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Conserved domains on  [gi|37590327|gb|AAH59453|]
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Retinol dehydrogenase 8 [Danio rerio]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10176850)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase may catalyze isomerization, decarboxylation, epimerization, C=N bond reduction, dehydration, dehalogenation, enoyl-CoA reduction, and/or carbonyl-alcohol oxidoreduction; classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue; similar to 17-beta-hydroxysteroid dehydrogenase type 1 and retinol dehydrogenase 8

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 8-265 3.07e-178

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: 492.75  E-value: 3.07e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRHI 87
Cdd:cd09806   1 TVVLITGCSSGIGLHLAVRLASDPSKRFKVYATMRDLKKKGRLWEAAGALAGGTLETLQLDVCDSKSVAAAVERVTERHV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  88 DVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAIEG 167
Cdd:cd09806  81 DVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFALEG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327 168 FCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYPGADPDTVRYFKDVYVPSSIDIFEAMGQTPDDIAKCTKK 247
Cdd:cd09806 161 LCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSPEEVLDRTADDITTFHFFYQYLAHSKQVFREAAQNPEEVAEVFLT 240

                       250
                ....*....|....*...
gi 37590327 248 VIETSQPRFRNLTNSLYT 265
Cdd:cd09806 241 AIRAPKPPLRYFTNERYL 258
 
Name Accession Description Interval E-value
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 8-265 3.07e-178

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: 492.75  E-value: 3.07e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRHI 87
Cdd:cd09806   1 TVVLITGCSSGIGLHLAVRLASDPSKRFKVYATMRDLKKKGRLWEAAGALAGGTLETLQLDVCDSKSVAAAVERVTERHV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  88 DVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAIEG 167
Cdd:cd09806  81 DVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFALEG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327 168 FCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYPGADPDTVRYFKDVYVPSSIDIFEAMGQTPDDIAKCTKK 247
Cdd:cd09806 161 LCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSPEEVLDRTADDITTFHFFYQYLAHSKQVFREAAQNPEEVAEVFLT 240

                       250
                ....*....|....*...
gi 37590327 248 VIETSQPRFRNLTNSLYT 265
Cdd:cd09806 241 AIRAPKPPLRYFTNERYL 258
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
7-216 2.05e-72

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 223.98  E-value: 2.05e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   7 QKVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDlkkKDRLVEAAGEV--YGQTLTLLPLDICSDESVRQCVNSVKD 84
Cdd:COG0300   5 GKTVLITGASSGIGRALARALAA---RGARVVLVARD---AERLEALAAELraAGARVEVVALDVTDPDAVAALAEAVLA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  85 RH--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASK 162
Cdd:COG0300  79 RFgpIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASK 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 37590327 163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMeevAKMEYPGADPDTV 216
Cdd:COG0300 159 AALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAG---APAGRPLLSPEEV 209
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 7-266 1.64e-59

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 191.65  E-value: 1.64e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDLKKKDRLveaagevygQTLTLLPLDICSDESVRQCVNSVKDR- 85
Cdd:PRK06179   4 SKVALVTGASSGIGRATAEKLAR---AGYRVFGTSRNPARAAPI---------PGVELLELDVTDDASVQAAVDEVIARa 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 -HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:PRK06179  72 gRIDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKHA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKM-EYpgadpDTVR-YFKDVyvpssidIFEAM--GQTPDD 240
Cdd:PRK06179 152 VEGYSESLDHEVRQFGIRVSLVEPAYTKTNFDANAPEPDSPLaEY-----DRERaVVSKA-------VAKAVkkADAPEV 219

                        250       260
                 ....*....|....*....|....*.
gi 37590327  241 IAKCTKKVIETSQPRFRnltnslYTP 266
Cdd:PRK06179 220 VADTVVKAALGPWPKMR------YTA 239
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 8-207 2.08e-53

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 173.57  E-value: 2.08e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327     8 KVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDlkkKDRLVEAAGEV--YGQTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAK---EGAKVVLVDRS---EEKLEAVAKELgaLGGKALFIQGDVTDRAQVKALVEQAVER 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    86 H--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:pfam00106  75 LgrLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 37590327   164 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTEfetkMMEEVAKME 207
Cdd:pfam00106 155 AVIGFTRSLALELAPHGIRVNAVAPGGVDTD----MTKELREDE 194
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 8-114 1.82e-08

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: 53.25  E-value: 1.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327      8 KVVLITGCSSGIGLRIAVLLARDEQKryHVIATMR---DLKKKDRLVEAAGEvYGQTLTLLPLDICSDESVRQCVNSVKD 84
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGAR--RLVLLSRsgpDAPGAAALLAELEA-AGARVTVVACDVADRDALAAVLAAIPA 77

                           90       100       110
                   ....*....|....*....|....*....|..
gi 37590327     85 RH--IDVLINNAGVGLLGPVESISMDEMKRVF 114
Cdd:smart00822  78 VEgpLTGVIHAAGVLDDGVLASLTPERFAAVL 109
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 9-221 1.60e-05

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 45.67  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327     9 VVLITGCSSGIGLRIAV-LLARDEQKRYHVIATMRDLKK-KDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSV---- 82
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQeLAKCLKSPGSVLVLSARNDEAlRQLKAEIGAERSGLRVVRVSLDLGAEAGLEQLLKALrelp 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    83 --KDRHIDVLINNAG-VGLLGPVE-SIS-MDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIII--MSSVMGLQGVVFN 155
Cdd:TIGR01500  82 rpKGLQRLLLINNAGtLGDVSKGFvDLSdSTQVQNYWALNLTSMLCLTSSVLKAFKDSPGLNRTVvnISSLCAIQPFKGW 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37590327   156 DVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEvakmeypGADPDTVRYFKD 221
Cdd:TIGR01500 162 ALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQQVREE-------SVDPDMRKGLQE 220
 
Name Accession Description Interval E-value
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 8-265 3.07e-178

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: 492.75  E-value: 3.07e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRHI 87
Cdd:cd09806   1 TVVLITGCSSGIGLHLAVRLASDPSKRFKVYATMRDLKKKGRLWEAAGALAGGTLETLQLDVCDSKSVAAAVERVTERHV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  88 DVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAIEG 167
Cdd:cd09806  81 DVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFALEG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327 168 FCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYPGADPDTVRYFKDVYVPSSIDIFEAMGQTPDDIAKCTKK 247
Cdd:cd09806 161 LCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSPEEVLDRTADDITTFHFFYQYLAHSKQVFREAAQNPEEVAEVFLT 240

                       250
                ....*....|....*...
gi 37590327 248 VIETSQPRFRNLTNSLYT 265
Cdd:cd09806 241 AIRAPKPPLRYFTNERYL 258
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 8-262 2.03e-82

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: 249.46  E-value: 2.03e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDLKKkdrlVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAA---QGYRVIATARNPDK----LESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFg 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 -IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:cd05374  74 rIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAAL 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327 166 EGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYPGAdpdtvryfkdvYVPSSIDIFEAM------GQTPD 239
Cdd:cd05374 154 EALSESLRLELAPFGIKVTIIEPGPVRTGFADNAAGSALEDPEISP-----------YAPERKEIKENAagvgsnPGDPE 222

                       250       260
                ....*....|....*....|...
gi 37590327 240 DIAKCTKKVIETSQPRFRNLTNS 262
Cdd:cd05374 223 KVADVIVKALTSESPPLRYFLGS 245
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
7-216 2.05e-72

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 223.98  E-value: 2.05e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   7 QKVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDlkkKDRLVEAAGEV--YGQTLTLLPLDICSDESVRQCVNSVKD 84
Cdd:COG0300   5 GKTVLITGASSGIGRALARALAA---RGARVVLVARD---AERLEALAAELraAGARVEVVALDVTDPDAVAALAEAVLA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  85 RH--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASK 162
Cdd:COG0300  79 RFgpIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASK 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 37590327 163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMeevAKMEYPGADPDTV 216
Cdd:COG0300 159 AALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAG---APAGRPLLSPEEV 209
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-255 9.26e-68

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: 211.58  E-value: 9.26e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   1 MASGGgqKVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDlkkKDRLVEAAGEVYGQTLTLlPLDICSDESVRQCVN 80
Cdd:COG4221   1 MSDKG--KVALITGASSGIGAATARALAAAG---ARVVLAARR---AERLEALAAELGGRALAV-PLDVTDEAAVEAAVA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  81 SVKDR--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVY 158
Cdd:COG4221  72 AAVAEfgRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVY 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327 159 TASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAkmeypgadpdtvRYFKDVYVPssidiFEAMgqTP 238
Cdd:COG4221 152 AATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDA------------EAAAAVYEG-----LEPL--TP 212

                       250
                ....*....|....*..
gi 37590327 239 DDIAKCTKKVIetSQPR 255
Cdd:COG4221 213 EDVAEAVLFAL--TQPA 227
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 10-213 1.52e-59

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: 190.57  E-value: 1.52e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  10 VLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDLKKKDRLVEAAGEvyGQTLTLLPLDICSDESVRQCVNSVKDRH--I 87
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAR---EGAKVVLADRNEEALAELAAIEAL--GGNAVAVQADVSDEEDVEALVEEALEEFgrL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  88 DVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAIEG 167
Cdd:cd05233  76 DILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEG 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 37590327 168 FCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYPGADP 213
Cdd:cd05233 156 LTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAAIP 201
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 7-266 1.64e-59

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 191.65  E-value: 1.64e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDLKKKDRLveaagevygQTLTLLPLDICSDESVRQCVNSVKDR- 85
Cdd:PRK06179   4 SKVALVTGASSGIGRATAEKLAR---AGYRVFGTSRNPARAAPI---------PGVELLELDVTDDASVQAAVDEVIARa 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 -HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:PRK06179  72 gRIDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKHA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKM-EYpgadpDTVR-YFKDVyvpssidIFEAM--GQTPDD 240
Cdd:PRK06179 152 VEGYSESLDHEVRQFGIRVSLVEPAYTKTNFDANAPEPDSPLaEY-----DRERaVVSKA-------VAKAVkkADAPEV 219

                        250       260
                 ....*....|....*....|....*.
gi 37590327  241 IAKCTKKVIETSQPRFRnltnslYTP 266
Cdd:PRK06179 220 VADTVVKAALGPWPKMR------YTA 239
PRK06914 PRK06914
SDR family oxidoreductase;
7-257 1.09e-57

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 187.15  E-value: 1.09e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDLKKKDRLVEAAGEVYGQT-LTLLPLDICSDESVrQCVNSVKDR 85
Cdd:PRK06914   3 KKIAIVTGASSGFGLLTTLELAK---KGYLVIATMRNPEKQENLLSQATQLNLQQnIKVQQLDVTDQNSI-HNFQLVLKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 H--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:PRK06914  79 IgrIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  164 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVakMEYPGADPDTVRYFKDV--YVPSSIDIFEAmgqtPDDI 241
Cdd:PRK06914 159 ALEGFSESLRLELKPFGIDVALIEPGSYNTNIWEVGKQLA--ENQSETTSPYKEYMKKIqkHINSGSDTFGN----PIDV 232

                        250
                 ....*....|....*.
gi 37590327  242 AKCTKKVIETSQPRFR 257
Cdd:PRK06914 233 ANLIVEIAESKRPKLR 248
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 8-207 2.08e-53

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 173.57  E-value: 2.08e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327     8 KVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDlkkKDRLVEAAGEV--YGQTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAK---EGAKVVLVDRS---EEKLEAVAKELgaLGGKALFIQGDVTDRAQVKALVEQAVER 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    86 H--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:pfam00106  75 LgrLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 37590327   164 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTEfetkMMEEVAKME 207
Cdd:pfam00106 155 AVIGFTRSLALELAPHGIRVNAVAPGGVDTD----MTKELREDE 194
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 8-242 1.39e-52

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: 173.05  E-value: 1.39e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDlkkKDRLVEAAGEV--YGQTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:COG1028   7 KVALVTGGSSGIGRAIARALAAEG---ARVVITDRD---AEALEAAAAELraAGGRALAVAADVTDEAAVEALVAAAVAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 H--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:COG1028  81 FgrLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327 164 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTEfetkMMEEVAkmeypgADPDTVRYFKDvYVPssidifeaMGQ--TPDDI 241
Cdd:COG1028 161 AVVGLTRSLALELAPRGIRVNAVAPGPIDTP----MTRALL------GAEEVREALAA-RIP--------LGRlgTPEEV 221


                .
gi 37590327 242 A 242
Cdd:COG1028 222 A 222
PRK06182 PRK06182
short chain dehydrogenase; Validated
 6-271 3.81e-50

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 167.44  E-value: 3.81e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    6 GQKVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDLKKKDRLVEAAGEVygqtltlLPLDICSDESVRQCVNSVKDR 85
Cdd:PRK06182   2 QKKVALVTGASSGIGKATARRLAAQG---YTVYGAARRVDKMEDLASLGVHP-------LSLDVTDEASIKAAVDTIIAE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 H--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:PRK06182  72 EgrIDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKF 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  164 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYPGADPDTVRYFKDVYVPSSIDifeAMGQTPDDIAK 243
Cdd:PRK06182 152 ALEGFSDALRLEVAPFGIDVVVIEPGGIKTEWGDIAADHLLKTSGNGAYAEQAQAVAASMRSTYGS---GRLSDPSVIAD 228

                        250       260
                 ....*....|....*....|....*...
gi 37590327  244 CTKKVIETSQPRFRNLTNSLYTPIVAMK 271
Cdd:PRK06182 229 AISKAVTARRPKTRYAVGFGAKPLIFLR 256
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 8-202 1.62e-49

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 166.24  E-value: 1.62e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVL-LARDeqkrYHVIATMRDLKKKDRLVEAAGE-VYGqtltlLPLDICSDESVRQCVNSVKDR 85
Cdd:PRK06180   5 KTWLITGVSSGFGRALAQAaLAAG----HRVVGTVRSEAARADFEALHPDrALA-----RLLDVTDFDAIDAVVADAEAT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 H--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:PRK06180  76 FgpIDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKF 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 37590327  164 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEE 202
Cdd:PRK06180 156 ALEGISESLAKEVAPFGIHVTAVEPGSFRTDWAGRSMVR 194
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 8-208 3.74e-46

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: 156.59  E-value: 3.74e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:cd05332   4 KVVIITGASSGIGEELAYHLAR---LGARLVLSARREERLEEVKSECLELGAPSPHVVPLDMSDLEDAEQVVEEALKLFg 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 -IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:cd05332  81 gLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHAL 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 37590327 166 EGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEY 208
Cdd:cd05332 161 QGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNALSGDGSMSA 203
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 7-207 4.65e-45

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 154.43  E-value: 4.65e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAV-LLARDEQkryhVIATMRDLKKKDRLVEaageVYGQTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:PRK08263   3 EKVWFITGASRGFGRAWTEaALERGDR----VVATARDTATLADLAE----KYGDRLLPLALDVTDRAAVFAAVETAVEH 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 --HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:PRK08263  75 fgRLDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKW 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 37590327  164 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKME 207
Cdd:PRK08263 155 ALEGMSEALAQEVAEFGIKVTLVEPGGYSTDWAGTSAKRATPLD 198
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 8-267 2.37e-43

