKTASEGDNGSAkSLPGTIEEtaeeieaaggqalpiVVDVRDEDQVRALV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  68 DKIFNEEKRLDFVLANAG-----IAEDTamffashptgippPPDMTGLT-DINFTGAIYTSYLAMHYFRRSpektkGNRH 141
Cdd:cd05338  84 EATVDQFGRLDILVNNAGaiwlsLVEDT-------------PAKRFDLMqRVNLRGTYLLSQAALPHMVKA-----GQGH 145

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83775806 142 LIIMSSIGGLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTEL 202
Cdd:cd05338 146 ILNISPPLSLRPARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIETPAATEL 206
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 5-195 2.47e-14

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: 70.23  E-value: 2.47e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   5 ALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLRNTIFHQV-DVTKYEQQGAAFDKIFNEEKRLDFVLAN 83
Cdd:cd08929   3 ALVTGASRGIGEATARLLHAEG-YRVGICARDEARLAAAAAQELEGVLGLAgDVRDEADVRRAVDAMEEAFGGLDALVNN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  84 AGIAedtamffASHPTGIPPPPDMTGLTDINFTGAIYTSYLAMhyfrrSPEKTKGNRHLIIMSSIGGLYPCAHTPVYSAT 163
Cdd:cd08929  82 AGVG-------VMKPVEELTPEEWRLVLDTNLTGAFYCIHKAA-----PALLRRGGGTIVNVGSLAGKNAFKGGAAYNAS 149

                       170       180       190
                ....*....|....*....|....*....|..
gi 83775806 164 KHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT 195
Cdd:cd08929 150 KFGLLGLSEAAMLDLREANIRVVNVMPGSVDT 181
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 5-207 2.65e-14

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


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 70.46  E-value: 2.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   5 ALITGGTSGMGLDVAQELDKTGlWKVHIigsNANRGEEAAASLRNTIFH--------QVDVTKYEQQGAAFDKIFNEEKR 76
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERG-ADVVI---NYRKSKDAAAEVAAEIEElggkavvvRADVSQPQDVEEMFAAVKERFGR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  77 LDFVLANAgiaedtamffasHPTGIPPPPDMT-----GLTDINFTGAIYTSYLAMHYFRRspektKGNRHLIIMSSIGGL 151
Cdd:cd05359  77 LDVLVSNA------------AAGAFRPLSELTpahwdAKMNTNLKALVHCAQQAAKLMRE-----RGGGRIVAISSLGSI 139

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 83775806 152 YPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLtplmtTELQAFFP 207
Cdd:cd05359 140 RALPNYLAVGTAKAALEALVRYLAVELGPRGIRVNAVSPGVID-----TDALAHFP 190
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 5-199 2.72e-14

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 71.14  E-value: 2.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTIF--HQV--DVTKYEQQGAAFDKIFNEEKRLDFV 80
Cdd:PRK05876   9 AVITGGASGIGLATGTEFARRGA-RVVLGDVDKPGLRQAVNHLRAEGFdvHGVmcDVRHREEVTHLADEAFRLLGHVDVV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   81 LANAGIAEDTAMFFASHPtgippppDMTGLTDINFTGAIYTsylAMHYFRRSPEKTKGNrHLIIMSSIGGLYPCAHTPVY 160
Cdd:PRK05876  88 FSNAGIVVGGPIVEMTHD-------DWRWVIDVDLWGSIHT---VEAFLPRLLEQGTGG-HVVFTASFAGLVPNAGLGAY 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 83775806  161 SATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMT 199
Cdd:PRK05876 157 GVAKYGVVGLAETLAREVTADGIGVSVLCPMVVETNLVA 195
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 6-191 3.07e-14

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 70.71  E-value: 3.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    6 LITGGTSGMGLDVAQELDKTGlWKVhiIGSNanRGEEAAASLRNTIFHQV-----DVTKYEQQGAAFDKIFNEEKRLDFV 80
Cdd:PRK06180   8 LITGVSSGFGRALAQAALAAG-HRV--VGTV--RSEAARADFEALHPDRAlarllDVTDFDAIDAVVADAEATFGPIDVL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   81 LANAGIAEDTAMFFAshptgipPPPDMTGLTDINFTGAIYTSYLAMHYFRrspEKTKGnrHLIIMSSIGGLYPCAHTPVY 160
Cdd:PRK06180  83 VNNAGYGHEGAIEES-------PLAEMRRQFEVNVFGAVAMTKAVLPGMR---ARRRG--HIVNITSMGGLITMPGIGYY 150

                        170       180       190
                 ....*....|....*....|....*....|.
gi 83775806  161 SATKHGLVGFTRSVGKRLLDEGVKVNTVCPG 191
Cdd:PRK06180 151 CGSKFALEGISESLAKEVAPFGIHVTAVEPG 181
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 4-205 3.70e-14

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


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 70.21  E-value: 3.70e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlwkVHIIGSNANRG--EEAAASL-RNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFV 80
Cdd:cd08944   5 VAIVTGAGAGIGAACAARLAREG---ARVVVADIDGGaaQAVVAQIaGGALALRVDVTDEQQVAALFERAVEEFGGLDLL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  81 LANAGIAEdtamffASHPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRSpektkGNRHLIIMSSIGGLYPCAHTPVY 160
Cdd:cd08944  82 VNNAGAMH------LTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIAR-----GGGSIVNLSSIAGQSGDPGYGAY 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 83775806 161 SATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAF 205
Cdd:cd08944 151 GASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGF 195
PRK07856 PRK07856
SDR family oxidoreductase;
4-195 1.04e-13

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 69.19  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGsnanRGEEAAASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLAN 83
Cdd:PRK07856   8 VVLVTGGTRGIGAGIARAFLAAG-ATVVVCG----RRAPETVDGRPAEFHAADVRDPDQVAALVDAIVERHGRLDVLVNN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   84 AG------IAEDTAMFFAShptgippppdmtgLTDINFTGAIYTSYLAMHYFRRSPektkGNRHLIIMSSIGGLYPCAHT 157
Cdd:PRK07856  83 AGgspyalAAEASPRFHEK-------------IVELNLLAPLLVAQAANAVMQQQP----GGGSIVNIGSVSGRRPSPGT 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 83775806  158 PVYSATKHGLVGFTRSvgkrLLDE---GVKVNTVCPGVVLT 195
Cdd:PRK07856 146 AAYGAAKAGLLNLTRS----LAVEwapKVRVNAVVVGLVRT 182
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 4-197 1.52e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 68.59  E-value: 1.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNAN-----RGEEAAASLRntifhqVDVTKYEQQGAAFDkifnEEKRLD 78
Cdd:PRK07060  11 SVLVTGASSGIGRACAVALAQRGA-RVVAAARNAAaldrlAGETGCEPLR------LDVGDDAAIRAALA----AAGAFD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   79 FVLANAGIAEdtamffashptgIPPPPDMTG-----LTDINFTGAIYTsylAMHYFRRSPEKTKGNRhLIIMSSIGGLYP 153
Cdd:PRK07060  80 GLVNCAGIAS------------LESALDMTAegfdrVMAVNARGAALV---ARHVARAMIAAGRGGS-IVNVSSQAALVG 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 83775806  154 CAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:PRK07060 144 LPDHLAYCASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPM 187
PRK06138 PRK06138
SDR family oxidoreductase;
4-199 2.19e-13

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 68.25  E-value: 2.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR---NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFV 80
Cdd:PRK06138   7 VAIVTGAGSGIGRATAKLFAREGA-RVVVADRDAEAAERVAAAIAaggRAFARQGDVGSAEAVEALVDFVAARWGRLDVL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   81 LANAGIA-----EDTamffashptgipPPPDMTGLTDINFTGAIYTSYLAMHYFRRspektKGNRHLIIMSSIGGLYPCA 155
Cdd:PRK06138  86 VNNAGFGcggtvVTT------------DEADWDAVMRVNVGGVFLWAKYAIPIMQR-----QGGGSIVNTASQLALAGGR 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 83775806  156 HTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMT 199
Cdd:PRK06138 149 GRAAYVASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFR 192
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 4-241 2.92e-13

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: 67.30  E-value: 2.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlwkvHIIGSNANRGEEAAASLRNTIFH--------QVDVTKYEQQGAAFDKIFNEEK 75
Cdd:cd05357   2 VALVTGAAKRIGRAIAEALAAEG----YRVVVHYNRSEAEAQRLKDELNAlrnsavlvQADLSDFAACADLVAAAFRAFG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  76 RLDFVLANAGIaedtamFFAShPTGIPPPPDMTGLTDINftgAIYTSYLAMHYFRRSPEKTKGNrhlII-MSSIGGLYPC 154
Cdd:cd05357  78 RCDVLVNNASA------FYPT-PLGQGSEDAWAELFGIN---LKAPYLLIQAFARRLAGSRNGS---IInIIDAMTDRPL 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806 155 AHTPVYSATKHGLVGFTRSVGKRLLDEgVKVNTVCPGVVLTPL-MTTELQAFFPEKIVMKM----SDVTNVVLKLISGTE 229
Cdd:cd05357 145 TGYFAYCMSKAALEGLTRSAALELAPN-IRVNGIAPGLILLPEdMDAEYRENALRKVPLKRrpsaEEIADAVIFLLDSNY 223

                       250
                ....*....|..
gi 83775806 230 VTdsnGTSVPSD 241
Cdd:cd05357 224 IT---GQIIKVD 232
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 3-197 4.63e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 67.75  E-value: 4.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    3 LVALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASL-----RNTIFHQVDVTKYEQQGAAFDKIFNEEKRL 77
Cdd:PRK06701  47 KVALITGGDSGIGRAVAVLFAKEGA-DIAIVYLDEHEDANETKQRvekegVKCLLIPGDVSDEAFCKDAVEETVRELGRL 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   78 DFVLANAGIAEdtamffashptgipPPPDMTGLTD--------INFTGAIYTSYLAMHYFRRSPEktkgnrhlIIM-SSI 148
Cdd:PRK06701 126 DILVNNAAFQY--------------PQQSLEDITAeqldktfkTNIYSYFHMTKAALPHLKQGSA--------IINtGSI 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 83775806  149 GGLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:PRK06701 184 TGYEGNETLIDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPL 232
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 4-197 5.36e-13

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: 66.99  E-value: 5.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLRNTIFHQV-DVTKYEQQGAAFDKIFNEEKRLDFVLA 82
Cdd:cd05348   6 VALITGGGSGLGRALVERFVAEG-AKVAVLDRSAEKVAELRADFGDAVVGVEgDVRSLADNERAVARCVERFGKLDCFIG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  83 NAGIAEdtamffasHPTGIPPPPDMT------GLTDINFTGAIYTSYLAMhyfrrsPEKTKGNRHLIIMSSIGGLYPCAH 156
Cdd:cd05348  85 NAGIWD--------YSTSLVDIPEEKldeafdELFHINVKGYILGAKAAL------PALYATEGSVIFTVSNAGFYPGGG 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 83775806 157 TPVYSATKHGLVGFTRSVGKRLLDEgVKVNTVCPGVVLTPL 197
Cdd:cd05348 151 GPLYTASKHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTDL 190
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 5-239 9.44e-13

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: 66.17  E-value: 9.44e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   5 ALITGGTSGMGLDVAQELDKTGlwKVHIIGS--NANRGEEAAA---SLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARG--NNTVIATcrDPSAATELAAlgaSHSRLHILELDVTDEIAESAEAVAERLGDAGLDV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGIAedtamffasHPTGI---PPPPDMTGLTDINFTGAIytsyLAMHYFRrsPEKTKGNRHLII-----MSSI--- 148
Cdd:cd05325  79 LINNAGIL---------HSYGPaseVDSEDLLEVFQVNVLGPL----LLTQAFL--PLLLKGARAKIInissrVGSIgdn 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806 149 --GGLYPcahtpvYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTELQA----FFPEKIVMKMsdvtnvvL 222
Cdd:cd05325 144 tsGGWYS------YRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTD-MGGPFAKnkgpITPEESVAGL-------L 209

                       250       260
                ....*....|....*....|...
gi 83775806 223 KLISGTEVTDS------NGTSVP 239
Cdd:cd05325 210 KVIDNLNEEDSgkfldyDGTEIP 232
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 4-210 1.14e-12

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


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 66.16  E-value: 1.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHII-----GSNANRGEEAA-ASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRL 77
Cdd:cd05355  28 KALITGGDSGIGRAVAIAFAREGA-DVAINylpeeEDDAEETKKLIeEEGRKCLLIPGDLGDESFCRDLVKEVVKEFGKL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  78 DFVLANAgiaedtAMFFAShptgipppPDMTGLTDINFTGAIYTSYLAMHYFRRS--PEKTKGNRhLIIMSSIGGLYPCA 155
Cdd:cd05355 107 DILVNNA------AYQHPQ--------ESIEDITTEQLEKTFRTNIFSMFYLTKAalPHLKKGSS-IINTTSVTAYKGSP 171

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 83775806 156 HTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTelqAFFPEKI 210
Cdd:cd05355 172 HLLDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIPS---SFPEEKV 223
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 4-195 1.69e-12

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 66.08  E-value: 1.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK08277  12 VAVITGGGGVLGGAMAKELARAGA-KVAILDRNQEKAEAVVAEIKaaggEALAVKADVLDKESLEQARQQILEDFGPCDI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAG--------------IAEDTAMFFASHPTGIppppdmTGLTDINFTGAIYTSylaMHYFRRSPEKTKGNrhlII- 144
Cdd:PRK08277  91 LINGAGgnhpkattdnefheLIEPTKTFFDLDEEGF------EFVFDLNLLGTLLPT---QVFAKDMVGRKGGN---IIn 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 83775806  145 MSSIGGLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT 195
Cdd:PRK08277 159 ISSMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLT 209
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
4-216 2.31e-12

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 65.21  E-value: 2.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLW--------KVHIIGSN-ANRGEEAAAslrntifHQVDVTKYEQQGAAFDKIFNEE 74
Cdd:PRK08226   8 TALITGALQGIGEGIARVFARHGANlilldispEIEKLADElCGRGHRCTA-------VVADVRDPASVAAAIKRAKEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   75 KRLDFVLANAGIAEdTAMFFAShptgippPPDMTGLT-DINFTGAIYTSYLAMHYFRRspektKGNRHLIIMSSI-GGLY 152
Cdd:PRK08226  81 GRIDILVNNAGVCR-LGSFLDM-------SDEDRDFHiDINIKGVWNVTKAVLPEMIA-----RKDGRIVMMSSVtGDMV 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83775806  153 PCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL---MTTELQAFFPEKIVMKMSD 216
Cdd:PRK08226 148 ADPGETAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMaesIARQSNPEDPESVLTEMAK 214
PRK12743 PRK12743
SDR family oxidoreductase;
1-199 2.36e-12

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 65.05  E-value: 2.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    1 MVLVALITGGTSGMGLDVAQELDKTGlwkvHIIGSNANRGEEAA--------ASLRNTIFHQVDVTKYEQQGAAFDKIFN 72
Cdd:PRK12743   1 MAQVAIVTASDSGIGKACALLLAQQG----FDIGITWHSDEEGAketaeevrSHGVRAEIRQLDLSDLPEGAQALDKLIQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   73 EEKRLDFVLANAGIAEDTAMffashptgipppPDMTGLT-----DINFTGAIYTSYLAMHYFRRSPEktkGNRhLIIMSS 147
Cdd:PRK12743  77 RLGRIDVLVNNAGAMTKAPF------------LDMDFDEwrkifTVDVDGAFLCSQIAARHMVKQGQ---GGR-IINITS 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 83775806  148 IGGLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMT 199
Cdd:PRK12743 141 VHEHTPLPGASAYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIATP-MN 191
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 4-197 3.37e-12

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 64.76  E-value: 3.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLWKVHIIGSNANRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK12937   7 VAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADELVAEIEaaggRAIAVQADVADAAAVTRLFDAAETAFGRIDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIaedtaMFFASHPTGIPPPPDMTglTDINFTGAIYTSYLAMHYFRRspektkGNRHLIIMSSIGGLYPCAHTPv 159
Cdd:PRK12937  87 LVNNAGV-----MPLGTIADFDLEDFDRT--IATNLRGAFVVLREAARHLGQ------GGRIINLSTSVIALPLPGYGP- 152

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 83775806  160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:PRK12937 153 YAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL 190
PRK07074 PRK07074
SDR family oxidoreductase;
4-226 3.89e-12

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 64.79  E-value: 3.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTIFHQV--DVTKYEQQGAAFDKIFNEEKRLDFVL 81
Cdd:PRK07074   4 TALVTGAAGGIGQALARRFLAAGD-RVLALDIDAAALAAFADALGDARFVPVacDLTDAASLAAALANAAAERGPVDVLV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   82 ANAGIAEDTAMffasHPTgipPPPDMTGLTDINFTGAiytsYLAMHYFRRSP-EKTKGNrhLIIMSSIGGLYPCAHtPVY 160
Cdd:PRK07074  83 ANAGAARAASL----HDT---TPASWRADNALNLEAA----YLCVEAVLEGMlKRSRGA--VVNIGSVNGMAALGH-PAY 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83775806  161 SATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT----------PLMTTELQAFFPEKIVMKMSDVTNVVLKLIS 226
Cdd:PRK07074 149 SAAKAGLIHYTKLLAVEYGRFGIRANAVAPGTVKTqawearvaanPQVFEELKKWYPLQDFATPDDVANAVLFLAS 224
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 4-197 4.18e-12

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 64.75  E-value: 4.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLWKVHIIGSNANRGEEAAASLRNT----IFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK08936   9 VVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEANDVAEEIKKAggeaIAVKGDVTVESDVVNLIQTAVKEFGTLDV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAEdtamffaSHPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRspEKTKGNrhLIIMSSIGGLYPCAHTPV 159
Cdd:PRK08936  89 MINNAGIEN-------AVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVE--HDIKGN--IINMSSVHEQIPWPLFVH 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 83775806  160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:PRK08936 158 YAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPI 195
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 4-196 5.05e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 64.26  E-value: 5.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLWKVHIIGSNANRGEEAAASLRNT----IFHQVDVTKYEQQGAAFDKIFNEEKRLDf 79
Cdd:PRK06198   8 VALVTGGTQGLGAAIARAFAERGAAGLVICGRNAEKGEAQAAELEALgakaVFVQADLSDVEDCRRVVAAADEAFGRLD- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAEDTAMFFASHPTgippppdmtgLTDINFTGAIYTSYLAM-----HYFRRSPEKTKGNrhLIIMSSIGG---L 151
Cdd:PRK06198  87 ALVNAAGLTDRGTILDTSPE----------LFDRHFAVNVRAPFFLMqeaikLMRRRKAEGTIVN--IGSMSAHGGqpfL 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 83775806  152 YPcahtpvYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTP 196
Cdd:PRK06198 155 AA------YCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATE 193
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-195 5.70e-12

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 64.37  E-value: 5.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlwkVHIIGSNANRGEEAAASL-----RNTIFHQVDVTKYEQQGAAFDKIFNEEKRLD 78
Cdd:PRK06935  17 VAIVTGGNTGLGQGYAVALAKAG---ADIIITTHGTNWDETRRLiekegRKVTFVQVDLTKPESAEKVVKEALEEFGKID 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   79 FVLANAG-IAEDTAMFFASHptgippppDMTGLTDINFTgAIYtsYLAMHYFRRSPEKTKGNrhlII-----MSSIGGLY 152
Cdd:PRK06935  94 ILVNNAGtIRRAPLLEYKDE--------DWNAVMDINLN-SVY--HLSQAVAKVMAKQGSGK---IIniasmLSFQGGKF 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 83775806  153 pcahTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT 195
Cdd:PRK06935 160 ----VPAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKT 198
PRK07832 PRK07832
SDR family oxidoreductase;
5-200 6.14e-12

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 64.29  E-value: 6.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR----NTIFHQ-VDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGA-ELFLTDRDADGLAQTVADARalggTVPEHRaLDISDYDAVAAFAADIHAAHGSMDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAEDTAMFFASHPtgippppDMTGLTDINFTGAIYTsylaMHYFrrSPEKTKGNR--HLIIMSSIGGLYPCAHT 157
Cdd:PRK07832  82 VMNIAGISAWGTVDRLTHE-------QWRRMVDVNLMGPIHV----IETF--VPPMVAAGRggHLVNVSSAAGLVALPWH 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 83775806  158 PVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTT 200
Cdd:PRK07832 149 AAYSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVNT 191
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 4-204 6.52e-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: 6.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTIfHQVDVTKYEQqgaaFDKIFNEEKRLDFVLAN 83
Cdd:cd05368   4 VALITAAAQGIGRAIALAFAREGA-NVIATDINEEKLKELERGPGITT-RVLDVTDKEQ----VAALAKEEGRIDVLFNC 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  84 AGiaedtamfFASHPTGIppppDMT-GLTDINFTGAIYTSYLAMHYFRRSPEKTKGNRhLIIMSSIGG-LYPCAHTPVYS 161
Cdd:cd05368  78 AG--------FVHHGSIL----DCEdDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGS-IINMSSVASsIKGVPNRFVYS 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 83775806 162 ATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQA 204
Cdd:cd05368 145 TTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLEERIQA 187
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 4-193 9.12e-12

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: 63.63  E-value: 9.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlWKVHI-IGSNANRGEEAAASL-RNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVL 81
Cdd:cd05349   2 VVLVTGASRGLGAAIARSFAREG-ARVVVnYYRSTESAEAVAAEAgERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTIV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  82 ANAGIAedtamfFASHPTGIPPPPDMTG---LTDINFT--GAIYTSYLAMHYFRrspeKTKGNRHLIIMSSIgglypcAH 156
Cdd:cd05349  81 NNALID------FPFDPDQRKTFDTIDWedyQQQLEGAvkGALNLLQAVLPDFK----ERGSGRVINIGTNL------FQ 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 83775806 157 TPV-----YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVV 193
Cdd:cd05349 145 NPVvpyhdYTTAKAALLGFTRNMAKELGPYGITVNMVSGGLL 186
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 4-197 1.00e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 63.52  E-value: 1.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANrGEEAAASLR--NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVL 81
Cdd:PRK06841  17 VAVVTGGASGIGHAIAELFAAKGA-RVALLDRSED-VAEVAAQLLggNAKGLVCDVSDSQSVEAAVAAVISAFGRIDILV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   82 ANAGIAEdtamffashptgIPPPPDMT-----GLTDINFTGaiytSYLAMHYFRRSPEKTKGNRhLIIMSSIGGLYPCAH 156
Cdd:PRK06841  95 NSAGVAL------------LAPAEDVSeedwdKTIDINLKG----SFLMAQAVGRHMIAAGGGK-IVNLASQAGVVALER 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 83775806  157 TPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:PRK06841 158 HVAYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTEL 198
PRK08628 PRK08628
SDR family oxidoreductase;
4-205 1.16e-11

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 63.44  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLWKVhIIGSNAnRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK08628   9 VVIVTGGASGIGAAISLRLAEEGAIPV-IFGRSA-PDDEFAEELRalqpRAEFVQVDLTDDAQCRDAVEQTVAKFGRIDG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAedtamffashptgippppDMTGLTDIN--FTGAIY---TSYLAM-HYFRRSPEKTKGNrhLIIMSSIGGLYP 153
Cdd:PRK08628  87 LVNNAGVN------------------DGVGLEAGReaFVASLErnlIHYYVMaHYCLPHLKASRGA--IVNISSKTALTG 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 83775806  154 CAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAF 205
Cdd:PRK08628 147 QGGTSGYAAAKGAQLALTREWAVALAKDGVRVNAVIPAEVMTPLYENWIATF 198
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
4-193 1.21e-11

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 64.48  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlwkVHIIGS--NANRGEEAAASLRNT---IFHQVDVTKYEQQGAAFDKIFNEEKRLD 78
Cdd:PRK08324 424 VALVTGAAGGIGKATAKRLAAEG---ACVVLAdlDEEAAEAAAAELGGPdraLGVACDVTDEAAVQAAFEEAALAFGGVD 500

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   79 FVLANAGIAedtamffASHPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRspEKTKGNrhLIIMSSIGGLYPCAHTP 158
Cdd:PRK08324 501 IVVSNAGIA-------ISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKA--QGLGGS--IVFIASKNAVNPGPNFG 569

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 83775806  159 VYSATKHGLVGFTRSVGKRLLDEGVKVNTVCP-GVV 193
Cdd:PRK08324 570 AYGAAKAAELHLVRQLALELGPDGIRVNGVNPdAVV 605
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 4-218 1.79e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 62.66  E-value: 1.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASL----RNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK08213  14 TALVTGGSRGLGLQIAEALGEAGA-RVVLSARKAEELEEAAAHLealgIDALWIAADVADEADIERLAEETLERFGHVDI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGI-----AEDtamffasHPTgipppPDMTGLTDINFTGaiyTSYLAMHYFRRSPEKTKGNRhLIIMSSIGGL--- 151
Cdd:PRK08213  93 LVNNAGAtwgapAED-------HPV-----EAWDKVMNLNVRG---LFLLSQAVAKRSMIPRGYGR-IINVASVAGLggn 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83775806  152 YP-CAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGvvltplmttelqaFFPEkivmKMSDVT 218
Cdd:PRK08213 157 PPeVMDTIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPG-------------FFPT----KMTRGT 207
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 4-214 1.95e-11

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: 62.30  E-value: 1.95e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLW-KVHIIGSNANRGEEAAASLRNT---IFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSPsVVVLLARSEEPLQELKEELRPGlrvTTVKADLSDAAGVEQLLEAIRKLDGERDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGIAEDTA-MFFAShptgippPPDMTGLTDINFTGAIYTSYLAMhyfrRSPEKTKGNRHLIIMSSIGGLYPCAHTP 158
Cdd:cd05367  81 LINNAGSLGPVSkIEFID-------LDELQKYFDLNLTSPVCLTSTLL----RAFKKRGLKKTVVNVSSGAAVNPFKGWG 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 83775806 159 VYSATKHGLVGFTRSVGKRLldEGVKVNTVCPGVVLTPlMTTELQAFFPEKIVMKM 214
Cdd:cd05367 150 LYCSSKAARDMFFRVLAAEE--PDVRVLSYAPGVVDTD-MQREIRETSADPETRSR 202
PRK07201 PRK07201
SDR family oxidoreductase;
4-197 2.50e-11

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 63.82  E-value: 2.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK07201 373 VVLITGASSGIGRATAIKVAEAGA-TVFLVARNGEALDELVAEIRakggTAHAYTCDLTDSAAVDHTVKDILAEHGHVDY 451

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAG------IAEDTAMFfasHptgippppDMTGLTDINFTGAIytsYLAMHYFRRSPEKTKGnrHLIIMSSIGGLyp 153
Cdd:PRK07201 452 LVNNAGrsirrsVENSTDRF---H--------DYERTMAVNYFGAV---RLILGLLPHMRERRFG--HVVNVSSIGVQ-- 513

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 83775806  154 cAHTPVYSA---TKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:PRK07201 514 -TNAPRFSAyvaSKAALDAFSDVAASETLSDGITFTTIHMPLVRTPM 559
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 4-199 2.50e-11

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: 62.46  E-value: 2.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIG-----SNANRGEEAAASLRNTIFHQVDVTKYEQQGAAFDKIFNEEK-RL 77
Cdd:cd09763   5 IALVTGASRGIGRGIALQLGEAGA-TVYITGrtilpQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQgRL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  78 DfVLANAGIAEDTAMFFASHPTGIPPPPDMtgLTDINFTGaIYTSYLAMHYFRRSpEKTKGNRHLIIMSSIGGL-YpcAH 156
Cdd:cd09763  84 D-ILVNNAYAAVQLILVGVAKPFWEEPPTI--WDDINNVG-LRAHYACSVYAAPL-MVKAGKGLIVIISSTGGLeY--LF 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 83775806 157 TPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMT 199
Cdd:cd09763 157 NVAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVL 199
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 4-218 2.92e-11