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


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 149.35  E-value: 2.37e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRdlkKKDRLVEAAGEV---YGQTLTLLPLDICSDESVRQCVNSVKD 84
Cdd:cd05346   1 KTVLITGASSGIGEATARRFA---KAGAKLILTGR---RAERLQELADELgakFPVKVLPLQLDVSDRESIEAALENLPE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  85 --RHIDVLINNAGVGL-LGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTAS 161
Cdd:cd05346  75 efRDIDILVNNAGLALgLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCAT 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327 162 KFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFET---KMMEEVAKMEYPGADPdtvryfkdvyvpssidifeamgQTP 238
Cdd:cd05346 155 KAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETEFSLvrfHGDKEKADKVYEGVEP----------------------LTP 212

                       250       260
                ....*....|....*....|....*....
gi 37590327 239 DDIAKCTkkVIETSQPRFRNLTNSLYTPI 267
Cdd:cd05346 213 EDIAETI--LWVASRPAHVNINDIEIMPV 239
PRK05993 PRK05993
SDR family oxidoreductase;
6-195 1.15e-41

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 145.55  E-value: 1.15e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    6 GQKVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDLKKKDRLvEAAGevygqtLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:PRK05993   3 MKRSILITGCSSGIGAYCARALQSDG---WRVFATCRKEEDVAAL-EAEG------LEAFQLDYAEPESIAALVAQVLEL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 ---HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASK 162
Cdd:PRK05993  73 sggRLDALFNNGAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAYNASK 152

                        170       180       190
                 ....*....|....*....|....*....|...
gi 37590327  163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEF 195
Cdd:PRK05993 153 FAIEGLSLTLRMELQGSGIHVSLIEPGPIETRF 185
PRK08017 PRK08017
SDR family oxidoreductase;
7-195 6.11e-40

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 140.61  E-value: 6.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLardEQKRYHVIATMRdlKKKDrlVEAAGEVyGQTLTLLPLDicSDESVRQCVNSV---K 83
Cdd:PRK08017   2 QKSVLITGCSSGIGLEAALEL---KRRGYRVLAACR--KPDD--VARMNSL-GFTGILLDLD--DPESVERAADEVialT 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   84 DRHIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:PRK08017  72 DNRLYGLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKY 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 37590327  164 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTEF 195
Cdd:PRK08017 152 ALEAWSDALRMELRHSGIKVSLIEPGPIRTRF 183
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 8-206 2.33e-39

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: 138.54  E-value: 2.33e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKKKDRLVEAAGEVY---GQTLTLLPLDICSDESVRQCVNSV-- 82
Cdd:cd08939   2 KHVLITGGSSGIGKALAKELV---KEGANVIIVARSESKLEEAVEEIEAEAnasGQKVSYISADLSDYEEVEQAFAQAve 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  83 KDRHIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASK 162
Cdd:cd08939  79 KGGPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSK 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 37590327 163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEF----------ETKMMEEVAKM 206
Cdd:cd08939 159 FALRGLAESLRQELKPYNIRVSVVYPPDTDTPGfeeenktkpeETKAIEGSSGP 212
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-202 7.45e-38

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 134.97  E-value: 7.45e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEqkrYHV-IATMRDLKKKDRLVEAAGEVYGQTLTLlPLDICSDESVRQCVNSVKDRH 86
Cdd:PRK05565   6 KVAIVTGASGGIGRAIAELLAKEG---AKVvIAYDINEEAAQELLEEIKEEGGDAIAV-KADVSSEEDVENLVEQIVEKF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 --IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:PRK05565  82 gkIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKGA 161

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 37590327  165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEE 202
Cdd:PRK05565 162 VNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEE 199
PRK09291 PRK09291
SDR family oxidoreductase;
7-201 1.63e-37

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 134.36  E-value: 1.63e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDLKKKDRLVEAAGEVyGQTLTLLPLDICSDESVRQCVNSvkdrH 86
Cdd:PRK09291   2 SKTILITGAGSGFGREVALRLAR---KGHNVIAGVQIAPQVTALRAEAARR-GLALRVEKLDLTDAIDRAQAAEW----D 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAIE 166
Cdd:PRK09291  74 VDVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHALE 153

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 37590327  167 GFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMME 201
Cdd:PRK09291 154 AIAEAMHAELKPFGIQVATVNPGPYLTGFNDTMAE 188
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 8-257 4.64e-37

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: 132.10  E-value: 4.64e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDLKKKDRLVEAAGEVYgqtltLLPLDICSDESVRQCVNSVKDR-- 85
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDG---YRVSLGLRNPEDLAALSASGGDVE-----AVPYDARDPEDARALVDALRDRfg 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:cd08932  73 RIDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFAL 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327 166 EGFCESMAVQLLKFNVKLSLIEPGPVhtefETKMMEEVAKMEYPGAdpdtvryfkdvyvpssidifEAMGQtPDDIAKCT 245
Cdd:cd08932 153 RALAHALRQEGWDHGVRVSAVCPGFV----DTPMAQGLTLVGAFPP--------------------EEMIQ-PKDIANLV 207

                       250
                ....*....|..
gi 37590327 246 KKVIETSQPRFR 257
Cdd:cd08932 208 RMVIELPENITS 219
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
8-206 9.45e-37

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 131.82  E-value: 9.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDLKK----KDRLVEAAGEVYgqtltLLPLDICSDESVRQCVNSVK 83
Cdd:PRK05653   6 KTALVTGASRGIGRAIALRLAADG---AKVVIYDSNEEAaealAAELRAAGGEAR-----VLVFDVSDEAAVRALIEAAV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   84 DRH--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTAS 161
Cdd:PRK05653  78 EAFgaLDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 37590327  162 KFAIEGFCESMAVQLLKFNVKLSLIEPGPVhtefETKMMEEVAKM 206
Cdd:PRK05653 158 KAGVIGFTKALALELASRGITVNAVAPGFI----DTDMTEGLPEE 198
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-242 1.66e-36

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 131.14  E-value: 1.66e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRdlKKKDRLVEAAGEV--YGQTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:PRK12825   7 RVALVTGAARGLGRAIALRLARAG---ADVVVHYR--SDEEAAEELVEAVeaLGRRAQAVQADVTDKAALEAAVAAAVER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 H--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:PRK12825  82 FgrIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  164 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTEfetkMMEEVAKMEypgadpdtvRYFKDVYVPssidifeaMGQ--TPDDI 241
Cdd:PRK12825 162 GLVGLTKALARELAEYGITVNMVAPGDIDTD----MKEATIEEA---------REAKDAETP--------LGRsgTPEDI 220


                 .
gi 37590327  242 A 242
Cdd:PRK12825 221 A 221
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 8-208 1.71e-36

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: 131.12  E-value: 1.71e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQKRyhVIATMRdlkkKDRLVEAAGEVYGQTLTLLPL--DICSDESVRQCVNSVKDR 85
Cdd:cd08934   4 KVALVTGASSGIGEATARALAAEGAAV--AIAARR----VDRLEALADELEAEGGKALVLelDVTDEQQVDAAVERTVEA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 --HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:cd08934  78 lgRLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKF 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 37590327 164 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEY 208
Cdd:cd08934 158 GVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHITHTITKEAY 202
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-204 2.08e-36

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 130.96  E-value: 2.08e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKKKDRLVEAAGEvYGQTLTLLPLDICSDESVRQCVNSVKDR-- 85
Cdd:PRK07666   8 KNALITGAGRGIGRAVAIALA---KEGVNVGLLARTEENLKAVAEEVEA-YGVKVVIATADVSDYEEVTAAIEQLKNElg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:PRK07666  84 SIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKFGV 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 37590327  166 EGFCESMAVQLLKFNVKLSLIEPGPVHTEF----------ETKMM--EEVA 204
Cdd:PRK07666 164 LGLTESLMQEVRKHNIRVTALTPSTVATDMavdlgltdgnPDKVMqpEDLA 214
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 8-195 5.43e-36

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: 129.28  E-value: 5.43e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQkrYHVIATMRDLkkkDRLVEAAGEVYGQTLTLLP--LDICSDESVRQCVNSVKDR 85
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGP--GTVILTARDV---ERGQAAVEKLRAEGLSVRFhqLDVTDDASIEAAADFVEEK 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 H--IDVLINNAGVGLLGPVESISMDE-MKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVvfndVYTASK 162
Cdd:cd05324  76 YggLDILVNNAGIAFKGFDDSTPTREqARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLTS----AYGVSK 151

                       170       180       190
                ....*....|....*....|....*....|...
gi 37590327 163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEF 195
Cdd:cd05324 152 AALNALTRILAKELKETGIKVNACCPGWVKTDM 184
PRK06181 PRK06181
SDR family oxidoreductase;
8-211 6.25e-36

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 130.10  E-value: 6.25e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLlPLDICSDESVRQCVNSVKDR-- 85
Cdd:PRK06181   2 KVVIITGASEGIGRALAVRLA---RAGAQLVLAARNETRLASLAQELADHGGEALVV-PTDVSDAEACERLIEAAVARfg 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 HIDVLINNAGVGLLGPVESIS-MDEMKRVFETNFFGTVRMIKEVMPDMKKRQaGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:PRK06181  78 GIDILVNNAGITMWSRFDELTdLSVFERVMRVNYLGAVYCTHAALPHLKASR-GQIVVVSSLAGLTGVPTRSGYAASKHA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37590327  165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTEF------------------ETKMM--EEVAKMEYPGA 211
Cdd:PRK06181 157 LHGFFDSLRIELADDGVAVTVVCPGFVATDIrkraldgdgkplgkspmqESKIMsaEECAEAILPAI 223
PRK07326 PRK07326
SDR family oxidoreductase;
1-195 3.97e-35

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 127.43  E-value: 3.97e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    1 MASGGGqKVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDlkkKDRLVEAAGEV--YGQTLTLlPLDICSDESVRQC 78
Cdd:PRK07326   1 MMSLKG-KVALITGGSKGIGFAIAEALLAEG---YKVAITARD---QKELEEAAAELnnKGNVLGL-AADVRDEADVQRA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   79 VNSVKDR--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQaGHIIIMSSVMGLQGVVFND 156
Cdd:PRK07326  73 VDAIVAAfgGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGG-GYIINISSLAGTNFFAGGA 151

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 37590327  157 VYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEF 195
Cdd:PRK07326 152 AYNASKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATHF 190
PRK06482 PRK06482
SDR family oxidoreductase;
11-195 7.53e-35

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 127.92  E-value: 7.53e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   11 LITGCSSGIGlRI--AVLLARDEQkryhVIATMRDLKKKDRLVEAagevYGQTLTLLPLDICSDESVRQCVNSVKDR--H 86
Cdd:PRK06482   6 FITGASSGFG-RGmtERLLARGDR----VAATVRRPDALDDLKAR----YGDRLWVLQLDVTDSAAVRAVVDRAFAAlgR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAIE 166
Cdd:PRK06482  77 IDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIE 156

                        170       180
                 ....*....|....*....|....*....
gi 37590327  167 GFCESMAVQLLKFNVKLSLIEPGPVHTEF 195
Cdd:PRK06482 157 GFVEAVAQEVAPFGIEFTIVEPGPARTNF 185
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 9-195 1.10e-34

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: 126.20  E-value: 1.10e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   9 VVLITGCSSGIGLRIAVLLArdeqKRYHVIATMrDLKKKdRLVEAAGEVYGQTLTLLPL--DICSDESVRQCVNSVKD-- 84
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFA----KRGAKVVIL-DINEK-GAEETANNVRKAGGKVHYYkcDVSKREEVYEAAKKIKKev 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  85 RHIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:cd05339  75 GDVTILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAA 154

                       170       180       190
                ....*....|....*....|....*....|....
gi 37590327 165 IEGFCESMAVQLL---KFNVKLSLIEPGPVHTEF 195
Cdd:cd05339 155 AVGFHESLRLELKaygKPGIKTTLVCPYFINTGM 188
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 1-195 1.22e-34

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 128.50  E-value: 1.22e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    1 MASGGGQKVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDlkkKDRLVEAAGEV--YGQTLTLLPLDICSDESVRQC 78
Cdd:PRK07109   2 MLKPIGRQVVVITGASAGVGRATARAFAR---RGAKVVLLARG---EEGLEALAAEIraAGGEALAVVADVADAEAVQAA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   79 VNSVKDR--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFND 156
Cdd:PRK07109  76 ADRAEEElgPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQS 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 37590327  157 VYTASKFAIEGFCESMAVQLL--KFNVKLSLIEPGPVHTEF 195
Cdd:PRK07109 156 AYCAAKHAIRGFTDSLRCELLhdGSPVSVTMVQPPAVNTPQ 196
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 9-195 1.80e-34

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: 125.57  E-value: 1.80e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   9 VVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLlPLDICSDESVRQCVNSVKDR--H 86
Cdd:cd05360   2 VVVITGASSGIGRATALAFAE---RGAKVVLAARSAEALHELAREVRELGGEAIAV-VADVADAAQVERAADTAVERfgR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAIE 166
Cdd:cd05360  78 IDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVR 157

                       170       180       190
                ....*....|....*....|....*....|.
gi 37590327 167 GFCESMAVQLLK--FNVKLSLIEPGPVHTEF 195
Cdd:cd05360 158 GFTESLRAELAHdgAPISVTLVQPTAMNTPF 188
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 7-194 1.94e-34

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 125.69  E-value: 1.94e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLARDEQKRyhVIATMRDLKKKDRLVEAAGEvYGQTLTLLPLDICSDESVRQCVNSVKDRH 86
Cdd:PRK05557   5 GKVALVTGASRGIGRAIAERLAAQGANV--VINYASSEAGAEALVAEIGA-LGGKALAVQGDVSDAESVERAVDEAKAEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 --IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:PRK05557  82 ggVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAG 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 37590327  165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK05557 162 VIGFTKSLARELASRGITVNAVAPGFIETD 191
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 17-206 2.28e-34

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: 125.24  E-value: 2.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    17 SGIGLRIAVLLARDEqkrYHVIATMRDLKKKDRLVEAAGEVYGQtltLLPLDICSDESVRQCVNSVKDRH--IDVLINNA 94
Cdd:pfam13561   6 SGIGWAIARALAEEG---AEVVLTDLNEALAKRVEELAEELGAA---VLPCDVTDEEQVEALVAAAVEKFgrLDILVNNA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    95 GVG--LLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRqaGHIIIMSSVMGLQGVVFNDVYTASKFAIEGFCESM 172
Cdd:pfam13561  80 GFApkLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEG--GSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 37590327   173 AVQLLKFNVKLSLIEPGPVHT-------EFEtKMMEEVAKM 206
Cdd:pfam13561 158 AVELGPRGIRVNAISPGPIKTlaasgipGFD-ELLAAAEAR 197
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 1-242 3.68e-34

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 125.56  E-value: 3.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    1 MASGGGqKVVLITGCSSGIGLRIAVLLARdEQKRYHVIAtmRDLKKKDRLVEAAGEVygqTLTLLPLDICSDESVRQCVN 80
Cdd:PRK12829   6 LKPLDG-LRVLVTGGASGIGRAIAEAFAE-AGARVHVCD--VSEAALAATAARLPGA---KVTATVADVADPAQVERVFD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   81 SVKDRH--IDVLINNAGV-GLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAG-HIIIMSSVMGLQGVVFND 156
Cdd:PRK12829  79 TAVERFggLDVLVNNAGIaGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGgVIIALSSVAGRLGYPGRT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  157 VYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYPGADPDTVRYFKdvYVPssidiFEAMGq 236
Cdd:PRK12829 159 PYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEARAQQLGIGLDEMEQEYLE--KIS-----LGRMV- 230