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


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 62.09  E-value: 2.92e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQEL--DKTGLWKVHIIGSNANRGEEAAASLRNTI-----FHQVDVTKYEQQGAAFDKIfnEEKR 76
Cdd:cd09806   2 VVLITGCSSGIGLHLAVRLasDPSKRFKVYATMRDLKKKGRLWEAAGALAggtleTLQLDVCDSKSVAAAVERV--TERH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  77 LDFVLANAGIaedtamffashptGIPPPPDMTGLT------DINFTGAIYTSYLAMhyfrrsPE-KTKGNRHLIIMSSIG 149
Cdd:cd09806  80 VDVLVCNAGV-------------GLLGPLEALSEDamasvfDVNVFGTVRMLQAFL------PDmKRRGSGRILVTSSVG 140

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83775806 150 GLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAffpekiVMKMSDVT 218
Cdd:cd09806 141 GLQGLPFNDVYCASKFALEGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGS------PEEVLDRT 203
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 4-232 3.25e-11

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 62.36  E-value: 3.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGldvaQELDKTGLwkvhiigsnaNRGEEAAASLRNTI----FH----------QVDVTKYEQQGAAFDK 69
Cdd:PRK08263   5 VWFITGASRGFG----RAWTEAAL----------ERGDRVVATARDTAtladLAekygdrllplALDVTDRAAVFAAVET 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   70 IFNEEKRLDFVLANAGIAEDTAMFFASHPtgippppDMTGLTDINFTGAIYTSYLAMHYFRrspekTKGNRHLIIMSSIG 149
Cdd:PRK08263  71 AVEHFGRLDIVVNNAGYGLFGMIEEVTES-------EARAQIDTNFFGALWVTQAVLPYLR-----EQRSGHIIQISSIG 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  150 GLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTT----------------ELQAFFPE----- 208
Cdd:PRK08263 139 GISAFPMSGIYHASKWALEGMSEALAQEVAEFGIKVTLVEPGGYSTDWAGTsakratpldaydtlreELAEQWSErsvdg 218

                        250       260       270
                 ....*....|....*....|....*....|
gi 83775806  209 ------KIVMKMSDVTNVVLKLISGTEVTD 232
Cdd:PRK08263 219 dpeaaaEALLKLVDAENPPLRLFLGSGVLD 248
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-199 6.00e-11

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 60.75  E-value: 6.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlwkVHIIGSNANRGEEAAASLRntiFHQVDVTKyeqqgaAFDKIFNEEKRLDFVLAN 83
Cdd:PRK06550   7 TVLITGAASGIGLAQARAFLAQG---AQVYGVDKQDKPDLSGNFH---FLQLDLSD------DLEPLFDWVPSVDILCNT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   84 AGIAEDTamffasHPTGIPPPPDMTGLTDINFTGaiyTSYLAMHYFRRSPEKTKGnrHLIIMSSIGGLYPCAHTPVYSAT 163
Cdd:PRK06550  75 AGILDDY------KPLLDTSLEEWQHIFDTNLTS---TFLLTRAYLPQMLERKSG--IIINMCSIASFVAGGGGAAYTAS 143

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 83775806  164 KHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMT 199
Cdd:PRK06550 144 KHALAGFTKQLALDYAKDGIQVFGIAPGAVKTP-MT 178
PRK09242 PRK09242
SDR family oxidoreductase;
5-202 7.09e-11

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 60.92  E-value: 7.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTIF-HQV-----DVTKYEQQGAAFDKIFNEEKRLD 78
Cdd:PRK09242  12 ALITGASKGIGLAIAREFLGLGA-DVLIVARDADALAQARDELAEEFPeREVhglaaDVSDDEDRRAILDWVEDHWDGLH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   79 FVLANAGIAEDTAMFFAShptgippPPDMTGLTDINFTGAIYTSYLAMHYFRRSpektkGNRHLIIMSSIGGLYPCAHTP 158
Cdd:PRK09242  91 ILVNNAGGNIRKAAIDYT-------EDEWRGIFETNLFSAFELSRYAHPLLKQH-----ASSAIVNIGSVSGLTHVRSGA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 83775806  159 VYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTEL 202
Cdd:PRK09242 159 PYGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPL 202
PRK07063 PRK07063
SDR family oxidoreductase;
4-197 9.43e-11

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 60.83  E-value: 9.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR------NTIFHQVDVTKYEQQGAAFDKIFNEEKRL 77
Cdd:PRK07063   9 VALVTGAAQGIGAAIARAFAREGA-AVALADLDAALAERAAAAIArdvagaRVLAVPADVTDAASVAAAVAAAEEAFGPL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   78 DFVLANAGI---AEDTAMffashptgipPPPDMTGLTDINFTGAIYTSYLAM-HYFRRspektkGNRHLIIMSSIGGLYP 153
Cdd:PRK07063  88 DVLVNNAGInvfADPLAM----------TDEDWRRCFAVDLDGAWNGCRAVLpGMVER------GRGSIVNIASTHAFKI 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 83775806  154 CAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:PRK07063 152 IPGCFPYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQL 195
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 4-227 1.19e-10

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 60.33  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806     4 VALITGGTSGMGLDVAQELDKTGlWKVHIigsNANRGEEAAASLRNT---------IFHQVDVTK----YEQQGAAFDKI 70
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEG-YRVVL---HYHRSAAAASTLAAElnarrpnsaVTCQADLSNsatlFSRCEAIIDAC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    71 FNEEKRLDFVLANAGIAEDTAMFFASHPTGIP-PPPDMTGLTDINFTGAIYTSYLAMHYFRR----SPEKTKGNRHLIIM 145
Cdd:TIGR02685  79 FRAFGRCDVLVNNASAFYPTPLLRGDAGEGVGdKKSLEVQVAELFGSNAIAPYFLIKAFAQRqagtRAEQRSTNLSIVNL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   146 SSIGGLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGV-VLTPLMTTELQAFFPEKIVMKMSD-----VTN 219
Cdd:TIGR02685 159 CDAMTDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLsLLPDAMPFEVQEDYRRKVPLGQREasaeqIAD 238


                  ....*...
gi 83775806   220 VVLKLISG 227
Cdd:TIGR02685 239 VVIFLVSP 246
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 5-227 1.55e-10

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: 59.79  E-value: 1.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   5 ALITGGTSGMGLDVAQELDKTGlwkVHIIGSNANRGEEAAASLRNTIFhQVDVTKYEQQGAAFDKIFNEEKRLDFVLANA 84
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAG---ATVIALDLPFVLLLEYGDPLRLT-PLDVADAAAVREVCSRLLAEHGPIDALVNCA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  85 GIAedtamffasHPTGIPPPP--DMTGLTDINFTGAIYTSYLAMHYFRRspektKGNRHLIIMSSigglyPCAHTP---- 158
Cdd:cd05331  77 GVL---------RPGATDPLSteDWEQTFAVNVTGVFNLLQAVAPHMKD-----RRTGAIVTVAS-----NAAHVPrism 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806 159 -VYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQ---------AFFPE---------KIVMKmSDVTN 219
Cdd:cd05331 138 aAYGASKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAMQRTLWHdedgaaqviAGVPEqfrlgiplgKIAQP-ADIAN 216


                ....*...
gi 83775806 220 VVLKLISG 227
Cdd:cd05331 217 AVLFLASD 224
PRK06182 PRK06182
short chain dehydrogenase; Validated
 4-196 1.69e-10

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 59.97  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLRNTIfhQVDVTKYEQQGAAFDKIFNEEKRLDFVLAN 83
Cdd:PRK06182   5 VALVTGASSGIGKATARRLAAQG-YTVYGAARRVDKMEDLASLGVHPL--SLDVTDEASIKAAVDTIIAEEGRIDVLVNN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   84 AG-----------IAEDTAMFfashptgippppdmtgltDINFTGAIYTSYLAMHYFRRspektKGNRHLIIMSSIGGLY 152
Cdd:PRK06182  82 AGygsygaiedvpIDEARRQF------------------EVNLFGAARLTQLVLPHMRA-----QRSGRIINISSMGGKI 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 83775806  153 pcaHTPV---YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTP 196
Cdd:PRK06182 139 ---YTPLgawYHATKFALEGFSDALRLEVAPFGIDVVVIEPGGIKTE 182
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-227 1.77e-10

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 59.98  E-value: 1.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlWKVHIIG-SNANRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKRLD 78
Cdd:PRK12745   4 VALVTGGRRGIGLGIARALAAAG-FDLAINDrPDDEELAATQQELRalgvEVIFFPADVADLSAHEAMLDAAQAAWGRID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   79 FVLANAGIAedtamffashptgippPP---DMTGLT--------DINFTGAIY-TSYLAMHYFRRSPEKTKGNRHLIIMS 146
Cdd:PRK12745  83 CLVNNAGVG----------------VKvrgDLLDLTpesfdrvlAINLRGPFFlTQAVAKRMLAQPEPEELPHRSIVFVS 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  147 SIGGLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTELQAFFPEKI-----VMKM----SDV 217
Cdd:PRK12745 147 SVNAIMVSPNRGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTD-MTAPVTAKYDALIakglvPMPRwgepEDV 225

                        250
                 ....*....|
gi 83775806  218 TNVVLKLISG 227
Cdd:PRK12745 226 ARAVAALASG 235
PRK08251 PRK08251
SDR family oxidoreductase;
6-191 2.29e-10

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 59.56  E-value: 2.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    6 LITGGTSGMGLDVAQELDKTGlwkvHIIGSNANRGE---------EAAASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKR 76
Cdd:PRK08251   6 LITGASSGLGAGMAREFAAKG----RDLALCARRTDrleelkaelLARYPGIKVAVAALDVNDHDQVFEVFAEFRDELGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   77 LDFVLANAGIAED----TAMFFASHPTgippppdmtglTDINFTGAIYTSYLAMHYFRRspektKGNRHLIIMSSIGGL- 151
Cdd:PRK08251  82 LDRVIVNAGIGKGarlgTGKFWANKAT-----------AETNFVAALAQCEAAMEIFRE-----QGSGHLVLISSVSAVr 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 83775806  152 -YPCAHTpVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPG 191
Cdd:PRK08251 146 gLPGVKA-AYAASKAGVASLGEGLRAELAKTPIKVSTIEPG 185
PRK06101 PRK06101
SDR family oxidoreductase;
4-197 4.25e-10

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 58.73  E-value: 4.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLRNTIFHQVDVTKYEQQGAAFDKifneekrLDFV--- 80
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQG-WQVIACGRNQSVLDELHTQSANIFTLAFDVTDHPGTKAALSQ-------LPFIpel 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   81 -LANAGIAEdtamffaSHPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRspektkGNRhLIIMSSIGGLYPCAHTPV 159
Cdd:PRK06101  75 wIFNAGDCE-------YMDDGKVDATLMARVFNVNVLGVANCIEGIQPHLSC------GHR-VVIVGSIASELALPRAEA 140

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 83775806  160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:PRK06101 141 YGASKAAVAYFARTLQLDLRPKGIEVVTVFPGFVATPL 178
PRK09291 PRK09291
SDR family oxidoreductase;
6-218 4.96e-10

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 58.47  E-value: 4.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    6 LITGGTSGMGLDVAQELDKTG---LWKVHIIGSNANRGEEAAA---SLRntiFHQVDVT-KYEQQGAA-FDkifneekrL 77
Cdd:PRK09291   6 LITGAGSGFGREVALRLARKGhnvIAGVQIAPQVTALRAEAARrglALR---VEKLDLTdAIDRAQAAeWD--------V 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   78 DFVLANAGIAEDTAMffASHPTGIppppdMTGLTDINFTGAIYtsyLAMHYFRRSPEKTKGNrhLIIMSSIGGLYPCAHT 157
Cdd:PRK09291  75 DVLLNNAGIGEAGAV--VDIPVEL-----VRELFETNVFGPLE---LTQGFVRKMVARGKGK--VVFTSSMAGLITGPFT 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83775806  158 PVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT----PLMTTELQAFFPEKIVMKMSDVT 218
Cdd:PRK09291 143 GAYCASKHALEAIAEAMHAELKPFGIQVATVNPGPYLTgfndTMAETPKRWYDPARNFTDPEDLA 207
PRK07454 PRK07454
SDR family oxidoreductase;
5-201 5.85e-10

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 58.05  E-value: 5.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLRNT----IFHQVDVTKYEQQGAAFDKIFNEEKRLDFV 80
Cdd:PRK07454   9 ALITGASSGIGKATALAFAKAG-WDLALVARSQDALEALAAELRSTgvkaAAYSIDLSNPEAIAPGIAELLEQFGCPDVL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   81 LANAGIAEdTAmffashPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRrspEKTKGnrhLII-MSSIGGLYPCAHTPV 159
Cdd:PRK07454  88 INNAGMAY-TG------PLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMR---ARGGG---LIInVSSIAARNAFPQWGA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 83775806  160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTE 201
Cdd:PRK07454 155 YCVSKAALAAFTKCLAEEERSHGIRVCTITLGAVNTPLWDTE 196
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 4-220 6.43e-10

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


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 58.25  E-value: 6.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlWKVHII---GSNANR--GEEAAASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLD 78
Cdd:cd05322   4 VAVVIGGGQTLGEFLCHGLAEAG-YDVAVAdinSENAEKvaDEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKRVD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  79 FVLANAGIAEdtAMFFASHPTGippppDMTGLTDINFTGaiytsylamhYFRRSPEKTK-----GNRHLII-MSSIGGLY 152
Cdd:cd05322  83 LLVYSAGIAK--SAKITDFELG-----DFDRSLQVNLVG----------YFLCAREFSKlmirdGIQGRIIqINSKSGKV 145

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83775806 153 PCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAFFPEKIVMKMSDVTNV 220
Cdd:cd05322 146 GSKHNSGYSAAKFGGVGLTQSLALDLAEHGITVNSLMLGNLLKSPMFQSLLPQYAKKLGIKESEVEQY 213
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 4-197 6.92e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 58.44  E-value: 6.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASL--RNTIFHQV-DVTKYEQQGAAFDKIFNEEKRLDFV 80
Cdd:PRK05872  11 VVVVTGAARGIGAELARRLHARGA-KLALVDLEEAELAALAAELggDDRVLTVVaDVTDLAAMQAAAEEAVERFGGIDVV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   81 LANAGIAE-------DTAMFfashptgippppdmTGLTDINFTGAIYTsylaMHYFRRSPEKTKGnrHLIIMSSIGGLYP 153
Cdd:PRK05872  90 VANAGIASggsvaqvDPDAF--------------RRVIDVNLLGVFHT----VRATLPALIERRG--YVLQVSSLAAFAA 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 83775806  154 CAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:PRK05872 150 APGMAAYCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDL 193
PRK05717 PRK05717
SDR family oxidoreductase;
4-191 7.46e-10

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 57.98  E-value: 7.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASL-RNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLA 82
Cdd:PRK05717  12 VALVTGAARGIGLGIAAWLIAEG-WQVVLADLDRERGSKVAKALgENAWFIAMDVADEAQVAAGVAEVLGQFGRLDALVC 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   83 NAGIAEDTAMFFASHPTGippppDMTGLTDINFTGAIytsYLAMHYfrrSPEKTKGNRHLIIMSSIGGLYPCAHTPVYSA 162
Cdd:PRK05717  91 NAAIADPHNTTLESLSLA-----HWNRVLAVNLTGPM---LLAKHC---APYLRAHNGAIVNLASTRARQSEPDTEAYAA 159

                        170       180
                 ....*....|....*....|....*....
gi 83775806  163 TKHGLVGFTRSVGKRLLDEgVKVNTVCPG 191
Cdd:PRK05717 160 SKGGLLALTHALAISLGPE-IRVNAVSPG 187
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 4-226 8.67e-10

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 57.59  E-value: 8.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlwkVHIIGSNANRGEEAAASLRNtifHQVDVTKYEQQGAAFDKIFNEEKRLDfVLAN 83
Cdd:PRK08220  10 TVWVTGAAQGIGYAVALAFVEAG---AKVIGFDQAFLTQEDYPFAT---FVLDVSDAAAVAQVCQRLLAETGPLD-VLVN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   84 -AGI----------AEDTAMFFAshptgippppdmtgltdINFTGAIYTSYLAMHYFRRspeKTKGNrhLIIMSSiggly 152
Cdd:PRK08220  83 aAGIlrmgatdslsDEDWQQTFA-----------------VNAGGAFNLFRAVMPQFRR---QRSGA--IVTVGS----- 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  153 PCAHTP-----VYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQ---------AFFPE---------K 209
Cdd:PRK08220 136 NAAHVPrigmaAYGASKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTDMQRTLWVdedgeqqviAGFPEqfklgiplgK 215

                        250
                 ....*....|....*..
gi 83775806  210 IVMKmSDVTNVVLKLIS 226
Cdd:PRK08220 216 IARP-QEIANAVLFLAS 231
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 6-197 9.63e-10

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: 58.06  E-value: 9.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   6 LITGGTSGMGLDVAQELDKTGLwkvHIIGSNANRGEEAAASLRN-------TIfhQVDVTKYEQQGAAFDKIFNE--EKR 76
Cdd:cd09805   4 LITGCDSGFGNLLAKKLDSLGF---TVLAGCLTKNGPGAKELRRvcsdrlrTL--QLDVTKPEQIKRAAQWVKEHvgEKG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  77 LDFVLANAGIAEDTAMFFAShptgipPPPDMTGLTDINFTGAIYTSYLAMHYFRRSpektKGnrHLIIMSSIGGLYPCAH 156
Cdd:cd09805  79 LWGLVNNAGILGFGGDEELL------PMDDYRKCMEVNLFGTVEVTKAFLPLLRRA----KG--RVVNVSSMGGRVPFPA 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 83775806 157 TPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:cd09805 147 GGAYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGI 187
PRK07985 PRK07985
SDR family oxidoreductase;
5-197 1.08e-09

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 58.08  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGLwkvhIIGSNANRGEEAAASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLANA 84
Cdd:PRK07985  52 ALVTGGDSGIGRAAAIAYAREGA----DVAISYLPVEEEDAQDVKKIIEECGRKAVLLPGDLSDEKFARSLVHEAHKALG 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   85 GIaeDTAMFFASHPTGIPpppDMTGLTDINFTGAIYTSYLAMHYFRRS--PEKTKGNRhLIIMSSIGGLYPCAHTPVYSA 162
Cdd:PRK07985 128 GL--DIMALVAGKQVAIP---DIADLTSEQFQKTFAINVFALFWLTQEaiPLLPKGAS-IITTSSIQAYQPSPHLLDYAA 201

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 83775806  163 TKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:PRK07985 202 TKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTAL 236
PRK06114 PRK06114
SDR family oxidoreductase;
4-221 1.10e-09

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 57.48  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASL-----RNTIFHQVDVTKYEQQGAAFDKIFNEEKRLD 78
Cdd:PRK06114  10 VAFVTGAGSGIGQRIAIGLAQAGA-DVALFDLRTDDGLAETAEHieaagRRAIQIAADVTSKADLRAAVARTEAELGALT 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   79 FVLANAGIAedtamffashptGIPPPPDMTG-----LTDINFTGaIYTSYLAMHyfRRSPEKTKGNrhLIIMSSIGGL-- 151
Cdd:PRK06114  89 LAVNAAGIA------------NANPAEEMEEeqwqtVMDINLTG-VFLSCQAEA--RAMLENGGGS--IVNIASMSGIiv 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83775806  152 ---YPCAHtpvYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL-----MTTELQAFFPEKIVMKMSDVTNVV 221
Cdd:PRK06114 152 nrgLLQAH---YNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMntrpeMVHQTKLFEEQTPMQRMAKVDEMV 226
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 4-197 1.66e-09

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


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 57.09  E-value: 1.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR-NTIFHQVDV-------TKYEQQGAAfdKIFNEEK 75
Cdd:cd09807   3 TVIITGANTGIGKETARELARRGA-RVIMACRDMAKCEEAAAEIRrDTLNHEVIVrhldlasLKSIRAFAA--EFLAEED 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  76 RLDFVLANAGI-------AEDT-AMFFAshptgippppdmtgltdINFTGAIYTSYLAMHYFRRSpektkGNRHLIIMSS 147
Cdd:cd09807  80 RLDVLINNAGVmrcpyskTEDGfEMQFG-----------------VNHLGHFLLTNLLLDLLKKS-----APSRIVNVSS 137

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83775806 148 IGGLYPCAHTP------------VYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:cd09807 138 LAHKAGKINFDdlnseksyntgfAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTEL 199
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 4-196 1.69e-09

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 56.86  E-value: 1.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTIFH-QVDVTKYEQQGAAFDKIFNEEKRLDFVLA 82
Cdd:cd05363   5 TALITGSARGIGRAFAQAYVREGA-RVAIADINLEAARATAAEIGPAACAiSLDVTDQASIDRCVAALVDRWGSIDILVN 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  83 NAgiaedtAMFfashptGIPPPPDMT-----GLTDINFTGAIYTSYLAMhyfRRSPEKTKGNRhLIIMSSIGGLYPCAHT 157
Cdd:cd05363  84 NA------ALF------DLAPIVDITresydRLFAINVSGTLFMMQAVA---RAMIAQGRGGK-IINMASQAGRRGEALV 147

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 83775806 158 PVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTP 196
Cdd:cd05363 148 GVYCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGE 186
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
4-227 2.44e-09

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 56.65  E-value: 2.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLWKVHIIGSNANRGEEAAASL----RNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK08063   6 VALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAAEETAEEIealgRKALAVKANVGDVEKIKEMFAQIDEEFGRLDV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANA--GIAEDTAMFFASHptgipppPDMTglTDINftgAIYTSYLAMHYFRRSPEktKGNRHLIIMSSIGGLYPCAHT 157
Cdd:PRK08063  86 FVNNAasGVLRPAMELEESH-------WDWT--MNIN---AKALLFCAQEAAKLMEK--VGGGKIISLSSLGSIRYLENY 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83775806  158 PVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMT---------TELQAFFPEKIVMKMSDVTNVVLKLISG 227
Cdd:PRK08063 152 TTVGVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKhfpnreellEDARAKTPAGRMVEPEDVANAVLFLCSP 230
PRK05867 PRK05867
SDR family oxidoreductase;
5-239 2.55e-09

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 56.58  E-value: 2.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANR----GEEAAASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFV 80
Cdd:PRK05867  12 ALITGASTGIGKRVALAYVEAGA-QVAIAARHLDAleklADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGGIDIA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   81 LANAGIAEDTAMFFAshptgipPPPDMTGLTDINFTGAIYTSYLAMhyfRRSPEKTKGNRhLIIMSSIGGLYPCAHTPV- 159
Cdd:PRK05867  91 VCNAGIITVTPMLDM-------PLEEFQRLQNTNVTGVFLTAQAAA---KAMVKQGQGGV-IINTASMSGHIINVPQQVs 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  160 -YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMT--TELQAFFPEKIVM----KMSDVTNVVLKLIS------ 226
Cdd:PRK05867 160 hYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEpyTEYQPLWEPKIPLgrlgRPEELAGLYLYLASeassym 239

                        250
                 ....*....|....
gi 83775806  227 -GTEVTDSNGTSVP 239
Cdd:PRK05867 240 tGSDIVIDGGYTCP 253
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 4-197 2.63e-09

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 56.50  E-value: 2.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlWKVHIIgsnaNRGEEAAASLRNTIFHQV-----DVTKYEQQGAAFDKIFNEEKRLD 78
Cdd:PRK06200   8 VALITGGGSGIGRALVERFLAEG-ARVAVL----ERSAEKLASLRQRFGDHVlvvegDVTSYADNQRAVDQTVDAFGKLD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   79 FVLANAGIAEdtamffasHPTGIP--PPPDMTGLTD----INFTGAIYTSYLAMhyfrrsPEKTKGNRHLIIMSSIGGLY 152
Cdd:PRK06200  83 CFVGNAGIWD--------YNTSLVdiPAETLDTAFDeifnVNVKGYLLGAKAAL------PALKASGGSMIFTLSNSSFY 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 83775806  153 PCAHTPVYSATKHGLVGFTRSVGKRLLDEgVKVNTVCPGVVLTPL 197
Cdd:PRK06200 149 PGGGGPLYTASKHAVVGLVRQLAYELAPK-IRVNGVAPGGTVTDL 192
PRK06949 PRK06949
SDR family oxidoreductase;
4-227 3.30e-09

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 56.31  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIigsnANRGEEAAASLRNTI------FHQV--DVTKYEQQGAAFDKIFNEEK 75
Cdd:PRK06949  11 VALVTGASSGLGARFAQVLAQAGA-KVVL----ASRRVERLKELRAEIeaeggaAHVVslDVTDYQSIKAAVAHAETEAG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   76 RLDFVLANAGIAEDTAMFFAShptgippPPDMTGLTDINFTGAIYTS------YLAMHyfRRSPEKTKGNRhLIIMSSIG 149
Cdd:PRK06949  86 TIDILVNNSGVSTTQKLVDVT-------PADFDFVFDTNTRGAFFVAqevakrMIARA--KGAGNTKPGGR-IINIASVA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  150 GLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL----MTTE----LQAFFPEKIVMKMSDVTNVV 221
Cdd:PRK06949 156 GLRVLPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEInhhhWETEqgqkLVSMLPRKRVGKPEDLDGLL 235


                 ....*.
gi 83775806  222 LKLISG 227
Cdd:PRK06949 236 LLLAAD 241
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 5-211 4.32e-09

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 55.69  E-value: 4.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASL--RNTIFhQVDVTKYEQQGAAFDKIFNEEKRLDFVLA 82
Cdd:PRK12936   9 ALVTGASGGIGEEIARLLHAQGA-IVGLHGTRVEKLEALAAELgeRVKIF-PANLSDRDEVKALGQKAEADLEGVDILVN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   83 NAGIAEDTAMFFASHPtgippppDMTGLTDINFTGAIYTSYLAMHyfrrsPEKTKGNRHLIIMSSIGGLYPCAHTPVYSA 162
Cdd:PRK12936  87 NAGITKDGLFVRMSDE-------DWDSVLEVNLTATFRLTRELTH-----PMMRRRYGRIINITSVVGVTGNPGQANYCA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 83775806  163 TKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTELQAFFPEKIV 211
Cdd:PRK12936 155 SKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESA-MTGKLNDKQKEAIM 202
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 5-230 4.56e-09

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 54.90  E-value: 4.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   5 ALITGGTSGMGLDVAQELdktglwkvhiigsnANRGEEAAASLRNTIFHQVDVTKYEQQGAAFDKIfneeKRLDFVLANA 84
Cdd:cd11731   1 IIVIGATGTIGLAVAQLL--------------SAHGHEVITAGRSSGDYQVDITDEASIKALFEKV----GHFDAIVSTA 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  85 GIAEdtamfFAshptgipPPPDMTgLTDINFT------GAIYTSYLAMHYFRrspekTKGNRHLIimSSIGGLYPCAHTP 158
Cdd:cd11731  63 GDAE-----FA-------PLAELT-DADFQRGlnskllGQINLVRHGLPYLN-----DGGSITLT--SGILAQRPIPGGA 122

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83775806 159 VYSATKHGLVGFTRSVGKRLLDeGVKVNTVCPGVVLTPLmtTELQAFFPEKIVMKMSDVTNVVLKLISGTEV 230
Cdd:cd11731 123 AAATVNGALEGFVRAAAIELPR-GIRINAVSPGVVEESL--EAYGDFFPGFEPVPAEDVAKAYVRSVEGAFT 191
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
5-204 5.33e-09