                 ....*.
gi 37590327  237 TPDDIA 242
Cdd:PRK12829 231 EPEDIA 236
PRK12826 PRK12826
SDR family oxidoreductase;
8-242 3.81e-33

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 122.72  E-value: 3.81e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDRLVEAAGEVYGQTLTLlPLDICSDESVRQCVNSVKDRH- 86
Cdd:PRK12826   7 RVALVTGAARGIGRAIAVRLAADGAE---VIVVDICGDDAAATAELVEAAGGKARAR-QVDVRDRAALKAAVAAGVEDFg 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 -IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQ-GVVFNDVYTASKFA 164
Cdd:PRK12826  83 rLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRvGYPGLAHYAASKAG 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37590327  165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTEfetkMMEEVAKMEYPGAdpdtvryfkdvyVPSSIDIFEAMgqTPDDIA 242
Cdd:PRK12826 163 LVGFTRALALELAARNITVNSVHPGGVDTP----MAGNLGDAQWAEA------------IAAAIPLGRLG--EPEDIA 222
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 8-206 1.65e-32

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: 120.73  E-value: 1.65e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDLKKKDRLVEAAGEvYGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAEG---AKVAVTDRSEEAAAETVEEIKA-LGGNAAALEADVSDREAVEALVEKVEAEFg 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 -IDVLINNAGV---GLLgpvesISM--DEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTA 160
Cdd:cd05333  77 pVDILVNNAGItrdNLL-----MRMseEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAA 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 37590327 161 SKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKM 206
Cdd:cd05333 152 SKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEK 197
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 8-189 2.81e-32

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: 121.23  E-value: 2.81e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLriavLLARD-EQKRYHVIATMrdLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCV----NSV 82
Cdd:cd09805   1 KAVLITGCDSGFGN----LLAKKlDSLGFTVLAGC--LTKNGPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAqwvkEHV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  83 KDRHIDVLINNAGV-GLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPdMKKRQAGHIIIMSSVMGLQGVVFNDVYTAS 161
Cdd:cd09805  75 GEKGLWGLVNNAGIlGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLP-LLRRAKGRVVNVSSMGGRVPFPAGGAYCAS 153

                       170       180
                ....*....|....*....|....*...
gi 37590327 162 KFAIEGFCESMAVQLLKFNVKLSLIEPG 189
Cdd:cd09805 154 KAAVEAFSDSLRRELQPWGVKVSIIEPG 181
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 8-195 4.99e-32

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: 119.15  E-value: 4.99e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKkkdRLVEAAGEVYGQTLTLlPLDICSDESVRQCVNSVKDRH- 86
Cdd:cd08929   1 KAALVTGASRGIGEATARLLH---AEGYRVGICARDEA---RLAAAAAQELEGVLGL-AGDVRDEADVRRAVDAMEEAFg 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 -IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:cd08929  74 gLDALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGL 153

                       170       180       190
                ....*....|....*....|....*....|
gi 37590327 166 EGFCESMAVQLLKFNVKLSLIEPGPVHTEF 195
Cdd:cd08929 154 LGLSEAAMLDLREANIRVVNVMPGSVDTGF 183
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 10-199 2.11e-30

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: 115.12  E-value: 2.11e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  10 VLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDlkkKDRLVEAAGEVYGQT--LTLLPLDICSDESVRQCVNSVKDR-- 85
Cdd:cd05350   1 VLITGASSGIGRALAREFA---KAGYNVALAARR---TDRLDELKAELLNPNpsVEVEILDVTDEERNQLVIAELEAElg 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:cd05350  75 GLDLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAAL 154

                       170       180       190
                ....*....|....*....|....*....|....
gi 37590327 166 EGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKM 199
Cdd:cd05350 155 SSLAESLRYDVKKRGIRVTVINPGFIDTPLTANM 188
PRK06138 PRK06138
SDR family oxidoreductase;
7-242 7.50e-30

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 114.09  E-value: 7.50e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDlkkKDRLVEAAGEVY-GQTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:PRK06138   5 GRVAIVTGAGSGIGRATAKLFAREGAR---VVVADRD---AEAAERVAAAIAaGGRAFARQGDVGSAEAVEALVDFVAAR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 H--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:PRK06138  79 WgrLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  164 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVakmeypgADPDTVRyfkdvyvpSSIDIFEAMGQ--TPDDI 241
Cdd:PRK06138 159 AIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIFARH-------ADPEALR--------EALRARHPMNRfgTAEEV 223


                 .
gi 37590327  242 A 242
Cdd:PRK06138 224 A 224
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 8-215 1.14e-29

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: 113.22  E-value: 1.14e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDRlVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDR-- 85
Cdd:cd05347   6 KVALVTGASRGIGFGIASGLAEAGAN---IVINSRNEEKAEE-AQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDfg 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:cd05347  82 KIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGV 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 37590327 166 EGFCESMAVQLLKFNVKLSLIEPGpvhtEFETKMMEEVakmeypGADPDT 215
Cdd:cd05347 162 AGLTKALATEWARHGIQVNAIAPG----YFATEMTEAV------VADPEF 201
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 10-212 1.58e-29

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: 111.07  E-value: 1.58e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  10 VLITGCSSGIGLRIAVLLARDeqKRYHVIATMRDlkkkdrlveaagevygqtltllpldicsdesvrqcvnsvkdrhiDV 89
Cdd:cd02266   1 VLVTGGSGGIGGAIARWLASR--GSPKVLVVSRR--------------------------------------------DV 34

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  90 LINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAIEGFC 169
Cdd:cd02266  35 VVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLA 114

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 37590327 170 ESMAVQLLKFNVKLSLIEPGPVHTEFETK---MMEEVAKMEYPGAD 212
Cdd:cd02266 115 QQWASEGWGNGLPATAVACGTWAGSGMAKgpvAPEEILGNRRHGVR 160
PRK05693 PRK05693
SDR family oxidoreductase;
7-195 4.39e-29

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 112.58  E-value: 4.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAvllarDEQKR--YHVIATMRDLKKKDRLVEAAgevygqtLTLLPLDICSDESVRQCVNSVKD 84
Cdd:PRK05693   1 MPVVLITGCSSGIGRALA-----DAFKAagYEVWATARKAEDVEALAAAG-------FTAVQLDVNDGAALARLAEELEA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   85 RH--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMkKRQAGHIIIMSSVMGLQGVVFNDVYTASK 162
Cdd:PRK05693  69 EHggLDVLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLL-RRSRGLVVNIGSVSGVLVTPFAGAYCASK 147

                        170       180       190
                 ....*....|....*....|....*....|...
gi 37590327  163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEF 195
Cdd:PRK05693 148 AAVHALSDALRLELAPFGVQVMEVQPGAIASQF 180
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-216 8.51e-29

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 110.44  E-value: 8.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATmrDLKKKDRLVEAagevygqtLTLLPLDICSDesVRQCVNSVKdrHI 87
Cdd:PRK06550   6 KTVLITGAASGIGLAQARAFL---AQGAQVYGV--DKQDKPDLSGN--------FHFLQLDLSDD--LEPLFDWVP--SV 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   88 DVLINNAGVgLLG--PVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:PRK06550  69 DILCNTAGI-LDDykPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHAL 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  166 EGFCESMAVQLLKFNVKLSLIEPGPVHT-----EFET-KMMEEVAKmEYPG---ADPDTV 216
Cdd:PRK06550 148 AGFTKQLALDYAKDGIQVFGIAPGAVKTpmtaaDFEPgGLADWVAR-ETPIkrwAEPEEV 206
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 8-205 9.05e-29

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: 111.07  E-value: 9.05e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:cd05343   7 RVALVTGASVGIGAAVARALV---QHGMKVVGCARRVDKIEALAAECQSAGYPTLFPYQCDLSNEEQILSMFSAIRTQHq 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 -IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQA--GHIIIMSSVMG---LQGVVFNdVYTA 160
Cdd:cd05343  84 gVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVddGHIININSMSGhrvPPVSVFH-FYAA 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 37590327 161 SKFAIEGFCESMAVQL--LKFNVKLSLIEPGPVHTEFETKMMEEVAK 205
Cdd:cd05343 163 TKHAVTALTEGLRQELreAKTHIRATSISPGLVETEFAFKLHDNDPE 209
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 8-205 1.52e-28

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: 110.17  E-value: 1.52e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDlkkkDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:cd05341   6 KVAIVTGGARGLGLAHARLLVAEGAK---VVLSDIL----DEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFg 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 -IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:cd05341  79 rLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKGAV 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 37590327 166 EGFCESMAVQL--LKFNVKLSLIEPGPVHtefeTKMMEEVAK 205
Cdd:cd05341 159 RGLTKSAALECatQGYGIRVNSVHPGYIY----TPMTDELLI 196
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 7-243 1.80e-28

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


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 109.80  E-value: 1.80e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   7 QKVVLITGCSSGIGLRIA-VLLARDEQKRYhviATMRDLKKKDRLVEAagevYGQTLTLLPLDICSDESVRQCVNSVKDr 85
Cdd:cd05354   3 DKTVLVTGANRGIGKAFVeSLLAHGAKKVY---AAVRDPGSAAHLVAK----YGDKVVPLRLDVTDPESIKAAAAQAKD- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 hIDVLINNAGVG-LLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:cd05354  75 -VDVVINNAGVLkPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327 165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTEFetkmmeeVAKMEYPGADPDTV-----RYFKDvyvpssiDIFEAMgqtPD 239
Cdd:cd05354 154 AYSLTQGLRAELAAQGTLVLSVHPGPIDTRM-------AAGAGGPKESPETVaeavlKALKA-------GEFHVF---PD 216


                ....
gi 37590327 240 DIAK 243
Cdd:cd05354 217 EMAK 220
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 8-244 3.53e-28

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: 109.39  E-value: 3.53e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQKryhviATMRDLKKKDRLVEAAGEV--YGQTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:cd05366   3 KVAIITGAAQGIGRAIAERLAADGFN-----IVLADLNLEEAAKSTIQEIseAGYNAVAVGADVTDKDDVEALIDQAVEK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 H--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQ-AGHIIIMSSVMGLQGVVFNDVYTASK 162
Cdd:cd05366  78 FgsFDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINASSIAGVQGFPNLGAYSASK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327 163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMeypGADPDTVRYfkdVYVPSSIdifeAMG--QTPDD 240
Cdd:cd05366 158 FAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVGEI---AGKPEGEGF---AEFSSSI----PLGrlSEPED 227


                ....
gi 37590327 241 IAKC 244
Cdd:cd05366 228 VAGL 231
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 10-209 5.65e-28

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: 108.54  E-value: 5.65e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  10 VLITGCSSGIGLRIAVLLARDeqKRYHVIATMRDlkkKDRLVEAAGE-VYGQTLTLLPLDICS--DESVRQCVNSVKDRH 86
Cdd:cd05325   1 VLITGASRGIGLELVRQLLAR--GNNTVIATCRD---PSAATELAALgASHSRLHILELDVTDeiAESAEAVAERLGDAG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 IDVLINNAGV-GLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMG-LQGVVFNDVYT--ASK 162
Cdd:cd05325  76 LDVLINNAGIlHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGsIGDNTSGGWYSyrASK 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 37590327 163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVhtefETKMMEEVAKMEYP 209
Cdd:cd05325 156 AALNMLTKSLAVELKRDGITVVSLHPGWV----RTDMGGPFAKNKGP 198
PRK07832 PRK07832
SDR family oxidoreductase;
8-250 6.47e-28

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 109.36  E-value: 6.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAA---QGAELFLTDRDADGLAQTVADARALGGTVPEHRALDISDYDAVAAFAADIHAAHg 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 -IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDM-KKRQAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:PRK07832  78 sMDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMvAAGRGGHLVNVSSAAGLVALPWHAAYSASKFG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTEFetkmmeeVAKMEYPGADPDTVRyfkdvyVPSSIDIFEAMGQTPDDIAKC 244
Cdd:PRK07832 158 LRGLSEVLRFDLARHGIGVSVVVPGAVKTPL-------VNTVEIAGVDREDPR------VQKWVDRFRGHAVTPEKAAEK 224


                 ....*.
gi 37590327  245 TKKVIE 250
Cdd:PRK07832 225 ILAGVE 230
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 8-199 1.17e-27

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: 108.27  E-value: 1.17e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRD---LKKKDRLVEAAGeVYGQTLTLLPLDICSDESVRQCVNSV-- 82
Cdd:cd05364   4 KVAIITGSSSGIGAGTAILFARLGAR---LALTGRDaerLEETRQSCLQAG-VSEKKILLVVADLTEEEGQDRIISTTla 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  83 KDRHIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQaGHIIIMSSVMGlqGVVFNDV--YTA 160
Cdd:cd05364  80 KFGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVSSVAG--GRSFPGVlyYCI 156

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 37590327 161 SKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKM 199
Cdd:cd05364 157 SKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRM 195
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 8-206 1.84e-27

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: 107.17  E-value: 1.84e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDlkkKDRLVEAAGEVYGqtLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:COG3967   6 NTILITGGTSGIGLALAKRLH---ARGNTVIITGRR---EEKLEEAAAANPG--LHTIVLDVADPASIAALAEQVTAEFp 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 -IDVLINNAGVG----LLGPVESIsmDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTAS 161
Cdd:COG3967  78 dLNVLINNAGIMraedLLDEAEDL--ADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSAT 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 37590327 162 KFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKM 206
Cdd:COG3967 156 KAALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTGGQGGDPRAM 200
FabG-like PRK07231
SDR family oxidoreductase;
8-242 2.51e-27

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 107.22  E-value: 2.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRdlkKKDRLVEAAGEV-YGQTLTLLPLDICSDESVRQCVNSVKDRH 86
Cdd:PRK07231   6 KVAIVTGASSGIGEGIARRFAAEGAR---VVVTDR---NEEAAERVAAEIlAGGRAIAVAADVSDEADVEAAVAAALERF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 --IDVLINNAGVGLL-GPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:PRK07231  80 gsVDILVNNAGTTHRnGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  164 AIEGFCESMAVQLLKFNVKLSLIEPGPVhtefETKMMEEVAKMEYPGADpDTVRyfkdvyvpSSIdifeAMGQ--TPDDI 241
Cdd:PRK07231 160 AVITLTKALAAELGPDKIRVNAVAPVVV----ETGLLEAFMGEPTPENR-AKFL--------ATI----PLGRlgTPEDI 222


                 .
gi 37590327  242 A 242
Cdd:PRK07231 223 A 223
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 8-242 3.35e-27

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: 106.59  E-value: 3.35e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQK---RYHviatmRDLKKKDRLVEAAGEVYGQTLtLLPLDICSDESVRQCVNSVKD 84
Cdd:cd05362   4 KVALVTGASRGIGRAIAKRLARDGASvvvNYA-----SSKAAAEEVVAEIEAAGGKAI-AVQADVSDPSQVARLFDAAEK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  85 R--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMkkRQAGHIIIMSSVMGLQGVVFNDVYTASK 162
Cdd:cd05362  78 AfgGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAAYTPNYGAYAGSK 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327 163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEfetkmmeevakMEYPGADPDTVRYFKdvyvpsSIDIFEAMGQtPDDIA 242
Cdd:cd05362 156 AAVEAFTRVLAKELGGRGITVNAVAPGPVDTD-----------MFYAGKTEEAVEGYA------KMSPLGRLGE-PEDIA 217
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 8-216 4.23e-27

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: 106.23  E-value: 4.23e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKK--KDRLVEAAGEVygqTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLL---KKGAKVAILDRNENPgaAAELQAINPKV---KATFVQCDVTSWEQLAAAFKKAIEK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 H--IDVLINNAGVGllgpvESISMDE-------MKRVFETNFFGTVRMIKEVMPDMKKRQAGH---IIIMSSVMGLQGVV 153
Cdd:cd05323  75 FgrVDILINNAGIL-----DEKSYLFagklpppWEKTIDVNLTGVINTTYLALHYMDKNKGGKggvIVNIGSVAGLYPAP 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37590327 154 FNDVYTASKFAIEGFCESMAVQL-LKFNVKLSLIEPGPVHTEFETKMMEEVAKME--YPGADPDTV 216
Cdd:cd05323 150 QFPVYSASKHGVVGFTRSLADLLeYKTGVRVNAICPGFTNTPLLPDLVAKEAEMLpsAPTQSPEVV 215
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 8-242 5.41e-27

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: 106.20  E-value: 5.41e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDlkkKDRLVEAAGEV--YGQTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:cd05344   2 KVALVTAASSGIGLAIARALAREG---ARVAICARN---RENLERAASELraGGAGVLAVVADLTDPEDIDRLVEKAGDA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 H--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:cd05344  76 FgrVDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARA 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327 164 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEypGADPDTVRYFKDVYVPssidifeaMGQ--TPDDI 241
Cdd:cd05344 156 GLIGLVKTLSRELAPDGVTVNSVLPGYIDTERVRRLLEARAEKE--GISVEEAEKEVASQIP--------LGRvgKPEEL 225


                .
gi 37590327 242 A 242
Cdd:cd05344 226 A 226
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
8-203 5.80e-27

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 106.00  E-value: 5.80e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDLKKKDRLVEaagEVYGQT---LTLLPLDICSDESVRQCVNSVKD 84
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDG---YRVIATYFSGNDCAKDWF---EEYGFTedqVRLKELDVTDTEECAEALAEIEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   85 RH--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASK 162
Cdd:PRK12824  77 EEgpVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAK 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 37590327  163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEV 203
Cdd:PRK12824 157 AGMIGFTKALASEGARYGITVNCIAPGYIATPMVEQMGPEV 197
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 8-194 6.12e-27

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 106.56  E-value: 6.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKRyhVIAtmrdlkkkDRLVEAAGEVyGQTLTL---LPLDICSDESVRQCVNSVKD 84
Cdd:PRK07825   6 KVVAITGGARGIGLATARALAALGARV--AIG--------DLDEALAKET-AAELGLvvgGPLDVTDPASFAAFLDAVEA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   85 R--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASK 162
Cdd:PRK07825  75 DlgPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASK 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 37590327  163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK07825 155 HAVVGFTDAARLELRGTGVHVSVVLPSFVNTE 186
PRK08264 PRK08264
SDR family oxidoreductase;
8-216 8.56e-27

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 105.36  E-value: 8.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIA-VLLARDEQKRYhviATMRDLkkkdrlveAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDrh 86
Cdd:PRK08264   7 KVVLVTGANRGIGRAFVeQLLARGAAKVY---AAARDP--------ESVTDLGPRVVPLQLDVTDPASVAAAAEAASD-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 IDVLINNAGVGLLG-PVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:PRK08264  74 VTILVNNAGIFRTGsLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAAA 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 37590327  166 EGFCESMAVQLLKFNVKLSLIEPGPVHTEfetkMmeeVAKMEYPGADPDTV 216
Cdd:PRK08264 154 WSLTQALRAELAPQGTRVLGVHPGPIDTD----M---AAGLDAPKASPADV 197
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 7-203 1.06e-26

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: 105.70  E-value: 1.06e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   7 QKVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKKK----DRLVEAAGEVYGqtltlLPLDICSDESVRQCVNSV 82
Cdd:cd08945   3 SEVALVTGATSGIGLAIARRLG---KEGLRVFVCARGEEGLattvKELREAGVEADG-----RTCDVRSVPEIEALVAAA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  83 KDRH--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPD--MKKRQAGHIIIMSSVMGLQGVVFNDVY 158
Cdd:cd08945  75 VARYgpIDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAAPY 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 37590327 159 TASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVhtefETKMMEEV 203
Cdd:cd08945 155 SASKHGVVGFTKALGLELARTGITVNAVCPGFV----ETPMAASV 195
PRK08219 PRK08219
SDR family oxidoreductase;
8-216 1.45e-26

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 104.63  E-value: 1.45e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDeqkrYHVIATMRDlkkKDRLVEAAGEVYGqtLTLLPLDICSDESVRQCVNSVKdrHI 87
Cdd:PRK08219   4 PTALITGASRGIGAAIARELAPT----HTLLLGGRP---AERLDELAAELPG--ATPFPVDLTDPEAIAAAVEQLG--RL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   88 DVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQaGHIIIMSSVMGLQGVVFNDVYTASKFAIEG 167
Cdd:PRK08219  73 DVLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAH-GHVVFINSGAGLRANPGWGSYAASKFALRA 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 37590327  168 FCESmavqlLKF----NVKLSLIEPGPVHTEFETKMMEEvAKMEYPGA---DPDTV 216
Cdd:PRK08219 152 LADA-----LREeepgNVRVTSVHPGRTDTDMQRGLVAQ-EGGEYDPErylRPETV 201
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 1-195 4.03e-26

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 103.90  E-value: 4.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    1 MASGGGQKVVLITGCSSGIGLRIAVLLARDEQKRyhVIATMRDLKKKD--RLVEAAGevyGQTLTLlPLDICSDESVRQC 78
Cdd:PRK12939   1 MASNLAGKRALVTGAARGLGAAFAEALAEAGATV--AFNDGLAAEARElaAALEAAG---GRAHAI-AADLADPASVQRF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   79 VNSVKDR--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFND 156
Cdd:PRK12939  75 FDAAAAAlgGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLG 154

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 37590327  157 VYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEF 195
Cdd:PRK12939 155 AYVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEA 193
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 8-194 5.63e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 103.58  E-value: 5.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDlkkkDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDR-- 85
Cdd:PRK06841  16 KVAVVTGGASGIGHAIAELFA---AKGARVALLDRS----EDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAfg 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSS---VMGLQGVVfndVYTASK 162
Cdd:PRK06841  89 RIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASqagVVALERHV---AYCASK 165

                        170       180       190
                 ....*....|....*....|....*....|..
gi 37590327  163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK06841 166 AGVVGMTKVLALEWGPYGITVNAISPTVVLTE 197
PRK07201 PRK07201
SDR family oxidoreductase;
8-186 9.07e-26

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 107.34  E-value: 9.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDlkkKDRLVEAAGEV--YGQTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:PRK07201 372 KVVLITGASSGIGRATAIKVAE---AGATVFLVARN---GEALDELVAEIraKGGTAHAYTCDLTDSAAVDHTVKDILAE 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 H--IDVLINNAGvgllgpvESI------SMDEM---KRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVmglqGVVF 154
Cdd:PRK07201 446 HghVDYLVNNAG-------RSIrrsvenSTDRFhdyERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSI----GVQT 514

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 37590327  155 N----DVYTASKFAIEGFCESMAVQLLKFNVKLSLI 186
Cdd:PRK07201 515 NaprfSAYVASKAALDAFSDVAASETLSDGITFTTI 550
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 8-205 1.15e-24

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: 100.21  E-value: 1.15e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARdeQKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:cd08940   3 KVALVTGSTSGIGLGIARALAA--AGANIVLNGFGDAAEIEAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFg 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 -IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:cd08940  81 gVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHGV 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 37590327 166 EGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAK 205
Cdd:cd08940 161 VGLTKVVALETAGTGVTCNAICPGWVLTPLVEKQISALAQ 200
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 8-242 1.50e-24

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 99.96  E-value: 1.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKRyhVIATMRDLKKKDRLVEAAGEvyGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:PRK12429   5 KVALVTGAASGIGLEIALALAKEGAKV--VIADLNDEAAAAAAEALQKA--GGKAIGVAMDVTDEEAINAGIDYAVETFg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 -IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:PRK12429  81 gVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37590327  166 EGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEypGADPDTVRyfKDVYVPSSIDifeamGQ--TPDDIA 242
Cdd:PRK12429 161 IGLTKVVALEGATHGVTVNAICPGYVDTPLVRKQIPDLAKER--GISEEEVL--EDVLLPLVPQ-----KRftTVEEIA 230
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 8-194 2.79e-24

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 98.80  E-value: 2.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATmrdlkkkDRlveAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDR-- 85
Cdd:PRK08220   9 KTVWVTGAAQGIGYAVALAFV---EAGAKVIGF-------DQ---AFLTQEDYPFATFVLDVSDAAAVAQVCQRLLAEtg 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSS------VMGLQgvvfndVYT 159
Cdd:PRK08220  76 PLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSnaahvpRIGMA------AYG 149

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 37590327  160 ASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK08220 150 ASKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTD 184
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 9-215 3.86e-24

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 98.68  E-value: 3.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    9 VVLITGCSSGIGLRIAVLLARDEQKryhVIATMRdlkKKDRLVEAAGEvYGQTLTLLPLDICSDESVRQCVNSVKD--RH 86
Cdd:PRK10538   2 IVLVTGATAGFGECITRRFIQQGHK---VIATGR---RQERLQELKDE-LGDNLYIAQLDVRNRAAIEEMLASLPAewRN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 IDVLINNAGVGL-LGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:PRK10538  75 IDVLVNNAGLALgLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFV 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 37590327  166 EGFCESMAVQLLKFNVKLSLIEPGPVH-TEFET---KMMEEVAKMEYPGADPDT 215
Cdd:PRK10538 155 RQFSLNLRTDLHGTAVRVTDIEPGLVGgTEFSNvrfKGDDGKAEKTYQNTVALT 208
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 8-217 4.72e-24

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: 97.93  E-value: 4.72e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATmrDLKKkDRLVEAAGevyGQTLTLLPLDICSDESVRQCVNSVkdRHI 87
Cdd:cd05368   3 KVALITAAAQGIGRAIALAFAREGAN---VIAT--DINE-EKLKELER---GPGITTRVLDVTDKEQVAALAKEE--GRI 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  88 DVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMG-LQGVVFNDVYTASKFAIE 166
Cdd:cd05368  72 DVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASsIKGVPNRFVYSTTKAAVI 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 37590327 167 GFCESMAVQLLKFNVKLSLIEPGPVhtefETKMMEEVAKMEypgADPDTVR 217
Cdd:cd05368 152 GLTKSVAADFAQQGIRCNAICPGTV----DTPSLEERIQAQ---PDPEEAL 195
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 10-193 1.33e-23

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: 96.77  E-value: 1.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  10 VLITGCSSGIGLRIAVLLArdeQKRYHVIATmrDLKkkdrlvEAAGEVYGQTLTLLPLDICSDESVRQCVNSVK--DRHI 87
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLL---QAGATVIAL--DLP------FVLLLEYGDPLRLTPLDVADAAAVREVCSRLLaeHGPI 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  88 DVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAIEG 167
Cdd:cd05331  70 DALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALAS 149

                       170       180
                ....*....|....*....|....*.
gi 37590327 168 FCESMAVQLLKFNVKLSLIEPGPVHT 193
Cdd:cd05331 150 LSKCLGLELAPYGVRCNVVSPGSTDT 175
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 8-194 1.64e-23

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: 96.22  E-value: 1.64e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAV-LLARDEQkryhVIATMRDlkkKDRLVEAAGEvyGQTLTLLPLDICSDESVRQCVNSVKDRH 86
Cdd:cd05370   6 NTVLITGGTSGIGLALARkFLEAGNT----VIITGRR---EERLAEAKKE--LPNIHTIVLDVGDAESVEALAEALLSEY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 --IDVLINNAGVGLlgPVE----SISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTA 160
Cdd:cd05370  77 pnLDILINNAGIQR--PIDlrdpASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCA 154

                       170       180       190
                ....*....|....*....|....*....|....
gi 37590327 161 SKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:cd05370 155 TKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTE 188
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 8-199 2.04e-23

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: 95.98  E-value: 2.04e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDlkkKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDR-- 85
Cdd:cd08931   1 KAIFITGAASGIGRETALLFAR---NGWFVGLYDID---EDGLAALAAELGAENVVAGALDVTDRAAWAAALADFAAAtg 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 -HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:cd08931  75 gRLDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFA 154

                       170       180       190
                ....*....|....*....|....*....|....*
gi 37590327 165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKM 199
Cdd:cd08931 155 VRGLTEALDVEWARHGIRVADVWPWFVDTPILTKG 189
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 8-194 2.48e-23

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 96.02  E-value: 2.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDRLVEAAGevyGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:PRK12828   8 KVVAITGGFGGLGRATAAWLAARGAR---VALIGRGAAPLSQTLPGVP---ADALRIGGIDLVDPQAARRAVDEVNRQFg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 -IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:PRK12828  82 rLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAGV 161

                        170       180
                 ....*....|....*....|....*....
gi 37590327  166 EGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK12828 162 ARLTEALAAELLDRGITVNAVLPSIIDTP 190
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 8-217 2.51e-23

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: 96.31  E-value: 2.51e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDLKKKD---------------RLVEAAGevyGQTLTLlPLDICSD 72
Cdd:cd05338   4 KVAFVTGASRGIGRAIALRLAKAG---ATVVVAAKTASEGDngsakslpgtieetaEEIEAAG---GQALPI-VVDVRDE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  73 ESVRQCVNSVKDRH--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQ 150
Cdd:cd05338  77 DQVRALVEATVDQFgrLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLR 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37590327 151 GVVFNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMeevakmeYPGADPDTVR 217
Cdd:cd05338 157 PARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIETPAATEL-------SGGSDPARAR 216
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 8-194 4.77e-23

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


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 96.14  E-value: 4.77e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDLkkkDRLVEAAGEVYGQT----LTLLPLDICSDESVRQCVNSVK 83
Cdd:cd05327   2 KVVVITGANSGIGKETARELAK---RGAHVIIACRNE---EKGEEAAAEIKKETgnakVEVIQLDLSSLASVRQFAEEFL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  84 DRH--IDVLINNAGVGLlgPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQG-VVFND---- 156
Cdd:cd05327  76 ARFprLDILINNAGIMA--PPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGpIDFNDldle 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 37590327 157 ---------VYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:cd05327 154 nnkeyspykAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTE 200
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 8-189 4.82e-23