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 55.46  E-value: 5.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNT--IFHQVDVTKYEQQGAAFDKIFN--EEKRLD-- 78
Cdd:PRK06924   4 VIITGTSQGLGEAIANQLLEKGT-HVISISRTENKELTKLAEQYNSnlTFHSLDLQDVHELETNFNEILSsiQEDNVSsi 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   79 FVLANAGIAedTAMffasHPTGIPPPPDMTGLTDINFTGAIytsyLAMHYFRRSPEKTKGNRHLIIMSSIGGLYPCAHTP 158
Cdd:PRK06924  83 HLINNAGMV--API----KPIEKAESEELITNVHLNLLAPM----ILTSTFMKHTKDWKVDKRVINISSGAAKNPYFGWS 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 83775806  159 VYSATKHGLVGFTRSVGKRLLDE--GVKVNTVCPGVvltplMTTELQA 204
Cdd:PRK06924 153 AYCSSKAGLDMFTQTVATEQEEEeyPVKIVAFSPGV-----MDTNMQA 195
PRK06947 PRK06947
SDR family oxidoreductase;
1-204 8.75e-09

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 54.81  E-value: 8.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    1 MVLVALITGGTSGMGLDVAQELDKTGlWKVHI-IGSNANRGEEAAASLRNTIFH----QVDVTKYEQQGAAFDKIFNEEK 75
Cdd:PRK06947   1 MRKVVLITGASRGIGRATAVLAAARG-WSVGInYARDAAAAEETADAVRAAGGRacvvAGDVANEADVIAMFDAVQSAFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   76 RLDFVLANAGIAEdtamffASHPTGIPPPPDMTGLTDINFTGAiytsYLAMHYFRRSPEKTKGNR--HLIIMSSIGGLYP 153
Cdd:PRK06947  80 RLDALVNNAGIVA------PSMPLADMDAARLRRMFDTNVLGA----YLCAREAARRLSTDRGGRggAIVNVSSIASRLG 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 83775806  154 CAHTPV-YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGvvltpLMTTELQA 204
Cdd:PRK06947 150 SPNEYVdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPG-----LIETEIHA 196
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 5-203 1.02e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 54.66  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTifHQVDVTKYEQ---QGAAFDKIFNEEKRLDFVL 81
Cdd:PRK06125  10 VLITGASKGIGAAAAEAFAAEGC-HLHLVARDADALEALAADLRAA--HGVDVAVHALdlsSPEAREQLAAEAGDIDILV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   82 ANAGiaedtamffashptGIPPppdmTGLTD-----------------INFTGAIYTsylAMhyfrrspektKGNRHLII 144
Cdd:PRK06125  87 NNAG--------------AIPG----GGLDDvddaawragwelkvfgyIDLTRLAYP---RM----------KARGSGVI 135

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83775806  145 MSSIG--GLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQ 203
Cdd:PRK06125 136 VNVIGaaGENPDADYICGSAGNAALMAFTRALGGKSLDDGVRVVGVNPGPVATDRMLTLLK 196
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 4-191 1.50e-08

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


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 54.12  E-value: 1.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLR-NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLA 82
Cdd:cd09761   3 VAIVTGGGHGIGKQICLDFLEAG-DKVVFADIDEERGADFAEAEGpNLFFVHGDVADETLVKFVVYAMLEKLGRIDVLVN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  83 NAGIAEDTAMFfaSHPTGippppDMTGLTDINFTGaiytSYLAMHYFRrsPEKTKGNRHLIIMSSIGGLYPCAHTPVYSA 162
Cdd:cd09761  82 NAARGSKGILS--SLLLE-----EWDRILSVNLTG----PYELSRYCR--DELIKNKGRIINIASTRAFQSEPDSEAYAA 148

                       170       180
                ....*....|....*....|....*....
gi 83775806 163 TKHGLVGFTRSVGKRlLDEGVKVNTVCPG 191
Cdd:cd09761 149 SKGGLVALTHALAMS-LGPDIRVNCISPG 176
PRK06128 PRK06128
SDR family oxidoreductase;
5-210 1.54e-08

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 54.48  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGlwkVHIIGSNANRGEEAAASL--------RNTIFHQVDVTKYEQQGAAFDKIFNEEKR 76
Cdd:PRK06128  58 ALITGADSGIGRATAIAFAREG---ADIALNYLPEEEQDAAEVvqliqaegRKAVALPGDLKDEAFCRQLVERAVKELGG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   77 LDFVLANAGiaEDTAMffashptgipppPDMTGLTDINFTGAIYTSYLAMHYFRRS--PEKTKGNRhLIIMSSIGGLYPC 154
Cdd:PRK06128 135 LDILVNIAG--KQTAV------------KDIADITTEQFDATFKTNVYAMFWLCKAaiPHLPPGAS-IINTGSIQSYQPS 199

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 83775806  155 AHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAffPEKI 210
Cdd:PRK06128 200 PTLLDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPSGGQP--PEKI 253
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 4-191 1.61e-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: 54.02  E-value: 1.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR---NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFV 80
Cdd:cd08942   8 IVLVTGGSRGIGRMIAQGFLEAGA-RVIISARKAEACADAAEELSaygECIAIPADLSSEEGIEALVARVAERSDRLDVL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  81 LANAGiaedtAMFFAshPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRSpeKTKGNRHLII-MSSIGGLY-PCAHTP 158
Cdd:cd08942  87 VNNAG-----ATWGA--PLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAA--ATAENPARVInIGSIAGIVvSGLENY 157

                       170       180       190
                ....*....|....*....|....*....|...
gi 83775806 159 VYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPG 191
Cdd:cd08942 158 SYGASKAAVHQLTRKLAKELAGEHITVNAIAPG 190
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
6-202 1.85e-08

decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 53.94  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    6 LITGGTSGMGLDVAQELDKTGlwKVHIIGS---NANRGEEAAASLRNTIFHQVDV-----TKYEQQGAAFDKIFnEEKRL 77
Cdd:PRK07904  12 LLLGGTSEIGLAICERYLKNA--PARVVLAalpDDPRRDAAVAQMKAAGASSVEVidfdaLDTDSHPKVIDAAF-AGGDV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   78 DFVLANAGIAEDTAMFFASHPTGIPpppdmtgLTDINFTGAIYTSYLAMHYFrrspeKTKGNRHLIIMSSIGGLYPCAHT 157
Cdd:PRK07904  89 DVAIVAFGLLGDAEELWQNQRKAVQ-------IAEINYTAAVSVGVLLGEKM-----RAQGFGQIIAMSSVAGERVRRSN 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 83775806  158 PVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTEL 202
Cdd:PRK07904 157 FVYGSTKAGLDGFYLGLGEALREYGVRVLVVRPGQVRTR-MSAHA 200
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-197 2.52e-08

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 53.57  E-value: 2.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlWKVHIigsNANRG-EEAAASLR-------NTIFHQVDVTKYEQQGAAFDKIFNEEK 75
Cdd:PRK06077   8 VVVVTGSGRGIGRAIAVRLAKEG-SLVVV---NAKKRaEEMNETLKmvkenggEGIGVLADVSTREGCETLAKATIDRYG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   76 RLDFVLANAGIAedTAMFFASHPTGIppppdMTGLTDINFTGAIYTSYLAMHYFRRSPEktkgnrhLIIMSSIGGLYPCA 155
Cdd:PRK06077  84 VADILVNNAGLG--LFSPFLNVDDKL-----IDKHISTDFKSVIYCSQELAKEMREGGA-------IVNIASVAGIRPAY 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 83775806  156 HTPVYSATKHGLVGFTRSVGKRLLDEgVKVNTVCPGVVLTPL 197
Cdd:PRK06077 150 GLSIYGAMKAAVINLTKYLALELAPK-IRVNAIAPGFVKTKL 190
PRK07577 PRK07577
SDR family oxidoreductase;
5-197 3.61e-08

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 52.81  E-value: 3.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELdktglwkvhiigsnANRGEEAAASLRNTI------FHQVDVTKYEQQGAAFDKIfNEEKRLD 78
Cdd:PRK07577   6 VLVTGATKGIGLALSLRL--------------ANLGHQVIGIARSAIddfpgeLFACDLADIEQTAATLAQI-NEIHPVD 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   79 FVLANAGIAedtamffASHPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRSPEKTKGNrhlIIMSSIGGLYpcAHTP 158
Cdd:PRK07577  71 AIVNNVGIA-------LPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVN---ICSRAIFGAL--DRTS 138

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 83775806  159 vYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:PRK07577 139 -YSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETEL 176
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-199 4.76e-08

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 52.66  E-value: 4.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK08217   7 VIVITGGAQGLGRAMAEYLAQKGA-KLALIDLNQEKLEEAVAECGalgtEVRGYAANVTDEEDVEATFAQIAEDFGQLNG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAED------------TAMFFASHPTGIppppdmtgltDINFTGAIYTSylamhyfRRSPEK--TKGNRHLII- 144
Cdd:PRK08217  86 LINNAGILRDgllvkakdgkvtSKMSLEQFQSVI----------DVNLTGVFLCG-------REAAAKmiESGSKGVIIn 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 83775806  145 MSSIGGLYPCAHTPvYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMT 199
Cdd:PRK08217 149 ISSIARAGNMGQTN-YSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETE-MT 201
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 3-241 6.12e-08

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


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 52.47  E-value: 6.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   3 LVALITGGTSGMGLDVAQELDKTGLWKVHIIGSNANRgEEAAASLRNTIFHQVDVTKYEQQGAAFDKIFneekRLDFVLA 82
Cdd:cd05351   8 KRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADL-DSLVRECPGIEPVCVDLSDWDATEEALGSVG----PVDLLVN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  83 NAGIAedtamffASHPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFrrspeKTKGNRHLII-MSSIGGLYPCAHTPVYS 161
Cdd:cd05351  83 NAAVA-------ILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGM-----IARGVPGSIVnVSSQASQRALTNHTVYC 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806 162 ATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT---------PLMTTELQAFFPEKIVMKMSDVTNVVLKLISgTEVTD 232
Cdd:cd05351 151 STKAALDMLTKVMALELGPHKIRVNSVNPTVVMTdmgrdnwsdPEKAKKMLNRIPLGKFAEVEDVVNAILFLLS-DKSSM 229


                ....*....
gi 83775806 233 SNGTSVPSD 241
Cdd:cd05351 230 TTGSTLPVD 238
PRK07062 PRK07062
SDR family oxidoreductase;
4-193 7.07e-08

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 52.35  E-value: 7.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNT-----IFHQV-DVTKYEQQGAAFDKIFNEEKRL 77
Cdd:PRK07062  10 VAVVTGGSSGIGLATVELLLEAGA-SVAICGRDEERLASAEARLREKfpgarLLAARcDVLDEADVAAFAAAVEARFGGV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   78 DFVLANAGIA-----EDTamffashptgipPPPDMTGLTDINFTGAIYTSYLAMHYFRRSPEKTkgnrhLIIMSSIGGLY 152
Cdd:PRK07062  89 DMLVNNAGQGrvstfADT------------TDDAWRDELELKYFSVINPTRAFLPLLRASAAAS-----IVCVNSLLALQ 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 83775806  153 PCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVV 193
Cdd:PRK07062 152 PEPHMVATSAARAGLLNLVKSLATELAPKGVRVNSILLGLV 192
PRK07041 PRK07041
SDR family oxidoreductase;
6-238 8.76e-08

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 51.58  E-value: 8.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    6 LITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRN-----TIfhQVDVTkyeqQGAAFDKIFNEEKRLDFV 80
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGA-RVTIASRSRDRLAAAARALGGgapvrTA--ALDIT----DEAAVDAFFAEAGPFDHV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   81 LAnagiaedTAMFFASHPTGIPPPPDMTGLTDINFTGAiytsYLAMhyfrRSPEKTKGNRhLIIMSSIGGLYPCAHTPVY 160
Cdd:PRK07041  74 VI-------TAADTPGGPVRALPLAAAQAAMDSKFWGA----YRVA----RAARIAPGGS-LTFVSGFAAVRPSASGVLQ 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  161 SATKHGLVGFTRSVGKRLldEGVKVNTVCPGVVLTPL-----------MTTELQAFFPEKIVMKMSDVTNVVLKLISGTE 229
Cdd:PRK07041 138 GAINAALEALARGLALEL--APVRVNTVSPGLVDTPLwsklagdareaMFAAAAERLPARRVGQPEDVANAILFLAANGF 215


                 ....*....
gi 83775806  230 VTdsnGTSV 238
Cdd:PRK07041 216 TT---GSTV 221
PRK09135 PRK09135
pteridine reductase; Provisional
 4-196 9.19e-08

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 51.85  E-value: 9.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlWKVHIigsNANRGEEAAASLR---------NTIFHQVDVTKYEQQGAAFDKIFNEE 74
Cdd:PRK09135   8 VALITGGARRIGAAIARTLHAAG-YRVAI---HYHRSAAEADALAaelnalrpgSAAALQADLLDPDALPELVAACVAAF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   75 KRLDFVLANAgiaedtAMFFAShPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRrspeKTKGNrhlII-MSSIGGLYP 153
Cdd:PRK09135  84 GRLDALVNNA------SSFYPT-PLGSITEAQWDDLFASNLKAPFFLSQAAAPQLR----KQRGA---IVnITDIHAERP 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 83775806  154 CAHTPVYSATKHGLVGFTRSVGKRLLDEgVKVNTVCPGVVLTP 196
Cdd:PRK09135 150 LKGYPVYCAAKAALEMLTRSLALELAPE-VRVNAVAPGAILWP 191
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 4-235 1.25e-07

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: 51.42  E-value: 1.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRN----TIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:cd05365   1 VAIVTGGAAGIGKAIAGTLAKAGA-SVVIADLKSEGAEAVAAAIQQaggqAIGLECNVTSEQDLEAVVKATVSQFGGITI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGiaedtamffashptGIPPPPDMTGLTDINFTGAIYTSYLAmhYFRRS----PEKTK-GNRHLIIMSSIGGLYPC 154
Cdd:cd05365  80 LVNNAG--------------GGGPKPFDMPMTEEDFEWAFKLNLFS--AFRLSqlcaPHMQKaGGGAILNISSMSSENKN 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806 155 AHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGV--------VLTPLMTTELQAFFPEKIVMKMSDVTNVVLKL-- 224
Cdd:cd05365 144 VRIAAYGSSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAvktdalasVLTPEIERAMLKHTPLGRLGEPEDIANAALFLcs 223

                       250
                ....*....|....*.
gi 83775806 225 -----ISGTEVTDSNG 235
Cdd:cd05365 224 pasawVSGQVLTVSGG 239
PRK07774 PRK07774
SDR family oxidoreductase;
4-223 1.78e-07