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 95.85  E-value: 4.82e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAvllarDEQKRYHVIATMRDLKKKDRLveaagevyGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:PRK06171  10 KIIIVTGGSSGIGLAIV-----KELLANGANVVNADIHGGDGQ--------HENYQFVPTDVSSAEEVNHTVAEIIEKFg 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 -IDVLINNAGVG---LL----GPVESISMDE--MKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFND 156
Cdd:PRK06171  77 rIDGLVNNAGINiprLLvdekDPAGKYELNEaaFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEGQS 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 37590327  157 VYTASKFAIEGFCESMAVQLLKFNVKLSLIEPG 189
Cdd:PRK06171 157 CYAATKAALNSFTRSWAKELGKHNIRVVGVAPG 189
PRK07454 PRK07454
SDR family oxidoreductase;
7-194 6.76e-23

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 95.03  E-value: 6.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKKKDRLVEAAGEVyGQTLTLLPLDICSDESVRQCVNSVKDR- 85
Cdd:PRK07454   6 MPRALITGASSGIGKATALAFA---KAGWDLALVARSQDALEALAAELRST-GVKAAAYSIDLSNPEAIAPGIAELLEQf 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 -HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQgvVFND--VYTASK 162
Cdd:PRK07454  82 gCPDVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARN--AFPQwgAYCVSK 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 37590327  163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK07454 160 AALAAFTKCLAEEERSHGIRVCTITLGAVNTP 191
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 10-194 1.07e-22

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: 94.34  E-value: 1.07e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  10 VLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDR--HI 87
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAE---RGADVVINYRKSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERfgRL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  88 DVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAIEG 167
Cdd:cd05359  78 DVLVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEA 157

                       170       180
                ....*....|....*....|....*..
gi 37590327 168 FCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:cd05359 158 LVRYLAVELGPRGIRVNAVSPGVIDTD 184
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 8-212 1.10e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 95.49  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLAR----------DEQkryhviatmRDLKKKDRLVEAAGevygQTLTLLPLDICSDESVRQ 77
Cdd:PRK06701  47 KVALITGGDSGIGRAVAVLFAKegadiaivylDEH---------EDANETKQRVEKEG----VKCLLIPGDVSDEAFCKD 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   78 CV-NSVKD-RHIDVLINNAGVGLlgPVES---ISMDEMKRVFETNFFGTVRMIKEVMPDMKkrQAGHIIIMSSVMGLQG- 151
Cdd:PRK06701 114 AVeETVRElGRLDILVNNAAFQY--PQQSledITAEQLDKTFKTNIYSYFHMTKAALPHLK--QGSAIINTGSITGYEGn 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37590327  152 VVFNDvYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEF--ETKMMEEVAKMeypGAD 212
Cdd:PRK06701 190 ETLID-YSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPLipSDFDEEKVSQF---GSN 248
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 7-215 1.28e-22

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 94.17  E-value: 1.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGlRIA-----------VLLARDEQKryhviatMRDLKKKdrlVEAAGevyGQTLTLLPLDI--CSDE 73
Cdd:PRK08945  12 DRIILVTGAGDGIG-REAaltyarhgatvILLGRTEEK-------LEAVYDE---IEAAG---GPQPAIIPLDLltATPQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   74 SVRQCVNSVKDR--HIDVLINNAGV-GLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQ 150
Cdd:PRK08945  78 NYQQLADTIEEQfgRLDGVLHNAGLlGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQ 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37590327  151 GVVFNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEfetkmMEEVAkmeYPGADPDT 215
Cdd:PRK08945 158 GRANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTA-----MRASA---FPGEDPQK 214
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 8-243 1.32e-22

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 94.58  E-value: 1.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKRyhVIATMRDLKKK---DRLVEAAGEVYGqtltlLPLDICSDESVRQCVNSVKD 84
Cdd:PRK13394   8 KTAVVTGAASGIGKEIALELARAGAAV--AIADLNQDGANavaDEINKAGGKAIG-----VAMDVTNEDAVNAGIDKVAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   85 R--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKK-RQAGHIIIMSSVMGLQGVVFNDVYTAS 161
Cdd:PRK13394  81 RfgSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKdDRGGVVIYMGSVHSHEASPLKSAYVTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  162 KFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEypGADPDTVRyfKDVYVPSSIDifeamGQ--TPD 239
Cdd:PRK13394 161 KHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQIPEQAKEL--GISEEEVV--KKVMLGKTVD-----GVftTVE 231


                 ....
gi 37590327  240 DIAK 243
Cdd:PRK13394 232 DVAQ 235
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 8-210 1.73e-22

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: 94.67  E-value: 1.73e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLAR----------DEQKRyhviatmrDLKKKDRLVEAAGevygQTLTLLPLDIcSDESVrq 77
Cdd:cd05355  27 KKALITGGDSGIGRAVAIAFARegadvainylPEEED--------DAEETKKLIEEEG----RKCLLIPGDL-GDESF-- 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  78 CVNSVKDRH-----IDVLINNAGVGLLGP-VESISMDEMKRVFETNFFGTVRMIKEVMPDMKKrqAGHIIIMSSVMGLQG 151
Cdd:cd05355  92 CRDLVKEVVkefgkLDILVNNAAYQHPQEsIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKK--GSSIINTTSVTAYKG 169

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37590327 152 VVFNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHT-----EFETKMMEEVAK---MEYPG 210
Cdd:cd05355 170 SPHLLDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTplipsSFPEEKVSEFGSqvpMGRAG 236
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 8-207 2.03e-22

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: 93.67  E-value: 2.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQKRyhVIATMRDlkkkDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:cd05326   5 KVAIITGGASGIGEATARLFAKHGARV--VIADIDD----DAGQAVAAELGDPDISFVHCDVTVEADVRAAVDTAVARFg 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 -IDVLINNAGVglLGP----VESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTAS 161
Cdd:cd05326  79 rLDIMFNNAGV--LGApcysILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTAS 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 37590327 162 KFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMM-EEVAKME 207
Cdd:cd05326 157 KHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFgVEDEAIE 203
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 8-205 4.98e-22

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: 92.97  E-value: 4.98e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQKRYHVIATMRDLKK-KDRLVEAAGEVygqTLTLLPLDICSDESVRQCVNSVKDR- 85
Cdd:cd05330   4 KVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAaKAALLEIAPDA---EVLLIKADVSDEAQVEAYVDATVEQf 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 -HIDVLINNAGV-GLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:cd05330  81 gRIDGFFNNAGIeGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKH 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 37590327 164 AIEGFCESMAVQLLKFNVKLSLIEPGPVHtefeTKMMEEVAK 205
Cdd:cd05330 161 GVVGLTRNSAVEYGQYGIRINAIAPGAIL----TPMVEGSLK 198
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
8-242 6.21e-22

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 92.78  E-value: 6.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARdEQKRYhVIAtmrDLKKKDrlVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDR-- 85
Cdd:PRK07067   7 KVALLTGAASGIGEAVAERYLA-EGARV-VIA---DIKPAR--ARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERfg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKR-QAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:PRK07067  80 GIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQgRGGKIINMASQAGRRGEALVSHYCATKAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTEfetkMMEEV----AKmeYPGADPDTVRYFKDVYVPssidiFEAMGqTPDD 240
Cdd:PRK07067 160 VISYTQSAALALIRHGINVNAIAPGVVDTP----MWDQVdalfAR--YENRPPGEKKRLVGEAVP-----LGRMG-VPDD 227


                 ..
gi 37590327  241 IA 242
Cdd:PRK07067 228 LT 229
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 8-207 9.68e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 92.09  E-value: 9.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKKKDRLVEAAGEvygqtlTLLPLDICSDESVRQCVnSVKDRhI 87
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALA---QRGARVVAAARNAAALDRLAGETGC------EPLRLDVGDDAAIRAAL-AAAGA-F 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   88 DVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDM-KKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAIE 166
Cdd:PRK07060  79 DGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMiAAGRGGSIVNVSSQAALVGLPDHLAYCASKAALD 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 37590327  167 GFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKME 207
Cdd:PRK07060 159 AITRVLCVELGPHGIRVNSVNPTVTLTPMAAEAWSDPQKSG 199
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
8-216 1.01e-21

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 92.17  E-value: 1.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKRYHVIATMRDLKKKDRLVEAagevyGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:PRK08226   7 KTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADELCGR-----GHRCTAVVADVRDPASVAAAIKRAKEKEg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 -IDVLINNAGVGLLGPVESISmDEMKRV-FETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGlqGVVFND---VYTAS 161
Cdd:PRK08226  82 rIDILVNNAGVCRLGSFLDMS-DEDRDFhIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTG--DMVADPgetAYALT 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 37590327  162 KFAIEGFCESMAVQLLKFNVKLSLIEPGPVhtefETKMMEEVAKMEYPGaDPDTV 216
Cdd:PRK08226 159 KAAIVGLTKSLAVEYAQSGIRVNAICPGYV----RTPMAESIARQSNPE-DPESV 208
PRK06172 PRK06172
SDR family oxidoreductase;
8-211 1.81e-21

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 91.35  E-value: 1.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDRLVEAAGEVYGQTLtLLPLDICSDESVRQCVNSVKDR-- 85
Cdd:PRK06172   8 KVALVTGGAAGIGRATALAFAREGAK---VVVADRDAAGGEETVALIREAGGEAL-FVACDVTRDAEVKALVEQTIAAyg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 HIDVLINNAGVGL-LGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:PRK06172  84 RLDYAFNNAGIEIeQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASKHA 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 37590327  165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTE-FETKMMEEVAKMEYPGA 211
Cdd:PRK06172 164 VIGLTKSAAIEYAKKGIRVNAVCPAVIDTDmFRRAYEADPRKAEFAAA 211
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 8-196 1.98e-21

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: 90.74  E-value: 1.98e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDLKKKDRLVEAAGEVYG-QTLTLLpLDICSDESVRQCVN-SVKDR 85
Cdd:cd05356   2 TWAVVTGATDGIGKAYAEELAK---RGFNVILISRTQEKLDAVAKEIEEKYGvETKTIA-ADFSAGDDIYERIEkELEGL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 HIDVLINNAGVGLLGPVESISMD--EMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:cd05356  78 DIGILVNNVGISHSIPEYFLETPedELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKA 157

                       170       180       190
                ....*....|....*....|....*....|...
gi 37590327 164 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFE 196
Cdd:cd05356 158 FLDFFSRALYEEYKSQGIDVQSLLPYLVATKMS 190
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 9-223 2.13e-21

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: 90.81  E-value: 2.13e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   9 VVLITGCSSGIGLRIA-VLLARDEQKRYHVIA-TMRDLKKkdrlvEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH 86
Cdd:cd05367   1 VIILTGASRGIGRALAeELLKRGSPSVVVLLArSEEPLQE-----LKEELRPGLRVTTVKADLSDAAGVEQLLEAIRKLD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 --IDVLINNAGVglLGPV---ESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQA-GHIIIMSSVMGLQGVVFNDVYTA 160
Cdd:cd05367  76 geRDLLINNAGS--LGPVskiEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkKTVVNVSSGAAVNPFKGWGLYCS 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37590327 161 SKFAIEGFCESMAVQLLKFNVkLSlIEPGPVHTEFETKMMEEvakmeypGADPDTVRYFKDVY 223
Cdd:cd05367 154 SKAARDMFFRVLAAEEPDVRV-LS-YAPGVVDTDMQREIRET-------SADPETRSRFRSLK 207
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 8-224 2.58e-21

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 90.87  E-value: 2.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARdEQKRYHVIAtmRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDrhI 87
Cdd:PRK06125   8 KRVLITGASKGIGAAAAEAFAA-EGCHLHLVA--RDADALEALAADLRAAHGVDVAVHALDLSSPEAREQLAAEAGD--I 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   88 DVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIimsSVMGLQGVVFNDVY---TASKFA 164
Cdd:PRK06125  83 DILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIV---NVIGAAGENPDADYicgSAGNAA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37590327  165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKME-------------YPGADPDTVRYFKDVYV 224
Cdd:PRK06125 160 LMAFTRALGGKSLDDGVRVVGVNPGPVATDRMLTLLKGRARAElgdesrwqellagLPLGRPATPEEVADLVA 232
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
8-194 3.03e-21

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 90.95  E-value: 3.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLAR---DEqkryhVIATMRD-LKKKDRLVEAAGevygQTLTLLPLDICSDESVRQCVNSVK 83
Cdd:PRK06935  16 KVAIVTGGNTGLGQGYAVALAKagaDI-----IITTHGTnWDETRRLIEKEG----RKVTFVQVDLTKPESAEKVVKEAL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   84 DRH--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTAS 161
Cdd:PRK06935  87 EEFgkIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGGKFVPAYTAS 166

                        170       180       190
                 ....*....|....*....|....*....|...
gi 37590327  162 KFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK06935 167 KHGVAGLTKAFANELAAYNIQVNAIAPGYIKTA 199
PRK06398 PRK06398
aldose dehydrogenase; Validated
 8-217 5.35e-21

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 90.28  E-value: 5.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDRLveaagevygqtlTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:PRK06398   7 KVAIVTGGSQGIGKAVVNRLKEEGSN---VINFDIKEPSYNDV------------DYFKVDVSNKEQVIKGIDYVISKYg 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 -IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:PRK06398  72 rIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAV 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 37590327  166 EGFCESMAVQ---LLKFNVKLsliePGPVhtefETKMMEEVAKMEYpGADPDTVR 217
Cdd:PRK06398 152 LGLTRSIAVDyapTIRCVAVC----PGSI----RTPLLEWAAELEV-GKDPEHVE 197
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 8-189 7.92e-21

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 89.63  E-value: 7.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKRyhVIATmrdlKKKDRLVEAAGEV--YGQTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:PRK07890   6 KVVVVSGVGPGLGRTLAVRAARAGADV--VLAA----RTAERLDEVAAEIddLGRRALAVPTDITDEDQCANLVALALER 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 H--IDVLINNA-GVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNdVYTASK 162
Cdd:PRK07890  80 FgrVDALVNNAfRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMINSMVLRHSQPKYG-AYKMAK 158

                        170       180
                 ....*....|....*....|....*..
gi 37590327  163 FAIEGFCESMAVQLLKFNVKLSLIEPG 189
Cdd:PRK07890 159 GALLAASQSLATELGPQGIRVNSVAPG 185
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 7-206 1.72e-20

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 88.65  E-value: 1.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLARDEQKRyhVIATMRDLKKKDRLVEAAGEVYGQTLTLlPLDICSDESVRQCVNSVKDRH 86
Cdd:PRK12937   5 NKVAIVTGASRGIGAAIARRLAADGFAV--AVNYAGSAAAADELVAEIEAAGGRAIAV-QADVADAAAVTRLFDAAETAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 --IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMkkRQAGHIIIMS-SVMGLQGVVFNdVYTASKF 163
Cdd:PRK12937  82 grIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLStSVIALPLPGYG-PYAASKA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 37590327  164 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTE--FETKMMEEVAKM 206
Cdd:PRK12937 159 AVEGLVHVLANELRGRGITVNAVAPGPVATElfFNGKSAEQIDQL 203
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 8-208 2.07e-20

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: 88.37  E-value: 2.07e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQkryHVIATMRDLKKKDRLVEA-AGEVYGQTLTLLPLDICSDEsvRQCVNSVKDRH 86
Cdd:cd08936  11 KVALVTASTDGIGLAIARRLAQDGA---HVVVSSRKQQNVDRAVATlQGEGLSVTGTVCHVGKAEDR--ERLVATAVNLH 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 --IDVLINNAGVGLL-GPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:cd08936  86 ggVDILVSNAAVNPFfGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNVSKT 165

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 37590327 164 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEY 208
Cdd:cd08936 166 ALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALWMDKAVEES 210
PRK06124 PRK06124
SDR family oxidoreductase;
8-208 2.10e-20

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 88.62  E-value: 2.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQkryHVIATMRDLKKKDRLVeAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:PRK06124  12 QVALVTGSARGLGFEIARALAGAGA---HVLVNGRNAATLEAAV-AALRAAGGAAEALAFDIADEEAVAAAFARIDAEHg 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 -IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGlQGVVFND-VYTASKFA 164
Cdd:PRK06124  88 rLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAG-QVARAGDaVYPAAKQG 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 37590327  165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEY 208
Cdd:PRK06124 167 LTGLMRALAAEFGPHGITSNAIAPGYFATETNAAMAADPAVGPW 210
PRK08267 PRK08267
SDR family oxidoreductase;
8-193 2.30e-20

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 88.46  E-value: 2.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDlkkKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAA---EGWRVGAYDIN---EAGLAALAAELGAGNAWTGALDVTDRAAWDAALADFAAATg 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 --IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:PRK08267  76 grLDVLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFA 155

                        170       180
                 ....*....|....*....|....*....
gi 37590327  165 IEGFCESMAVQLLKFNVKLSLIEPGPVHT 193
Cdd:PRK08267 156 VRGLTEALDLEWRRHGIRVADVMPLFVDT 184
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 7-194 2.72e-20

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: 88.03  E-value: 2.72e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   7 QKVVLITGCSSGIGLRIAVLLARdeqkryH----VIATmRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSV 82
Cdd:cd05369   3 GKVAFITGGGTGIGKAIAKAFAE------LgasvAIAG-RKPEVLEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDET 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  83 KDRH--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPD-MKKRQAGHIIIMSSVMGLQGVVFNDVYT 159
Cdd:cd05369  76 LKEFgkIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRlIEAKHGGSILNISATYAYTGSPFQVHSA 155

                       170       180       190
                ....*....|....*....|....*....|....*
gi 37590327 160 ASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:cd05369 156 AAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTT 190
PRK07577 PRK07577
SDR family oxidoreductase;
8-194 5.12e-20

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 87.09  E-value: 5.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDlkkkdrlveAAGEVYGQtltLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:PRK07577   4 RTVLVTGATKGIGLALSLRLANLG---HQVIGIARS---------AIDDFPGE---LFACDLADIEQTAATLAQINEIHp 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSvMGLQGVVFNDVYTASKFAIE 166
Cdd:PRK07577  69 VDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICS-RAIFGALDRTSYSAAKSALV 147

                        170       180
                 ....*....|....*....|....*...
gi 37590327  167 GFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK07577 148 GCTRTWALELAEYGITVNAVAPGPIETE 175
PRK05866 PRK05866
SDR family oxidoreductase;
8-181 5.15e-20

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 88.26  E-value: 5.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRdlkKKDRLVEAAGEVY--GQTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:PRK05866  41 KRILLTGASSGIGEAAAEQFAR---RGATVVAVAR---REDLLDAVADRITraGGDAMAVPCDLSDLDAVDALVADVEKR 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 H--IDVLINNAGVGLLGPVESiSMD---EMKRVFETNFFGTVRMIKEVMPDMKKRQAGHII------IMSSVMGLQGvvf 154
Cdd:PRK05866 115 IggVDILINNAGRSIRRPLAE-SLDrwhDVERTMVLNYYAPLRLIRGLAPGMLERGDGHIInvatwgVLSEASPLFS--- 190

                        170       180
                 ....*....|....*....|....*..
gi 37590327  155 ndVYTASKFAIEGFCESMAVQLLKFNV 181
Cdd:PRK05866 191 --VYNASKAALSAVSRVIETEWGDRGV 215
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 9-216 7.66e-20

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


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 86.67  E-value: 7.66e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   9 VVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH-- 86
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAA---EGFSVALAARREAKLEALLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIgp 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAIE 166
Cdd:cd05373  78 LEVLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALR 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 37590327 167 GFCESMAVQLLKFNVKLS-LIEPGPVHTEFETKMMEEVAKMEYPGA--DPDTV 216
Cdd:cd05373 158 ALAQSMARELGPKGIHVAhVIIDGGIDTDFIRERFPKRDERKEEDGilDPDAI 210
PRK05650 PRK05650
SDR family oxidoreductase;
10-189 8.36e-20

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 87.02  E-value: 8.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   10 VLITGCSSGIGLRIAVLLARD----------EQKRYHVIATMRdlkkkdrlvEAAGEVYGQtltllPLDICSDESVRQCV 79
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREgwrlaladvnEEGGEETLKLLR---------EAGGDGFYQ-----RCDVRDYSQLTALA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   80 NSVKDR--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDV 157
Cdd:PRK05650  69 QACEEKwgGIDVIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSS 148

                        170       180       190
                 ....*....|....*....|....*....|..
gi 37590327  158 YTASKFAIEGFCESMAVQLLKFNVKLSLIEPG 189
Cdd:PRK05650 149 YNVAKAGVVALSETLLVELADDEIGVHVVCPS 180
PRK05855 PRK05855
SDR family oxidoreductase;
6-254 1.00e-19

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 89.65  E-value: 1.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    6 GQKVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDL---KKKDRLVEAAG-EVYGQTLtllplDICSDESVRQCVNS 81
Cdd:PRK05855 314 SGKLVVVTGAGSGIGRETALAFAR---EGAEVVASDIDEaaaERTAELIRAAGaVAHAYRV-----DVSDADAMEAFAEW 385

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   82 VKDRH--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKR-QAGHIIIMSSVMGLQGVVFNDVY 158
Cdd:PRK05855 386 VRAEHgvPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERgTGGHIVNVASAAAYAPSRSLPAY 465

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  159 TASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFetkmmeeVAKMEYPGADPDTVRYFKDvyvpsSID-IFEAMGQT 237
Cdd:PRK05855 466 ATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNI-------VATTRFAGADAEDEARRRG-----RADkLYQRRGYG 533

                        250
                 ....*....|....*..
gi 37590327  238 PDDIAKCTKKVIETSQP 254
Cdd:PRK05855 534 PEKVAKAIVDAVKRNKA 550
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 7-194 1.19e-19

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: 86.28  E-value: 1.19e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   7 QKVVLITGCSSGIGLRIAVLLARDEQKryhVIATMR-DLKKKDRLVEAAGEVYGQTLtLLPLDICSDESVRQCVNSVKDR 85
Cdd:cd05358   3 GKVALVTGASSGIGKAIAIRLATAGAN---VVVNYRsKEDAAEEVVEEIKAVGGKAI-AVQADVSKEEDVVALFQSAIKE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 --HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKK-RQAGHIIIMSSVMGLQGVVFNDVYTASK 162
Cdd:cd05358  79 fgTLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKsKIKGKIINMSSVHEKIPWPGHVNYAASK 158

                       170       180       190
                ....*....|....*....|....*....|..
gi 37590327 163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:cd05358 159 GGVKMMTKTLAQEYAPKGIRVNAIAPGAINTP 190
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-263 1.41e-19

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 86.38  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKRyhVIATMRDLKKKDRLVEAAGEVYgqtltllPLDICSDESVRQCVNSV--KDR 85
Cdd:PRK06463   8 KVALITGGTRGIGRAIAEAFLREGAKV--AVLYNSAENEAKELREKGVFTI-------KCDVGNRDQVKKSKEVVekEFG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGL----QGVVFndvYTAS 161
Cdd:PRK06463  79 RVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIgtaaEGTTF---YAIT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  162 KFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFET--KMMEEVAKMEYPGADPDTVRYF-KDVYVpSSIDIFEAmgqtP 238
Cdd:PRK06463 156 KAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLsgKSQEEAEKLRELFRNKTVLKTTgKPEDI-ANIVLFLA----S 230

                        250       260
                 ....*....|....*....|....*
gi 37590327  239 DDIAKCTKKVIETSQPRFRNLTNSL 263
Cdd:PRK06463 231 DDARYITGQVIVADGGRIDNLTHSL 255
PRK08251 PRK08251
SDR family oxidoreductase;
8-194 1.78e-19

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 85.76  E-value: 1.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeqkryhviATMRDL----KKKDRLVEAAGEVYGQ----TLTLLPLDICSDESVRQCV 79
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFA----------AKGRDLalcaRRTDRLEELKAELLARypgiKVAVAALDVNDHDQVFEVF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   80 NSVKDR--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFN-D 156
Cdd:PRK08251  73 AEFRDElgGLDRVIVNAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRGLPGVkA 152

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 37590327  157 VYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK08251 153 AYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSE 190
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 8-199 2.33e-19

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 85.77  E-value: 2.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRdlkKKDRLVEAAGEVYGQTLTLLPL--DICSDESVRQCVNSVKDR 85
Cdd:PRK08213  13 KTALVTGGSRGLGLQIAEALGEAGAR---VVLSAR---KAEELEEAAAHLEALGIDALWIaaDVADEADIERLAEETLER 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 --HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPD-MKKRQAGHIIIMSSVMGLQGvvfND------ 156
Cdd:PRK08213  87 fgHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRsMIPRGYGRIINVASVAGLGG---NPpevmdt 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 37590327  157 -VYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGpvhtEFETKM 199
Cdd:PRK08213 164 iAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPG----FFPTKM 203
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 8-212 2.46e-19

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: 85.23  E-value: 2.46e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQkryHVIATMRDLkkkDRLVEAAGEVYGQTLTLlPLDICSDESVRQCVNSVKDRH- 86
Cdd:cd08944   4 KVAIVTGAGAGIGAACAARLAREGA---RVVVADIDG---GAAQAVVAQIAGGALAL-RVDVTDEQQVAALFERAVEEFg 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 -IDVLINNAGVGLLGP-VESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:cd08944  77 gLDLLVNNAGAMHLTPaIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAA 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 37590327 165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTEF-ETKMMEEVAKMEYPGAD 212
Cdd:cd08944 157 IRNLTRTLAAELRHAGIRCNALAPGLIDTPLlLAKLAGFEGALGPGGFH 205
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 1-200 3.09e-19

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 85.16  E-value: 3.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    1 MASGGGqKVVLITGCSSGIGLRIAVLLARDEQKRY----HVIATMRDLKKKDRLVEAAGevygQTLTLLPLDICSDESVR 76
Cdd:PRK12827   1 MASLDS-RRVLITGGSGGLGRAIAVRLAADGADVIvldiHPMRGRAEADAVAAGIEAAG----GKALGLAFDVRDFAATR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   77 QCVNSVKDRH--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEV-MPDMKKRQAGHIIIMSSVMGLQGVV 153
Cdd:PRK12827  76 AALDAGVEEFgrLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAAlPPMIRARRGGRIVNIASVAGVRGNR 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 37590327  154 FNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMM 200
Cdd:PRK12827 156 GQVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADNAA 202
PRK07775 PRK07775
SDR family oxidoreductase;
10-193 3.11e-19

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 85.58  E-value: 3.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   10 VLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKKKDRLVE----AAGEVYGqtltlLPLDICSDESVRQCVNSVKDR 85
Cdd:PRK07775  13 ALVAGASSGIGAATAIELA---AAGFPVALGARRVEKCEELVDkiraDGGEAVA-----FPLDVTDPDSVKSFVAQAEEA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 H--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:PRK07775  85 LgeIEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKA 164

                        170       180       190
                 ....*....|....*....|....*....|
gi 37590327  164 AIEGFCESMAVQLLKFNVKLSLIEPGPVHT 193
Cdd:PRK07775 165 GLEAMVTNLQMELEGTGVRASIVHPGPTLT 194
PRK09072 PRK09072
SDR family oxidoreductase;
7-176 3.21e-19

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 85.38  E-value: 3.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDLKKKDRLveAAGEVYGQTLTLLPLDICSdESVRQCVNSVKDRH 86
Cdd:PRK09072   5 DKRVLLTGASGGIGQALAEALAA---AGARLLLVGRNAEKLEAL--AARLPYPGRHRWVVADLTS-EAGREAVLARAREM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 --IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:PRK09072  79 ggINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFA 158

                        170
                 ....*....|..
gi 37590327  165 IEGFCESMAVQL 176
Cdd:PRK09072 159 LRGFSEALRREL 170
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 8-205 3.52e-19

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: 84.84  E-value: 3.52e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRdlkKKDRLVEAAGEV--YGqTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:cd08942   7 KIVLVTGGSRGIGRMIAQGFLEAGAR---VIISAR---KAEACADAAEELsaYG-ECIAIPADLSSEEGIEALVARVAER 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 --HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKK-RQAGH---IIIMSSVMGLQGVVF-NDVY 158
Cdd:cd08942  80 sdRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAaATAENparVINIGSIAGIVVSGLeNYSY 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 37590327 159 TASKFAIEGFCESMAVQLLKFNVKLSLIEPGPvhteFETKMMEEVAK 205
Cdd:cd08942 160 GASKAAVHQLTRKLAKELAGEHITVNAIAPGR----FPSKMTAFLLN 202
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 8-194 5.24e-19

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: 84.69  E-value: 5.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:cd05352   9 KVAIVTGGSRGIGLAIARALA---EAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFg 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 -IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVmglQGVVFND-----VYTA 160
Cdd:cd05352  86 kIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASM---SGTIVNRpqpqaAYNA 162

                       170       180       190
                ....*....|....*....|....*....|....
gi 37590327 161 SKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:cd05352 163 SKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTD 196
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
7-205 2.66e-18

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 82.85  E-value: 2.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLARDEQKryhvIATMrdlkkkDRLVEAAGEV------YGQTLTLLPLDICSDESVRQCVN 80
Cdd:PRK08643   2 SKVALVTGAGQGIGFAIAKRLVEDGFK----VAIV------DYNEETAQAAadklskDGGKAIAVKADVSDRDQVFAAVR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   81 SVKDR--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKR-QAGHIIIMSSVMGLQGVVFNDV 157
Cdd:PRK08643  72 QVVDTfgDLNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLgHGGKIINATSQAGVVGNPELAV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 37590327  158 YTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVhtefETKMMEEVAK 205
Cdd:PRK08643 152 YSSTKFAVRGLTQTAARDLASEGITVNAYAPGIV----KTPMMFDIAH 195
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 8-193 7.33e-18

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: 81.34  E-value: 7.33e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKKKDRLVEAAGEvYGQTLTLLPLDICSDESVRQCVNSVKDR-- 85
Cdd:cd05329   7 KTALVTGGTKGIGYAIVEELA---GLGAEVYTCARNQKELDECLTEWRE-KGFKVEGSVCDVSSRSERQELMDTVASHfg 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 -HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:cd05329  83 gKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGA 162

                       170       180
                ....*....|....*....|....*....
gi 37590327 165 IEGFCESMAVQLLKFNVKLSLIEPGPVHT 193
Cdd:cd05329 163 LNQLTRSLACEWAKDNIRVNAVAPWVIAT 191
PRK08589 PRK08589
SDR family oxidoreductase;
8-193 7.47e-18