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 50.90  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK07774   8 VAIVTGAAGGIGQAYAEALAREGA-SVVVADINAEGAERVAKQIVadggTAIAVQVDVSDPDSAKAMADATVSAFGGIDY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAEDTAMFFASHPtgipPPPDMTGLTDINFTGAIYTSYLAMHYFRRspektKGNRHLIIMSSIGG-LYpcahTP 158
Cdd:PRK07774  87 LVNNAAIYGGMKLDLLITV----PWDYYKKFMSVNLDGALVCTRAVYKHMAK-----RGGGAIVNQSSTAAwLY----SN 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83775806  159 VYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGvvltPLMTTELQAFFPEKIVMKMsdVTNVVLK 223
Cdd:PRK07774 154 FYGLAKVGLNGLTQQLARELGGMNIRVNAIAPG----PIDTEATRTVTPKEFVADM--VKGIPLS 212
PRK06482 PRK06482
SDR family oxidoreductase;
1-195 1.90e-07

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 51.27  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    1 MVLVALITGGTSGMGLDVAQELdktglwkvhiigsnANRGEEAAASLRNT------------IFH--QVDVTKYEQQGAA 66
Cdd:PRK06482   1 MSKTWFITGASSGFGRGMTERL--------------LARGDRVAATVRRPdalddlkarygdRLWvlQLDVTDSAAVRAV 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   67 FDKIFNEEKRLDFVLANAGIaedtAMFFASHptgippppdmtGLTD--------INFTGAIYTSYLAMHYFRRspektKG 138
Cdd:PRK06482  67 VDRAFAALGRIDVVVSNAGY----GLFGAAE-----------ELSDaqirrqidTNLIGSIQVIRAALPHLRR-----QG 126

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 83775806  139 NRHLIIMSSIGGLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT 195
Cdd:PRK06482 127 GGRIVQVSSEGGQIAYPGFSLYHATKWGIEGFVEAVAQEVAPFGIEFTIVEPGPART 183
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 4-223 2.51e-07

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: 50.48  E-value: 2.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLWKVHI----IGSNANRGEEAAAslrNTIFHQVDVTKYEQQGAAFDKIfneeKRLDF 79
Cdd:cd05354   5 TVLVTGANRGIGKAFVESLLAHGAKKVYAavrdPGSAAHLVAKYGD---KVVPLRLDVTDPESIKAAAAQA----KDVDV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  80 VLANAGIAEdtamffashPTGIPPPPDMTGLT---DINFTGAI-----YTSYLAMHyfrrspektkGNRHLIIMSSIGGL 151
Cdd:cd05354  78 VINNAGVLK---------PATLLEEGALEALKqemDVNVFGLLrlaqaFAPVLKAN----------GGGAIVNLNSVASL 138

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83775806 152 YPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTELQAFFPEKIvmkmsDVTNVVLK 223
Cdd:cd05354 139 KNFPAMGTYSASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTR-MAAGAGGPKESPE-----TVAEAVLK 204
PRK07102 PRK07102
SDR family oxidoreductase;
6-225 4.49e-07

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 49.54  E-value: 4.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    6 LITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLR-----NTIFHQVDVTKYEQQGAAFDKIfneEKRLDFV 80
Cdd:PRK07102   5 LIIGATSDIARACARRYAAAG-ARLYLAARDVERLERLADDLRargavAVSTHELDILDTASHAAFLDSL---PALPDIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   81 LANAGIAEDTAMFFAShptgipppPDMTGLT-DINFTGAI-YTSYLAMHYFRRspektkGNRHLIIMSSIGGLYPCAHTP 158
Cdd:PRK07102  81 LIAVGTLGDQAACEAD--------PALALREfRTNFEGPIaLLTLLANRFEAR------GSGTIVGISSVAGDRGRASNY 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83775806  159 VYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTELQafFPEKIVMKMSDVTNVVLKLI 225
Cdd:PRK07102 147 VYGSAKAALTAFLSGLRNRLFKSGVHVLTVKPGFVRTP-MTAGLK--LPGPLTAQPEEVAKDIFRAI 210
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 4-84 4.62e-07

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 49.68  E-value: 4.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLrNTIFHQV-----DVTKYEQQGAAFDKIFNEEKRLD 78
Cdd:PRK07677   3 VVIITGGSSGMGKAMAKRFAEEG-ANVVITGRTKEKLEEAKLEI-EQFPGQVltvqmDVRNPEDVQKMVEQIDEKFGRID 80


                 ....*.
gi 83775806   79 FVLANA 84
Cdd:PRK07677  81 ALINNA 86
PRK05855 PRK05855
SDR family oxidoreductase;
5-200 5.56e-07

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 50.36  E-value: 5.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGlwkVHIIGSNANrgEEAAASLRNTI--------FHQVDVTKYEQQGAAFDKIFNEEKR 76
Cdd:PRK05855 318 VVVTGAGSGIGRETALAFAREG---AEVVASDID--EAAAERTAELIraagavahAYRVDVSDADAMEAFAEWVRAEHGV 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   77 LDFVLANAGIAedTAMFFASHPtgippPPDMTGLTDINFTGAIYTSYLamhYFRRSPEKTKGNrHLIIMSSIGGLYPCAH 156
Cdd:PRK05855 393 PDIVVNNAGIG--MAGGFLDTS-----AEDWDRVLDVNLWGVIHGCRL---FGRQMVERGTGG-HIVNVASAAAYAPSRS 461

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 83775806  157 TPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTT 200
Cdd:PRK05855 462 LPAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVAT 505
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 5-213 7.72e-07

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 48.28  E-value: 7.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   5 ALITGGTSGMGLDVAQELDKTGLWKVHIIgsnanrgeeaaaslrntifhqvdvtkyeqqgaafdkifneeKRLDFVLANA 84
Cdd:cd02266   1 VLVTGGSGGIGGAIARWLASRGSPKVLVV-----------------------------------------SRRDVVVHNA 39

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  85 GIAEDTamffashptgipPPPDMTG-----LTDINFTGAiytsyLAMHYFRRSPEKTKGNRHLIIMSSIGGLYPCAHTPV 159
Cdd:cd02266  40 AILDDG------------RLIDLTGsrierAIRANVVGT-----RRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGG 102

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 83775806 160 YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAffPEKIVMK 213
Cdd:cd02266 103 YAASKAALDGLAQQWASEGWGNGLPATAVACGTWAGSGMAKGPVA--PEEILGN 154
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 4-196 9.67e-07

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 48.47  E-value: 9.67e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLWkvhIIGSNANRGEEAAASLrntIFHQVDVTKyEQQGAAFDKIFNEEKRLDFVLAN 83
Cdd:cd05334   3 VVLVYGGRGALGSAVVQAFKSRGWW---VASIDLAENEEADASI---IVLDSDSFT-EQAKQVVASVARLSGKVDALICV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  84 AG------IAEDTamFFAShptgippppdmtglTDINFTGAIYTSYLAMHYFRRSpekTKGNRHLIIMSSIGGLYPCAHT 157
Cdd:cd05334  76 AGgwaggsAKSKS--FVKN--------------WDLMWKQNLWTSFIASHLATKH---LLSGGLLVLTGAKAALEPTPGM 136

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 83775806 158 PVYSATKHGLVGFTRSVG--KRLLDEGVKVNTVCPGVVLTP 196
Cdd:cd05334 137 IGYGAAKAAVHQLTQSLAaeNSGLPAGSTANAILPVTLDTP 177
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-195 1.04e-06

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 48.72  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlwkVHIIGSN----ANRGEEAAASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK08993  12 VAVVTGCDTGLGQGMALGLAEAG---CDIVGINivepTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEFGHIDI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAG-IAEDTAMFFASHptgippppDMTGLTDINFTGAIYTSYLAMHYFRRSPEKTKGNRHLIIMSSIGGLypcaHTP 158
Cdd:PRK08993  89 LVNNAGlIRREDAIEFSEK--------DWDDVMNLNIKSVFFMSQAAAKHFIAQGNGGKIINIASMLSFQGGI----RVP 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 83775806  159 VYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT 195
Cdd:PRK08993 157 SYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMAT 193
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-190 1.05e-06

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 49.01  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    3 LVALITGGTSGMGLDVAQELDKTG-LWKVHIIGSNANrGEEAAASLR----NTIFHQVDVTKYEQqGAAFDKIFNEEKRL 77
Cdd:PRK07792  13 KVAVVTGAAAGLGRAEALGLARLGaTVVVNDVASALD-ASDVLDEIRaagaKAVAVAGDISQRAT-ADELVATAVGLGGL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   78 DFVLANAGIAEDTAMFFASHPtgippppDMTGLTDINFTGAIYTSYLAMHYFRrSPEKTKGNR---HLIIMSSIGGLYPC 154
Cdd:PRK07792  91 DIVVNNAGITRDRMLFNMSDE-------EWDAVIAVHLRGHFLLTRNAAAYWR-AKAKAAGGPvygRIVNTSSEAGLVGP 162

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 83775806  155 AHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCP 190
Cdd:PRK07792 163 VGQANYGAAKAGITALTLSAARALGRYGVRANAICP 198
PRK06139 PRK06139
SDR family oxidoreductase;
4-196 1.08e-06

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 48.95  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLWKVHiigsnANRGEEAAASLRNT--------IFHQVDVTKYEQQGAAFDKIFNEEK 75
Cdd:PRK06139   9 VVVITGASSGIGQATAEAFARRGARLVL-----AARDEEALQAVAEEcralgaevLVVPTDVTDADQVKALATQAASFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   76 RLDFVLANAGIA-----EDTAMffASHPTGIppppdmtgltDINFTGAIYTSYLAMHYFrrspeKTKGNRHLIIMSSIGG 150
Cdd:PRK06139  84 RIDVWVNNVGVGavgrfEETPI--EAHEQVI----------QTNLIGYMRDAHAALPIF-----KKQGHGIFINMISLGG 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 83775806  151 LYPCAHTPVYSATKHGLVGFTRSVGKRLLDE-GVKVNTVCPGVVLTP 196
Cdd:PRK06139 147 FAAQPYAAAYSASKFGLRGFSEALRGELADHpDIHVCDVYPAFMDTP 193
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 5-150 1.16e-06

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 49.05  E-value: 1.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   5 ALITGGTSGMGLDVAQELDKTGLWKVHIIGSNANRGEEAAASL-----RNTIFHqVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:cd09810   4 VVITGASSGLGLAAAKALARRGEWHVVMACRDFLKAEQAAQEVgmpkdSYSVLH-CDLASLDSVRQFVDNFRRTGRPLDA 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83775806  80 VLANAGIAEDTAMFFASHPTGIppppDMTglTDINFTGAIYTSYLAMHYFRRSPEKTKgnrHLIIMSSIGG 150
Cdd:cd09810  83 LVCNAAVYLPTAKEPRFTADGF----ELT--VGVNHLGHFLLTNLLLEDLQRSENASP---RIVIVGSITH 144
PRK09072 PRK09072
SDR family oxidoreductase;
6-204 1.24e-06

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 48.40  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    6 LITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTIFHQV---DVTKyEQQGAAFDKIFNEEKRLDFVLA 82
Cdd:PRK09072   9 LLTGASGGIGQALAEALAAAGA-RLLLVGRNAEKLEALAARLPYPGRHRWvvaDLTS-EAGREAVLARAREMGGINVLIN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   83 NAGIAeDTAMFFASHPTGIppppdmTGLTDINFTGAIYTSYLAMHYFRRSPektkgnrHLIIMS------SIGglYPcAH 156
Cdd:PRK09072  87 NAGVN-HFALLEDQDPEAI------ERLLALNLTAPMQLTRALLPLLRAQP-------SAMVVNvgstfgSIG--YP-GY 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 83775806  157 TpVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQA 204
Cdd:PRK09072 150 A-SYCASKFALRGFSEALRRELADTGVRVLYLAPRATRTAMNSEAVQA 196
PRK09186 PRK09186
flagellin modification protein A; Provisional
 4-226 1.52e-06

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 48.06  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTI------FHQVDVTKYEQQGAAFDKIFNEEKRL 77
Cdd:PRK09186   6 TILITGAGGLIGSALVKAILEAGG-IVIAADIDKEALNELLESLGKEFkskklsLVELDITDQESLEEFLSKSAEKYGKI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   78 DFVLANAGIAEDT--AMFFashptgippppDMTgLTDIN------FTGAIYTSYLAMHYFrrspeKTKGNRHLIIMSSIG 149
Cdd:PRK09186  85 DGAVNCAYPRNKDygKKFF-----------DVS-LDDFNenlslhLGSSFLFSQQFAKYF-----KKQGGGNLVNISSIY 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  150 GLYPCA---------HTPV-YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQAFFPE---KIVMKMSD 216
Cdd:PRK09186 148 GVVAPKfeiyegtsmTSPVeYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGILDNQPEAFLNAYKKCcngKGMLDPDD 227

                        250
                 ....*....|
gi 83775806  217 VTNVVLKLIS 226
Cdd:PRK09186 228 ICGTLVFLLS 237
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 5-197 1.73e-06

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 48.23  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTIFHQV----DVTKYEQQGAAFDKIFNEEKRLDFV 80
Cdd:PRK07523  13 ALVTGSSQGIGYALAEGLAQAGA-EVILNGRDPAKLAAAAESLKGQGLSAHalafDVTDHDAVRAAIDAFEAEIGPIDIL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   81 LANAGiaedtaMFFAShPTGIPPPPDMTGLTDINFTGAIYTSY-LAMHYFRRSPEKtkgnrhLIIMSSIG------GLYP 153
Cdd:PRK07523  92 VNNAG------MQFRT-PLEDFPADAFERLLRTNISSVFYVGQaVARHMIARGAGK------IINIASVQsalarpGIAP 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 83775806  154 cahtpvYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPL 197
Cdd:PRK07523 159 ------YTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPL 196
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 5-205 1.80e-06

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 47.83  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTIFHQV----DVTKYEQQGAAFDKIFNEEKRLDFV 80
Cdd:PRK08085  12 ILITGSAQGIGFLLATGLAEYGA-EIIINDITAERAELAVAKLRQEGIKAHaapfNVTHKQEVEAAIEHIEKDIGPIDVL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   81 LANAGIAEdtamffaSHPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFrrspekTKGNRHLII----MSSIGGLYPCah 156
Cdd:PRK08085  91 INNAGIQR-------RHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYM------VKRQAGKIInicsMQSELGRDTI-- 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 83775806  157 TPvYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTEL---QAF 205
Cdd:PRK08085 156 TP-YAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTE-MTKALvedEAF 205
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-195 2.01e-06

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 47.98  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlwkVHIIGSNANRGEEAAASLRNT--IFHQVDVTKYEQQG--AAFDKIFNEEKRLDF 79
Cdd:PRK12481  10 VAIITGCNTGLGQGMAIGLAKAG---ADIVGVGVAEAPETQAQVEALgrKFHFITADLIQQKDidSIVSQAVEVMGHIDI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIA--EDTAMFfashptgipPPPDMTGLTDINFTGAIYTSYLAMHYFRRSPEKTKGNRHLIIMSSIGGLypcaHT 157
Cdd:PRK12481  87 LINNAGIIrrQDLLEF---------GNKDWDDVININQKTVFFLSQAVAKQFVKQGNGGKIINIASMLSFQGGI----RV 153

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 83775806  158 PVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT 195
Cdd:PRK12481 154 PSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMAT 191
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-191 3.29e-06

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 47.06  E-value: 3.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    6 LITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR---NTIFHQVDVTKYEQQGAAFDKIFNEEKRLD-FVL 81
Cdd:PRK05786   9 AIIGVSEGLGYAVAYFALKEGA-QVCINSRNENKLKRMKKTLSkygNIHYVVGDVSSTESARNVIEKAAKVLNAIDgLVV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   82 ANAGIAEDTAmffashptgipppPDMTGLTDInFTGAIYTSYLAMHYFRRspeKTKGNRHLIIMSSIGGLYPCAHTPV-Y 160
Cdd:PRK05786  88 TVGGYVEDTV-------------EEFSGLEEM-LTNHIKIPLYAVNASLR---FLKEGSSIVLVSSMSGIYKASPDQLsY 150

                        170       180       190
                 ....*....|....*....|....*....|.
gi 83775806  161 SATKHGLVGFTRSVGKRLLDEGVKVNTVCPG 191
Cdd:PRK05786 151 AVAKAGLAKAVEILASELLGRGIRVNGIAPT 181
PRK08177 PRK08177
SDR family oxidoreductase;
5-195 3.53e-06

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 46.95  E-value: 3.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRgEEAAASLRNTIFHQVDVTKYEQQGAAFDKIfnEEKRLDFVLANA 84
Cdd:PRK08177   4 ALIIGASRGLGLGLVDRLLERG-WQVTATVRGPQQ-DTALQALPGVHIEKLDMNDPASLDQLLQRL--QGQRFDLLFVNA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   85 GIAEdtamffashptgiPPPPDMTGLT-----DINFTGAIYTSYLAMhyfRRSPEKTKGNRHLIIMSSIGG---LYPCAH 156
Cdd:PRK08177  80 GISG-------------PAHQSAADATaaeigQLFLTNAIAPIRLAR---RLLGQVRPGQGVLAFMSSQLGsveLPDGGE 143

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 83775806  157 TPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT 195
Cdd:PRK08177 144 MPLYKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKT 182
PRK08589 PRK08589
SDR family oxidoreductase;
4-198 3.60e-06

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 47.08  E-value: 3.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlwkVHIIGSNANRG-EEAAASLRN-----TIFHqVDVTKYEQQGAAFDKIFNEEKRL 77
Cdd:PRK08589   8 VAVITGASTGIGQASAIALAQEG---AYVLAVDIAEAvSETVDKIKSnggkaKAYH-VDISDEQQVKDFASEIKEQFGRV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   78 DFVLANAGIaEDTAMFFASHPTGIppppdMTGLTDINFTGAIYTSYLAMhyfrrsPEKTKGNRHLIIMSSIGGLYPCAHT 157
Cdd:PRK08589  84 DVLFNNAGV-DNAAGRIHEYPVDV-----FDKIMAVDMRGTFLMTKMLL------PLMMEQGGSIINTSSFSGQAADLYR 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 83775806  158 PVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLM 198
Cdd:PRK08589 152 SGYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLV 192
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 4-235 4.10e-06

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 46.93  E-value: 4.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHI--IGsNANRGEEAAASLRNTIFHQVdVTKYEQQGAAFDKIFNEEK------ 75
Cdd:cd05353   7 VVLVTGAGGGLGRAYALAFAERGA-KVVVndLG-GDRKGSGKSSSAADKVVDEI-KAAGGKAVANYDSVEDGEKivktai 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  76 ----RLDFVLANAGIAEDTAMFFASHPtgippppDMTGLTDINFTGAIYTSYLAMHYFRrspeKTKGNRhlIIM-SSIGG 150
Cdd:cd05353  84 dafgRVDILVNNAGILRDRSFAKMSEE-------DWDLVMRVHLKGSFKVTRAAWPYMR----KQKFGR--IINtSSAAG 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806 151 LYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVvlTPLMTtelQAFFPEKIV--MKMSDVTNVVLKLisGT 228
Cdd:cd05353 151 LYGNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPAA--GSRMT---ETVMPEDLFdaLKPEYVAPLVLYL--CH 223


                ....*..
gi 83775806 229 EVTDSNG 235
Cdd:cd05353 224 ESCEVTG 230
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 5-197 4.16e-06

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


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 46.36  E-value: 4.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   5 ALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANR----GEEAAASLRNTifhqvDVTKYEQQGAAFDkifnEEKRLDFV 80
Cdd:cd11730   1 ALILGATGGIGRALARALAGRG-WRLLLSGRDAGAlaglAAEVGALARPA-----DVAAELEVWALAQ----ELGPLDLL 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  81 LANAGIAEdtamffaSHPTGIPPPPDMTGLTDINFTGAiytsYLAMHYFRrsPEKTKGNRHLIImssigGLYP-CAHTP- 158
Cdd:cd11730  71 VYAAGAIL-------GKPLARTKPAAWRRILDANLTGA----ALVLKHAL--ALLAAGARLVFL-----GAYPeLVMLPg 132

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 83775806 159 --VYSATKHGLVGFTRSVGKRLldEGVKVNTVCPGVVLTPL 197
Cdd:cd11730 133 lsAYAAAKAALEAYVEVARKEV--RGLRLTLVRPPAVDTGL 171
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 4-195 1.31e-05

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: 45.61  E-value: 1.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGlwkVHIIGSNANRG--EEAAASLRN-------TIFHqvdVTKYEQQGAAFDKIFNEE 74
Cdd:cd08936  12 VALVTASTDGIGLAIARRLAQDG---AHVVVSSRKQQnvDRAVATLQGeglsvtgTVCH---VGKAEDRERLVATAVNLH 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  75 KRLDFVLANAGIAedtaMFFASHPTGIPPPPDMTglTDINFTGAIYTSYLAMhyfrrsPEKTK-GNRHLIIMSSIGGLYP 153
Cdd:cd08936  86 GGVDILVSNAAVN----PFFGNILDSTEEVWDKI--LDVNVKATALMTKAVV------PEMEKrGGGSVVIVSSVAAFHP 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 83775806 154 CAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT 195
Cdd:cd08936 154 FPGLGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKT 195
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 3-193 1.40e-05

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 45.13  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    3 LVALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLRNTIFH-QVDVTKYEQQGAAFDKIFNEEKRLDFVL 81
Cdd:PRK10538   1 MIVLVTGATAGFGECITRRFIQQG-HKVIATGRRQERLQELKDELGDNLYIaQLDVRNRAAIEEMLASLPAEWRNIDVLV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   82 ANAGIAedtamfFASHPTGIPPPPDMTGLTDINFTGAIYTSYLAMhyfrrsPEKTKGNR-HLIIMSSIGGLYPCAHTPVY 160
Cdd:PRK10538  80 NNAGLA------LGLEPAHKASVEDWETMIDTNNKGLVYMTRAVL------PGMVERNHgHIINIGSTAGSWPYAGGNVY 147

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 83775806  161 SATKhglvGFTR--SVGKR--LLDEGVKVNTVCPGVV 193
Cdd:PRK10538 148 GATK----AFVRqfSLNLRtdLHGTAVRVTDIEPGLV 180
PRK07035 PRK07035
SDR family oxidoreductase;
4-195 1.48e-05

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 45.39  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlwkVHIIGSNanRGEEAAASLRNTIF-----------HqvdVTKYEQQGAAFDKIFN 72
Cdd:PRK07035  10 IALVTGASRGIGEAIAKLLAQQG---AHVIVSS--RKLDGCQAVADAIVaaggkaealacH---IGEMEQIDALFAHIRE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   73 EEKRLDFVLANAG--------IAEDTAMFfashptgippppDMTglTDINFTGaiytsylamhYFRRSPE-----KTKGN 139
Cdd:PRK07035  82 RHGRLDILVNNAAanpyfghiLDTDLGAF------------QKT--VDVNIRG----------YFFMSVEagklmKEQGG 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 83775806  140 RHLIIMSSIGGLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT 195
Cdd:PRK07035 138 GSIVNVASVNGVSPGDFQGIYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDT 193
PRK07831 PRK07831
SDR family oxidoreductase;
4-196 1.97e-05

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 45.02  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITG--GTsGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR-----NTIFHQV-DVTKYEQQGAAFDKIFNEEK 75
Cdd:PRK07831  19 VVLVTAaaGT-GIGSATARRALEEGA-RVVISDIHERRLGETADELAaelglGRVEAVVcDVTSEAQVDALIDAAVERLG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   76 RLDFVLANAGIAEDTAMFfashptgippppDMTG-----LTDINFTGAIYTSYLAMHYFRrspekTKGNRHLII-MSSIG 149
Cdd:PRK07831  97 RLDVLVNNAGLGGQTPVV------------DMTDdewsrVLDVTLTGTFRATRAALRYMR-----ARGHGGVIVnNASVL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 83775806  150 GL---YPCAHtpvYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTP 196
Cdd:PRK07831 160 GWraqHGQAH---YAAAKAGVMALTRCSALEAAEYGVRINAVAPSIAMHP 206
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 6-199 2.02e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 45.18  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    6 LITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR------NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK05875  11 LVTGGGSGIGKGVAAGLVAAGA-AVMIVGRNPDKLAAAAEEIEalkgagAVRYEPADVTDEDQVARAVDAATAWHGRLHG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAEDtamffashptgIPPPPDMTG-----LTDINFTGAIYTSYLAMHYFRRSpektkGNRHLIIMSSIGGLYPC 154
Cdd:PRK05875  90 VVHCAGGSET-----------IGPITQIDSdawrrTVDLNVNGTMYVLKHAARELVRG-----GGGSFVGISSIAASNTH 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 83775806  155 AHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMT 199
Cdd:PRK05875 154 RWFGAYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVA 198
PRK06194 PRK06194
hypothetical protein; Provisional
 4-195 2.03e-05

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 45.01  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNT----IFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK06194   8 VAVITGAASGFGLAFARIGAALGM-KLVLADVQQDALDRAVAELRAQgaevLGVRTDVSDAAQVEALADAALERFGAVHL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAEDTAMFFAShptgippPPDMTGLTDINFTGAIYTSYLAMHYFRRSPEKTKGNR-HLIIMSSIGGLYPCAHTP 158
Cdd:PRK06194  87 LFNNAGVGAGGLVWENS-------LADWEWVLGVNLWGVIHGVRAFTPLMLAAAEKDPAYEgHIVNTASMAGLLAPPAMG 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 83775806  159 VYSATKHGLVGFTRSVGK--RLLDEGVKVNTVCPGVVLT 195
Cdd:PRK06194 160 IYNVSKHAVVSLTETLYQdlSLVTDQVGASVLCPYFVPT 198
PRK06196 PRK06196
oxidoreductase; Provisional
 4-86 2.19e-05

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 45.06  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLAN 83
Cdd:PRK06196  28 TAIVTGGYSGLGLETTRALAQAGA-HVIVPARRPDVAREALAGIDGVEVVMLDLADLESVRAFAERFLDSGRRIDILINN 106


                 ...
gi 83775806   84 AGI 86
Cdd:PRK06196 107 AGV 109
PRK12742 PRK12742
SDR family oxidoreductase;
5-195 2.51e-05

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 44.36  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGLWKVHIIGSNANRGEEAAASLRNTIFhQVDVTKYEQQGAAFDkifnEEKRLDFVLANA 84
Cdd:PRK12742   9 VLVLGGSRGIGAAIVRRFVTDGANVRFTYAGSKDAAERLAQETGATAV-QTDSADRDAVIDVVR----KSGALDILVVNA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   85 GIAedtamfFASHPTGIPPPpDMTGLTDINFTGAIYTSYLAMhyfRRSPEktkGNRHLIIMSSIGGLYPCAHTPVYSATK 164
Cdd:PRK12742  84 GIA------VFGDALELDAD-DIDRLFKINIHAPYHASVEAA---RQMPE---GGRIIIIGSVNGDRMPVAGMAAYAASK 150

                        170       180       190
                 ....*....|....*....|....*....|.
gi 83775806  165 HGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT 195
Cdd:PRK12742 151 SALQGMARGLARDFGPRGITINVVQPGPIDT 181
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 5-196 4.05e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 44.12  E-value: 4.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGlwkVHIIGSNANRGEEAAASLRntiFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLANA 84
Cdd:PRK06523  12 ALVTGGTKGIGAATVARLLEAG---ARVVTTARSRPDDLPEGVE---FVAADLTTAEGCAAVARAVLERLGGVDILVHVL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   85 GIAEdtamffaSHPTGIPPPPDMTGLT--DINFTGAIYTSYL---AMhyfrrspeKTKGNRHLIIMSSIGGLYPC-AHTP 158
Cdd:PRK06523  86 GGSS-------APAGGFAALTDEEWQDelNLNLLAAVRLDRAllpGM--------IARGSGVIIHVTSIQRRLPLpESTT 150