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 81.75  E-value: 7.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIAtmrdLKKKDRLVEAAGEVY--GQTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:PRK08589   7 KVAVITGASTGIGQASAIALA---QEGAYVLA----VDIAEAVSETVDKIKsnGGKAKAYHVDISDEQQVKDFASEIKEQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 --HIDVLINNAGV-GLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKrQAGHIIIMSSVMGLQGVVFNDVYTASK 162
Cdd:PRK08589  80 fgRVDVLFNNAGVdNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMME-QGGSIINTSSFSGQAADLYRSGYNAAK 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 37590327  163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHT 193
Cdd:PRK08589 159 GAVINFTKSIAIEYGRDGIRANAIAPGTIET 189
PRK09242 PRK09242
SDR family oxidoreductase;
6-207 8.70e-18

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 81.33  E-value: 8.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    6 GQKVvLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDRLVEAAGEVY-GQTLTLLPLDICSDESVRQCVNSVKD 84
Cdd:PRK09242   9 GQTA-LITGASKGIGLAIAREFLGLGAD---VLIVARDADALAQARDELAEEFpEREVHGLAADVSDDEDRRAILDWVED 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   85 R--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASK 162
Cdd:PRK09242  85 HwdGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMTK 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 37590327  163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKME 207
Cdd:PRK09242 165 AALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDYYE 209
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 1-215 8.93e-18

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


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 81.43  E-value: 8.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   1 MASGG--GQKVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDlkkkdrlvEAAGEVYGQTLT--------LLPLDIC 70
Cdd:cd08933   1 MASGLryADKVVIVTGGSRGIGRGIVRAFVENGAK---VVFCARG--------EAAGQALESELNragpgsckFVPCDVT 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  71 SDESVRQCVNSVKDRH--IDVLINNAGVGL-LGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQaGHIIIMSSVM 147
Cdd:cd08933  70 KEEDIKTLISVTVERFgrIDCLVNNAGWHPpHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQ-GNIINLSSLV 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37590327 148 GLQGVVFNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHtefeTKMMEEVAkmeypGADPDT 215
Cdd:cd08933 149 GSIGQKQAAPYVATKGAITAMTKALAVDESRYGVRVNCISPGNIW----TPLWEELA-----AQTPDT 207
PRK06139 PRK06139
SDR family oxidoreductase;
8-193 9.07e-18

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 82.46  E-value: 9.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIA----------VLLARDEQKRYHVIATMRDLkkkdrlveaagevyGQTLTLLPLDICSDESVRQ 77
Cdd:PRK06139   8 AVVVITGASSGIGQATAeafarrgarlVLAARDEEALQAVAEECRAL--------------GAEVLVVPTDVTDADQVKA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   78 CVNSVKD--RHIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFN 155
Cdd:PRK06139  74 LATQAASfgGRIDVWVNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYA 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 37590327  156 DVYTASKFAIEGFCESMAVQLLKF-NVKLSLIEPGPVHT 193
Cdd:PRK06139 154 AAYSASKFGLRGFSEALRGELADHpDIHVCDVYPAFMDT 192
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 8-194 1.37e-17

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: 80.74  E-value: 1.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQKryhviATMRDLKkkdrlVEAAGEV---YGQTLTLLPLDICSDESVRQCVNSVKD 84
Cdd:cd05363   4 KTALITGSARGIGRAFAQAYVREGAR-----VAIADIN-----LEAARATaaeIGPAACAISLDVTDQASIDRCVAALVD 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  85 R--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKR-QAGHIIIMSSVMGLQGVVFNDVYTAS 161
Cdd:cd05363  74 RwgSIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMASQAGRRGEALVGVYCAT 153

                       170       180       190
                ....*....|....*....|....*....|...
gi 37590327 162 KFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:cd05363 154 KAAVISLTQSAGLNLIRHGINVNAIAPGVVDGE 186
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 8-203 1.83e-17

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 80.05  E-value: 1.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKK-DRLVEAAGEvYGQTLTLLPLDICSDESVRQCVNSVKDR- 85
Cdd:PRK12935   7 KVAIVTGGAKGIGKAITVALAQEGAK---VVINYNSSKEAaENLVNELGK-EGHDVYAVQADVSKVEDANRLVEEAVNHf 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 -HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:PRK12935  83 gKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAG 162

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 37590327  165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEV 203
Cdd:PRK12935 163 MLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEEV 201
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 9-242 3.13e-17

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 79.46  E-value: 3.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   9 VVLITGCSSGIGLRIAVLLardEQKRYHVIATmrDLKKKDrlVEAagevygqtltllplDICSDESVRQCVNSVKDRH-- 86
Cdd:cd05328   1 TIVITGAASGIGAATAELL---EDAGHTVIGI--DLREAD--VIA--------------DLSTPEGRAAAIADVLARCsg 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 -IDVLINNAGVGLLGPVESismdemkrVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFND--------- 156
Cdd:cd05328  60 vLDGLVNCAGVGGTTVAGL--------VLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAGWAQDKLelakalaag 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327 157 ------------------VYTASKFAIEGFCESMAVQ-LLKFNVKLSLIEPGPVhtefETKMMEEVAKMEypgadpdtvR 217
Cdd:cd05328 132 tearavalaehagqpgylAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPV----ETPILQAFLQDP---------R 198

                       250       260
                ....*....|....*....|....*...
gi 37590327 218 YfkdvyvPSSIDIFEA-MGQ--TPDDIA 242
Cdd:cd05328 199 G------GESVDAFVTpMGRraEPDEIA 220
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 7-225 3.37e-17

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 79.64  E-value: 3.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   7 QKVVLITGCSSGIGLRIAVLLARdeQKRYHVIAtmrDLKKKDRLVEAAGevyGQTLTLLPLDICSDESVRQCVNSVKDRH 86
Cdd:cd05371   2 GLVAVVTGGASGLGLATVERLLA--QGAKVVIL---DLPNSPGETVAKL---GDNCRFVPVDVTSEKDVKAALALAKAKF 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 --IDVLINNAGVGLLGPV------ESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQA------GHIIIMSSVMGLQGV 152
Cdd:cd05371  74 grLDIVVNCAGIAVAAKTynkkgqQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNEPdqggerGVIINTASVAAFEGQ 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37590327 153 VFNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPvhteFETKMMeevAKMeypgadPDTVRYFKDVYVP 225
Cdd:cd05371 154 IGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGL----FDTPLL---AGL------PEKVRDFLAKQVP 213
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 8-191 3.64e-17

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: 79.30  E-value: 3.64e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:cd08930   3 KIILITGAAGLIGKAFCKALL---SAGARLILADINAPALEQLKEELTNLYKNRVIALELDITSKESIKELIESYLEKFg 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 -IDVLINNAGV---GLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFND------ 156
Cdd:cd08930  80 rIDILINNAYPspkVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIAPDFRIyentqm 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 37590327 157 ----VYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPV 191
Cdd:cd08930 160 yspvEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGI 198
PRK06484 PRK06484
short chain dehydrogenase; Validated
 8-217 4.40e-17

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 81.43  E-value: 4.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDLKKKDRLVEAAGEVYgqtlTLLPLDICSDESVRQCVNSVKDR-- 85
Cdd:PRK06484   6 RVVLVTGAAGGIGRAACQRFARAG---DQVVVADRNVERARERADSLGPDH----HALAMDVSDEAQIREGFEQLHREfg 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 HIDVLINNAGVglLGPVES----ISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIII-MSSVMGLQGVVFNDVYTA 160
Cdd:PRK06484  79 RIDVLVNNAGV--TDPTMTatldTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAAIVnVASGAGLVALPKRTAYSA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 37590327  161 SKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFetkmmeeVAKMEYPGA-DPDTVR 217
Cdd:PRK06484 157 SKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQM-------VAELERAGKlDPSAVR 207
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 8-194 4.52e-17

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: 79.04  E-value: 4.52e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQKRyhVIATMRDLKKKDRLVEAAGEvygqTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAREGARV--VVNYYRSTESAEAVAAEAGE----RAIAIQADVRDRDQVQAMIEEAKNHFg 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 -IDVLINNAgvglLGP----------VESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFN 155
Cdd:cd05349  75 pVDTIVNNA----LIDfpfdpdqrktFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPY 150

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 37590327 156 DVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:cd05349 151 HDYTTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKVT 189
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 8-201 4.92e-17

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 79.12  E-value: 4.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLlPLDICSDESVRQCVNSVKDR-- 85
Cdd:PRK06113  12 KCAIITGAGAGIGKEIAITFA---TAGASVVVSDINADAANHVVDEIQQLGGQAFAC-RCDITSEQELSALADFALSKlg 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 HIDVLINNAGVGLLGPVEsISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:PRK06113  88 KVDILVNNAGGGGPKPFD-MPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAA 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 37590327  166 EGFCESMAVQLLKFNVKLSLIEPGPVHT---------EFETKMME 201
Cdd:PRK06113 167 SHLVRNMAFDLGEKNIRVNGIAPGAILTdalksvitpEIEQKMLQ 211
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 8-213 6.41e-17

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: 78.39  E-value: 6.41e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIA----------VLLARDEQKryhviatmrdLKKKDRLVEAAGEVYGQTLTLlPLDICSDESVRQ 77
Cdd:cd05340   5 RIILVTGASDGIGREAAltyarygatvILLGRNEEK----------LRQVADHINEEGGRQPQWFIL-DLLTCTSENCQQ 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  78 CVNSVKDRH--IDVLINNAG-VGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVF 154
Cdd:cd05340  74 LAQRIAVNYprLDGVLHNAGlLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRAN 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 37590327 155 NDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMmeevakmeYPGADP 213
Cdd:cd05340 154 WGAYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRASA--------FPTEDP 204
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 8-242 7.80e-17

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: 78.59  E-value: 7.80e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDRLVEAAGEvygqTLTLLPLDICSDESVRQCVNSVKDR-- 85
Cdd:cd05345   6 KVAIVTGAGSGFGEGIARRFAQEGAR---VVIADINADGAERVAADIGE----AAIAIQADVTKRADVEAMVEAALSKfg 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 HIDVLINNAGVGLL-GPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQ---GVVFndvYTAS 161
Cdd:cd05345  79 RLDILVNNAGITHRnKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRprpGLTW---YNAS 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327 162 KFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMeevakmeypgaDPDTvryfkdvyvPSSIDIFEA---MGQ-- 236
Cdd:cd05345 156 KGWVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFM-----------GEDT---------PENRAKFRAtipLGRls 215


                ....*.
gi 37590327 237 TPDDIA 242
Cdd:cd05345 216 TPDDIA 221
PRK07063 PRK07063
SDR family oxidoreductase;
8-194 8.58e-17

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 78.55  E-value: 8.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARdEQKRyhVIATMRDLKKKDRLVEA-AGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH 86
Cdd:PRK07063   8 KVALVTGAAQGIGAAIARAFAR-EGAA--VALADLDAALAERAAAAiARDVAGARVLAVPADVTDAASVAAAVAAAEEAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 --IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:PRK07063  85 gpLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPVAKHG 164

                        170       180       190
                 ....*....|....*....|....*....|
gi 37590327  165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK07063 165 LLGLTRALGIEYAARNVRVNAIAPGYIETQ 194
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 7-148 1.20e-16

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: 79.10  E-value: 1.20e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   7 QKVVLITGCSSGIGLRIA-VLLARDEqkrYHVIATMRDLKKKDRLVEAAGeVYGQTLTLLPLDICSDESVRQCVNSVK-- 83
Cdd:cd09810   1 KGTVVITGASSGLGLAAAkALARRGE---WHVVMACRDFLKAEQAAQEVG-MPKDSYSVLHCDLASLDSVRQFVDNFRrt 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37590327  84 DRHIDVLINNAGVGL-LGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGH--IIIMSSVMG 148
Cdd:cd09810  77 GRPLDALVCNAAVYLpTAKEPRFTADGFELTVGVNHLGHFLLTNLLLEDLQRSENASprIVIVGSITH 144
PRK06484 PRK06484
short chain dehydrogenase; Validated
 8-193 1.22e-16

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 80.28  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDRLVEAAGevyGQTLTLlPLDICSDESVRQCVNSVKDR-- 85
Cdd:PRK06484 270 RVVAITGGARGIGRAVADRFAAAGDR---LLIIDRDAEGAKKLAEALG---DEHLSV-QADITDEAAVESAFAQIQARwg 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 HIDVLINNAGVG-LLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMkkRQAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:PRK06484 343 RLDVLVNNAGIAeVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLLALPPRNAYCASKAA 420

                        170       180
                 ....*....|....*....|....*....
gi 37590327  165 IEGFCESMAVQLLKFNVKLSLIEPGPVHT 193
Cdd:PRK06484 421 VTMLSRSLACEWAPAGIRVNTVAPGYIET 449
PRK06949 PRK06949
SDR family oxidoreductase;
8-194 1.30e-16

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 77.88  E-value: 1.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKRyhVIATMRdlkkKDRLVE--AAGEVYGQTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:PRK06949  10 KVALVTGASSGLGARFAQVLAQAGAKV--VLASRR----VERLKElrAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 --HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQ--------AGHIIIMSSVMGLQGVVFN 155
Cdd:PRK06949  84 agTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAkgagntkpGGRIINIASVAGLRVLPQI 163

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 37590327  156 DVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK06949 164 GLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTE 202
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 11-189 2.24e-16

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 77.12  E-value: 2.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   11 LITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLlPLDICSDESVRQCVNSVKDRH--ID 88
Cdd:PRK07523  14 LVTGSSQGIGYALAEGLA---QAGAEVILNGRDPAKLAAAAESLKGQGLSAHAL-AFDVTDHDAVRAAIDAFEAEIgpID 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   89 VLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSV---MGLQGVVfndVYTASKFAI 165
Cdd:PRK07523  90 ILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVqsaLARPGIA---PYTATKGAV 166

                        170       180
                 ....*....|....*....|....
gi 37590327  166 EGFCESMAVQLLKFNVKLSLIEPG 189
Cdd:PRK07523 167 GNLTKGMATDWAKHGLQCNAIAPG 190
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-206 2.97e-16

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 76.68  E-value: 2.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKRyhVIATMRDLKKKDRLVEAAGEVYGQTLTLLPlDICSDESVRQCVNSVKDRH- 86
Cdd:PRK06077   7 KVVVVTGSGRGIGRAIAVRLAKEGSLV--VVNAKKRAEEMNETLKMVKENGGEGIGVLA-DVSTREGCETLAKATIDRYg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 -IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMkkRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:PRK06077  84 vADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAGIRPAYGLSIYGAMKAAV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 37590327  166 EGFCESMAVQlLKFNVKLSLIEPGPVhtefETKMMEEVAKM 206
Cdd:PRK06077 162 INLTKYLALE-LAPKIRVNAIAPGFV----KTKLGESLFKV 197
PRK07024 PRK07024
SDR family oxidoreductase;
10-193 3.03e-16