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 83775806  159 VYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTP 196
Cdd:PRK06523 151 AYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETE 188
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 121-207 4.74e-05

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 43.91  E-value: 4.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  121 TSYLAMHYFRRSPEKTKGNrhLIIMSSIGGLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTT 200
Cdd:PRK12748 130 TMLLSSAFAKQYDGKAGGR--IINLTSGQSLGPMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGWITE 207

                         90
                 ....*....|.
gi 83775806  201 ELQAF----FP 207
Cdd:PRK12748 208 ELKHHlvpkFP 218
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 4-196 7.79e-05

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 43.13  E-value: 7.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLWKV--HIIGSNANRGEEAAASLR-NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFV 80
Cdd:PRK07097  12 IALITGASYGIGFAIAKAYAKAGATIVfnDINQELVDKGLAAYRELGiEAHGYVCDVTDEDGVQAMVSQIEKEVGVIDIL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   81 LANAGIAEDTAMFfashptgippppDMTG-----LTDINFTGAIYTSYLAMhyfrrsPEKTKGNRHLII-----MSSIGG 150
Cdd:PRK07097  92 VNNAGIIKRIPML------------EMSAedfrqVIDIDLNAPFIVSKAVI------PSMIKKGHGKIInicsmMSELGR 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 83775806  151 LYPCAhtpvYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTP 196
Cdd:PRK07097 154 ETVSA----YAAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIATP 195
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
 6-97 8.05e-05

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP 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 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: 187657 [Multi-domain]  Cd Length: 452  Bit Score: 43.59  E-value: 8.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   6 LITGGTSGMGLDVAQELDKTGLWKVHIIGSNANRGEEAAASLRN-----TIFH--QVDVTKYEQQGAAFDKIFNEEK--- 75
Cdd:cd08954 222 LITGGSGGLGLEILKWLVKRGAVENIIILSRSGMKWELELLIREwksqnIKFHfvSVDVSDVSSLEKAINLILNAPKigp 301

                        90       100
                ....*....|....*....|....*..
gi 83775806  76 -----RLDFVLANAGIAEDTAMFFASH 97
Cdd:cd08954 302 iggifHLAFVLIDKVLEIDTESLFISV 328
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 4-205 8.76e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 42.99  E-value: 8.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK07478   8 VAIITGASSGIGRAAAKLFAREGA-KVVVGARRQAELDQLVAEIRaeggEAVALAGDVRDEAYAKALVALAVERFGGLDI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGIAEDTAmffashPTGIPPPPDMTGLTDINFTGAiytsYLAMHYfrRSPEKTK-GNRHLIIMSSIGGlypcaHT- 157
Cdd:PRK07478  87 AFNNAGTLGEMG------PVAEMSLEGWRETLATNLTSA----FLGAKH--QIPAMLArGGGSLIFTSTFVG-----HTa 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 83775806  158 -----PVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLM-----TTELQAF 205
Cdd:PRK07478 150 gfpgmAAYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGramgdTPEALAF 207
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 6-85 1.11e-04

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 42.58  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   6 LITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASL------RNTIFHQVDVTKyEQQGAAFDKIFNEE-KRLD 78
Cdd:cd09808   5 LITGANSGIGKAAALAIAKRG-GTVHMVCRNQTRAEEARKEIetesgnQNIFLHIVDMSD-PKQVWEFVEEFKEEgKKLH 82


                ....*..
gi 83775806  79 FVLANAG 85
Cdd:cd09808  83 VLINNAG 89
PRK07775 PRK07775
SDR family oxidoreductase;
5-195 1.60e-04

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 42.43  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLR----NTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFV 80
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAG-FPVALGARRVEKCEELVDKIRadggEAVAFPLDVTDPDSVKSFVAQAEEALGEIEVL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   81 LANAGiaeDTAmFFASHPTGippPPDMTGLTDINFTGA--IYTSYL-AMhyfrrsPEKTKGNrhLIIMSSIGGLYPCAHT 157
Cdd:PRK07775  92 VSGAG---DTY-FGKLHEIS---TEQFESQVQIHLVGAnrLATAVLpGM------IERRRGD--LIFVGSDVALRQRPHM 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 83775806  158 PVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLT 195
Cdd:PRK07775 157 GAYGAAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLT 194
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 6-92 2.32e-04

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 40.93  E-value: 2.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806      6 LITGGTSGMGLDVAQELDKTGLWKVHIIGSNANRGEEAAASLR-------NTIFHQVDVTKYEQQGAAFDKIFNEEKRLD 78
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARRLVLLSRSGPDAPGAAALLAeleaagaRVTVVACDVADRDALAAVLAAIPAVEGPLT 83

                           90
                   ....*....|....
gi 83775806     79 FVLANAGIAEDTAM 92
Cdd:smart00822  84 GVIHAAGVLDDGVL 97
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 4-235 3.00e-04

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 41.37  E-value: 3.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRN----TIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK06113  13 CAIITGAGAGIGKEIAITFATAGA-SVVVSDINADAANHVVDEIQQlggqAFACRCDITSEQELSALADFALSKLGKVDI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   80 VLANAGiaedtamffashpTGIPPPPDMTGLT-----DINFTGAIYTSYLAMHYFrrspEKTKGNRHLIImSSIGGLYPC 154
Cdd:PRK06113  92 LVNNAG-------------GGGPKPFDMPMADfrrayELNVFSFFHLSQLVAPEM----EKNGGGVILTI-TSMAAENKN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  155 AHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGV--------VLTPLMTTELQAFFPEKIVMKMSDVTNVVLKL-- 224
Cdd:PRK06113 154 INMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAiltdalksVITPEIEQKMLQHTPIRRLGQPQDIANAALFLcs 233

                        250
                 ....*....|....*.
gi 83775806  225 -----ISGTEVTDSNG 235
Cdd:PRK06113 234 paaswVSGQILTVSGG 249
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 129-203 3.60e-04

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 40.92  E-value: 3.60e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83775806  129 FRRSPEKTKGNRhLIIMSSIGGLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMTTELQ 203
Cdd:PRK12859 138 FARGFDKKSGGR-IINMTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGWMTEEIK 211
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 4-202 5.02e-04

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 40.83  E-value: 5.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTG-LWKVHIiGSNANRGEEAAASLRNTIFHQVDVTKYEQQGAAFDKIFNE--------- 73
Cdd:PRK12747   6 VALVTGASRGIGRAIAKRLANDGaLVAIHY-GNRKEEAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSldnelqnrt 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   74 -EKRLDFVLANAGIA------EDTAMFFAShptgippppdmtgLTDINFTGAIYTSYLAMHYFRrspektkGNRHLIIMS 146
Cdd:PRK12747  85 gSTKFDILINNAGIGpgafieETTEQFFDR-------------MVSVNAKAPFFIIQQALSRLR-------DNSRIINIS 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 83775806  147 SIGGLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPlMTTEL 202
Cdd:PRK12747 145 SAATRISLPDFIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTD-MNAEL 199
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 4-206 1.19e-03

3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other enzymes) catalyzes NADP-dependent sterol C-4 demethylation, as part of steroid biosynthesis. 3-keto reductase is a classical SDR, with a well conserved canonical active site tetrad and fairly well conserved characteristic 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: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 39.68  E-value: 1.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQ----ELDKTGLWKVHIIGSNANRGEEAAASLRNTI--------FHQVDVTKYEQQGAAFDKIF 71
Cdd:cd08941   3 VVLVTGANSGLGLAICErllaEDDENPELTLILACRNLQRAEAACRALLASHpdarvvfdYVLVDLSNMVSVFAAAKELK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  72 NEEKRLDFVLANAGIAEDTA--------------MFFASHPT------GI------PPPPDMTGLTDINFTGAIYTSYLA 125
Cdd:cd08941  83 KRYPRLDYLYLNAGIMPNPGidwigaikevltnpLFAVTNPTykiqaeGLlsqgdkATEDGLGEVFQTNVFGHYYLIREL 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806 126 MHYFRRSPEKTKgnrhLIIMSSIGGL--------YPCAHTPV-YSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTP 196
Cdd:cd08941 163 EPLLCRSDGGSQ----IIWTSSLNASpkyfsledIQHLKGPApYSSSKYLVDLLSLALNRKFNKLGVYSYVVHPGICTTN 238

                       250
                ....*....|
gi 83775806 197 LMTTELQAFF 206
Cdd:cd08941 239 LTYGILPPFT 248
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 4-91 1.43e-03

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: 39.66  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLWKVHIIG------------SNANRGEEAAASLRntiFHQVDVTKYEQQGAAFDKIF 71
Cdd:cd08953 207 VYLVTGGAGGIGRALARALARRYGARLVLLGrsplppeeewkaQTLAALEALGARVL---YISADVTDAAAVRRLLEKVR 283

                        90       100
                ....*....|....*....|
gi 83775806  72 NEEKRLDFVLANAGIAEDTA 91
Cdd:cd08953 284 ERYGAIDGVIHAAGVLRDAL 303
PRK05693 PRK05693
SDR family oxidoreductase;
4-85 1.64e-03

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 39.00  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlWKVHIIGSNANRGEEAAASLRNTIfhQVDVTKYEQQGAAFDKIFNEEKRLDFVLAN 83
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAG-YEVWATARKAEDVEALAAAGFTAV--QLDVNDGAALARLAEELEAEHGGLDVLINN 79


                 ..
gi 83775806   84 AG 85
Cdd:PRK05693  80 AG 81
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 5-84 2.52e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 38.40  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    5 ALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNTIFHQV----DVTKYEQQGAAFDKIFNEEKRLDFV 80
Cdd:PRK07576  12 VVVVGGTSGINLGIAQAFARAGA-NVAVASRSQEKVDAAVAQLQQAGPEGLgvsaDVRDYAAVEAAFAQIADEFGPIDVL 90


                 ....
gi 83775806   81 LANA 84
Cdd:PRK07576  91 VSGA 94
PRK07806 PRK07806
SDR family oxidoreductase;
4-92 2.94e-03

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 38.16  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLWKVHIIGSNANRGEEAAASLRN----TIFHQVDVTKYEQQGAAFDKIFNEEKRLDF 79
Cdd:PRK07806   8 TALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPRANKVVAEIEAaggrASAVGADLTDEESVAALMDTAREEFGGLDA 87

                         90
                 ....*....|....*....
gi 83775806   80 VLANA------GIAEDTAM 92
Cdd:PRK07806  88 LVLNAsggmesGMDEDYAM 106
PRK09730 PRK09730
SDR family oxidoreductase;
4-86 3.02e-03

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 38.29  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGlwkvHIIGSNANRGEEAAASLRNTIFH--------QVDVTKYEQQGAAFDKIFNEEK 75
Cdd:PRK09730   3 IALVTGGSRGIGRATALLLAQEG----YTVAVNYQQNLHAAQEVVNLITQaggkafvlQADISDENQVVAMFTAIDQHDE 78

                         90
                 ....*....|.
gi 83775806   76 RLDFVLANAGI 86
Cdd:PRK09730  79 PLAALVNNAGI 89
PLN00015 PLN00015
protochlorophyllide reductase
 6-91 3.08e-03

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 38.53  E-value: 3.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    6 LITGGTSGMGLDVAQELDKTGLWKVHIIGSNANRGEEAAASL-----RNTIFHqVDVTKYEQQGAAFDKIFNEEKRLDFV 80
Cdd:PLN00015   1 IITGASSGLGLATAKALAETGKWHVVMACRDFLKAERAAKSAgmpkdSYTVMH-LDLASLDSVRQFVDNFRRSGRPLDVL 79

                         90
                 ....*....|.
gi 83775806   81 LANAGIAEDTA 91
Cdd:PLN00015  80 VCNAAVYLPTA 90
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 4-199 3.09e-03

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: 38.33  E-value: 3.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLRNT--------IFHQVDVTKYEQQGAAfDKIFNEEK 75
Cdd:cd05340   6 IILVTGASDGIGREAALTYARYGA-TVILLGRNEEKLRQVADHINEEggrqpqwfILDLLTCTSENCQQLA-QRIAVNYP 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  76 RLDFVLANAGIAEDTAmffashPTGIPPPPDMTGLTDINFTGAIYTSYLAMHYFRRSPEKTkgnrhLIIMSSIGGLYPCA 155
Cdd:cd05340  84 RLDGVLHNAGLLGDVC------PLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGS-----LVFTSSSVGRQGRA 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 83775806 156 HTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCPGVVLTPLMT 199
Cdd:cd05340 153 NWGAYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRA 196
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
41-199 5.35e-03

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 37.61  E-value: 5.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806   41 EEAAASLRNTIFHQVDVTKYEQQGAAFDKIFNEEKRLDFVLANagIAedtamfFAshptgipPPPDMTG-LTDINFTGAI 119
Cdd:PRK07533  53 EPLAEELDAPIFLPLDVREPGQLEAVFARIAEEWGRLDFLLHS--IA------FA-------PKEDLHGrVVDCSREGFA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806  120 ytsyLAM----HYFRR-----SPEKTKGNRhLIIMSSIGGLYPCAHTPVYSATKHGLVGFTRSVGKRLLDEGVKVNTVCP 190
Cdd:PRK07533 118 ----LAMdvscHSFIRmarlaEPLMTNGGS-LLTMSYYGAEKVVENYNLMGPVKAALESSVRYLAAELGPKGIRVHAISP 192


                 ....*....
gi 83775806  191 GvvltPLMT 199
Cdd:PRK07533 193 G----PLKT 197
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 4-86 6.59e-03

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 37.31  E-value: 6.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83775806    4 VALITGGTSGMGLDVAQELDKTGLwKVHIIGSNANRGEEAAASLR------NTIFHQVDVTKYEQQGAAFDKIFNEEKRL 77
Cdd:PRK06197  18 VAVVTGANTGLGYETAAALAAKGA-HVVLAVRNLDKGKAAAARITaatpgaDVTLQELDLTSLASVRAAADALRAAYPRI 96


                 ....*....
gi 83775806   78 DFVLANAGI 86
Cdd:PRK06197  97 DLLINNAGV 105
 
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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