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 76.89  E-value: 3.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   10 VLITGCSSGIGLRIAV----------LLARdeqkRYHVI-ATMRDLKKKDRLveaagEVYgqtltllPLDICSDESVRQC 78
Cdd:PRK07024   5 VFITGASSGIGQALAReyarqgatlgLVAR----RTDALqAFAARLPKAARV-----SVY-------AADVRDADALAAA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   79 VNSVKDRH--IDVLINNAGVG---LLGPVESIsmDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVV 153
Cdd:PRK07024  69 AADFIAAHglPDVVIANAGISvgtLTEEREDL--AVFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLP 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 37590327  154 FNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHT 193
Cdd:PRK07024 147 GAGAYSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRT 186
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 8-193 3.43e-16

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: 77.43  E-value: 3.43e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAV-LLARD-EQKRYHVIATMRDLKKKDRLVEAAGEVYGQ---TLTLLPLDICSDESVRQCVNSV 82
Cdd:cd08941   2 KVVLVTGANSGLGLAICErLLAEDdENPELTLILACRNLQRAEAACRALLASHPDarvVFDYVLVDLSNMVSVFAAAKEL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  83 KDR--HIDVLINNAGVG--------------LLGPVESIS-------------------MDEMKRVFETNFFGTVRMIKE 127
Cdd:cd08941  82 KKRypRLDYLYLNAGIMpnpgidwigaikevLTNPLFAVTnptykiqaegllsqgdkatEDGLGEVFQTNVFGHYYLIRE 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37590327 128 VMPDMKKRQA-GHIIIMSSVMG---------LQGVVFNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHT 193
Cdd:cd08941 162 LEPLLCRSDGgSQIIWTSSLNAspkyfsledIQHLKGPAPYSSSKYLVDLLSLALNRKFNKLGVYSYVVHPGICTT 237
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 9-194 4.39e-16

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: 76.07  E-value: 4.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   9 VVLITGCSSGIGLRIAVLLARDEQKRyhVIAtmrDLKKKD-RLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDR-- 85
Cdd:cd05365   1 VAIVTGGAAGIGKAIAGTLAKAGASV--VIA---DLKSEGaEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQfg 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 HIDVLINNAGVGLLGPVE-SISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:cd05365  76 GITILVNNAGGGGPKPFDmPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAA 155

                       170       180       190
                ....*....|....*....|....*....|
gi 37590327 165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:cd05365 156 VNHMTRNLAFDLGPKGIRVNAVAPGAVKTD 185
PRK06500 PRK06500
SDR family oxidoreductase;
8-193 1.06e-15

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 75.38  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArDEQKRyhVIATMRDLKKkdrlVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDR-- 85
Cdd:PRK06500   7 KTALITGGTSGIGLETARQFL-AEGAR--VAITGRDPAS----LEAARAELGESALVIRADAGDVAAQKALAQALAEAfg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAghIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:PRK06500  80 RLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPAS--IVLNGSINAHIGMPNSSVYAASKAAL 157

                        170       180
                 ....*....|....*....|....*...
gi 37590327  166 EGFCESMAVQLLKFNVKLSLIEPGPVHT 193
Cdd:PRK06500 158 LSLAKTLSGELLPRGIRVNAVSPGPVQT 185
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
7-194 1.28e-15

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 75.14  E-value: 1.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDR- 85
Cdd:PRK08063   4 GKVALVTGSSRGIGKAIALRLA---EEGYDIAVNYARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEf 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 -HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSvMGLQGVVFNdvYTA---S 161
Cdd:PRK08063  81 gRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSS-LGSIRYLEN--YTTvgvS 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 37590327  162 KFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK08063 158 KAALEALTRYLAVELAPKGIAVNAVSGGAVDTD 190
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-199 1.55e-15

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 76.80  E-value: 1.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQkryHVIATmrDL-KKKDRLVEAAGEVYGqtlTLLPLDICSDESVRQCVNSVKDRH 86
Cdd:PRK08261 211 KVALVTGAARGIGAAIAEVLARDGA---HVVCL--DVpAAGEALAAVANRVGG---TALALDITAPDAPARIAEHLAERH 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 --IDVLINNAGVG---LLGpvesiSMDEMK--RVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYT 159
Cdd:PRK08261 283 ggLDIVVHNAGITrdkTLA-----NMDEARwdSVLAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGIAGNRGQTNYA 357

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 37590327  160 ASKFAIEGFCESMAVQLLKFNVKLSLIEPGpvhteF-ETKM 199
Cdd:PRK08261 358 ASKAGVIGLVQALAPLLAERGITINAVAPG-----FiETQM 393
PRK12743 PRK12743
SDR family oxidoreductase;
8-210 1.64e-15

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 74.68  E-value: 1.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLAR---DEQKRYHviATMRDLKKKDRLVEAAgevyGQTLTLLPLDICSDESVRQCVNSVKD 84
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQqgfDIGITWH--SDEEGAKETAEEVRSH----GVRAEIRQLDLSDLPEGAQALDKLIQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   85 R--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKR-QAGHIIIMSSVMGLQGVVFNDVYTAS 161
Cdd:PRK12743  77 RlgRIDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQgQGGRIINITSVHEHTPLPGASAYTAA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 37590327  162 KFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYPG 210
Cdd:PRK12743 157 KHALGGLTKAMALELVEHGILVNAVAPGAIATPMNGMDDSDVKPDSRPG 205
PRK07069 PRK07069
short chain dehydrogenase; Validated
 11-206 2.61e-15

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 74.36  E-value: 2.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   11 LITGCSSGIGLRIAVLLARDEQKRYhvIATMRDLKKKDRLVEAAGEVYG-QTLTLLPLDICSDESVRQCVNSVKD--RHI 87
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVF--LTDINDAAGLDAFAAEINAAHGeGVAFAAVQDVTDEAQWQALLAQAADamGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   88 DVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAIEG 167
Cdd:PRK07069  81 SVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVAS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 37590327  168 FCESMAVQLLKFNVKlslIEPGPVHTEF-ETKMMEEVAKM 206
Cdd:PRK07069 161 LTKSIALDCARRGLD---VRCNSIHPTFiRTGIVDPIFQR 197
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
8-165 2.64e-15

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 76.42  E-value: 2.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQkryHVIATMRDLkkkDRLVEAAGEVYGQTLTL-LPLDICSDESVRQCVNSVKDRH 86
Cdd:PRK08324 423 KVALVTGAAGGIGKATAKRLAAEGA---CVVLADLDE---EAAEAAAAELGGPDRALgVACDVTDEAAVQAAFEEAALAF 496

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 --IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKrqaghiiimssvMGLQGVVfndVYTASKFA 164
Cdd:PRK08324 497 ggVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKA------------QGLGGSI---VFIASKNA 561


                 .
gi 37590327  165 I 165
Cdd:PRK08324 562 V 562
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
7-146 2.78e-15

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


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 75.03  E-value: 2.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   7 QKVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDLKKKDRLVEAAGEVYGQtLTLLPLDICSDESVRQCVNSVK--D 84
Cdd:COG5748   6 KSTVIITGASSGVGLYAAKALAD---RGWHVIMACRDLEKAEAAAQELGIPPDS-YTIIHIDLASLESVRRFVADFRalG 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37590327  85 RHIDVLINNAGV---GLLGPVESISMDEMKrvFETNFFGTVRMIKEVMPDMKKRQAG--HIIIMSSV 146
Cdd:COG5748  82 RPLDALVCNAAVyypLLKEPLRSPDGYELS--VATNHLGHFLLCNLLLEDLKKSPASdpRLVILGTV 146
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 8-193 3.38e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 74.00  E-value: 3.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKRyhVIATMRDLKKKdrlvEAAGEVYGqtlTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:PRK06057   8 RVAVITGGGSGIGLATARRLAAEGATV--VVGDIDPEAGK----AAADEVGG---LFVPTDVTDEDAVNALFDTAAETYg 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 -IDVLINNAGVGllgPVE--SI---SMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDV-YT 159
Cdd:PRK06057  79 sVDIAFNNAGIS---PPEddSIlntGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSATSQIsYT 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 37590327  160 ASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHT 193
Cdd:PRK06057 156 ASKGGVLAMSRELGVQFARQGIRVNALCPGPVNT 189
PRK06947 PRK06947
SDR family oxidoreductase;
8-194 3.50e-15

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 73.69  E-value: 3.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHV-IATMRDLKKKDRLVEAAGEVYGQTLTLLPlDICSDESVRQCVNSVKDR- 85
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAA---ARGWSVgINYARDAAAAEETADAVRAAGGRACVVAG-DVANEADVIAMFDAVQSAf 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 -HIDVLINNAG-VGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGH---IIIMSSVMGLQGVVFNDV-YT 159
Cdd:PRK06947  79 gRLDALVNNAGiVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGGRggaIVNVSSIASRLGSPNEYVdYA 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 37590327  160 ASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK06947 159 GSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETE 193
PRK08177 PRK08177
SDR family oxidoreductase;
8-194 3.51e-15

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 73.14  E-value: 3.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDLKKKDRLvEAAGEVYGQTLtllplDICSDESVRQCVNSVKDRHI 87
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERG---WQVTATVRGPQQDTAL-QALPGVHIEKL-----DMNDPASLDQLLQRLQGQRF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   88 DVLINNAGVglLGP----VESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQaGHIIIMSSVMGlqGVVFND-----VY 158
Cdd:PRK08177  73 DLLFVNAGI--SGPahqsAADATAAEIGQLFLTNAIAPIRLARRLLGQVRPGQ-GVLAFMSSQLG--SVELPDggempLY 147

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 37590327  159 TASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK08177 148 KASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTD 183
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 8-193 4.25e-15

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 73.61  E-value: 4.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKRyhVIATMRDLKKKDRLVEAAGEVYGQTLTLLPlDICSDESVRQCVNSVKDR-- 85
Cdd:PRK08936   8 KVVVITGGSTGLGRAMAVRFGKEKAKV--VINYRSDEEEANDVAEEIKKAGGEAIAVKG-DVTVESDVVNLIQTAVKEfg 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 HIDVLINNAGVGLLGPVESISMDEMKRVFETN----FFGTVRMIKEVMPDMKKrqaGHIIIMSSVMGLQGVVFNDVYTAS 161
Cdd:PRK08936  85 TLDVMINNAGIENAVPSHEMSLEDWNKVINTNltgaFLGSREAIKYFVEHDIK---GNIINMSSVHEQIPWPLFVHYAAS 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 37590327  162 KFAIEGFCESMAVQLLKFNVKLSLIEPGPVHT 193
Cdd:PRK08936 162 KGGVKLMTETLAMEYAPKGIRVNNIGPGAINT 193
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 8-194 4.25e-15

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: 73.66  E-value: 4.25e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDRLVEaagevygQTLTLLPL--DICSDESVRQCVNSVKDr 85
Cdd:cd05351   8 KRALVTGAGKGIGRATVKALAKAGAR---VVAVSRTQADLDSLVR-------ECPGIEPVcvDLSDWDATEEALGSVGP- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 hIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQA-GHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:cd05351  77 -VDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVpGSIVNVSSQASQRALTNHTVYCSTKAA 155

                       170       180       190
                ....*....|....*....|....*....|
gi 37590327 165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:cd05351 156 LDMLTKVMALELGPHKIRVNSVNPTVVMTD 185
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 8-215 5.08e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 73.43  E-value: 5.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDRLVE---AAGevyGQTLTlLPLDICSDESVRQCVNSVKD 84
Cdd:PRK07478   7 KVAIITGASSGIGRAAAKLFAREGAK---VVVGARRQAELDQLVAeirAEG---GEAVA-LAGDVRDEAYAKALVALAVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   85 RH--IDVLINNAG-VGLLGPVESISMDEMKRVFETN----FFGTvrmiKEVMPDMKKRQAGHIIIMSSVMG----LQGVV 153
Cdd:PRK07478  80 RFggLDIAFNNAGtLGEMGPVAEMSLEGWRETLATNltsaFLGA----KHQIPAMLARGGGSLIFTSTFVGhtagFPGMA 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37590327  154 fndVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMmeevakmeypGADPDT 215
Cdd:PRK07478 156 ---AYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAM----------GDTPEA 204
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 8-168 5.67e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 73.85  E-value: 5.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDlkkKDRLVEAAGEVYGQTLTL-LPLDICSDESVRQCVNSVKDRH 86
Cdd:PRK05872  10 KVVVVTGAARGIGAELARRLHA---RGAKLALVDLE---EAELAALAAELGGDDRVLtVVADVTDLAAMQAAAEEAVERF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 --IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRqAGHIIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:PRK05872  84 ggIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIER-RGYVLQVSSLAAFAAAPGMAAYCASKAG 162


                 ....
gi 37590327  165 IEGF 168
Cdd:PRK05872 163 VEAF 166
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 8-189 7.91e-15

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 72.76  E-value: 7.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTL-LPLDICSDESVRQCVNSVKDR- 85
Cdd:PRK12384   3 QVAVVIGGGQTLGAFLCHGLA---EEGYRVAVADINSEKAANVAQEINAEYGEGMAYgFGADATSEQSVLALSRGVDEIf 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 -HIDVLINNAGVGLLGPVESISMDEMKRVFETN---FFGTVRMIKEVMpdMKKRQAGHIIIMSSVMGLQGVVFNDVYTAS 161
Cdd:PRK12384  80 gRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNlvgYFLCAREFSRLM--IRDGIQGRIIQINSKSGKVGSKHNSGYSAA 157

                        170       180
                 ....*....|....*....|....*...
gi 37590327  162 KFAIEGFCESMAVQLLKFNVKLSLIEPG 189
Cdd:PRK12384 158 KFGGVGLTQSLALDLAEYGITVHSLMLG 185
PLN02253 PLN02253
xanthoxin dehydrogenase
 8-207 8.99e-15

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 73.32  E-value: 8.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKRyhVIATMRDlKKKDRLVEAAGEvyGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:PLN02253  19 KVALVTGGATGIGESIVRLFHKHGAKV--CIVDLQD-DLGQNVCDSLGG--EPNVCFFHCDVTVEDDVSRAVDFTVDKFg 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 -IDVLINNAGVGllGP----VESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTAS 161
Cdd:PLN02253  94 tLDIMVNNAGLT--GPpcpdIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGPHAYTGS 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 37590327  162 KFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKME 207
Cdd:PLN02253 172 KHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALAHLPEDERTE 217
PRK07774 PRK07774
SDR family oxidoreductase;
8-194 1.17e-14

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 72.47  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKRyhVIAtmrdlkkkDRLVEAAGEVY------GQTLTLLPLDICSDESVRQCVNS 81
Cdd:PRK07774   7 KVAIVTGAAGGIGQAYAEALAREGASV--VVA--------DINAEGAERVAkqivadGGTAIAVQVDVSDPDSAKAMADA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   82 VKDRH--IDVLINNAGV--GL-LGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLqgvVFND 156
Cdd:PRK07774  77 TVSAFggIDYLVNNAAIygGMkLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAW---LYSN 153

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 37590327  157 VYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK07774 154 FYGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTE 191
PRK07035 PRK07035
SDR family oxidoreductase;
8-195 1.51e-14

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 71.97  E-value: 1.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKK----KDRLVEAAGEVygqtlTLLPLDICSDESVRQCVNSVK 83
Cdd:PRK07035   9 KIALVTGASRGIGEAIAKLLA---QQGAHVIVSSRKLDGcqavADAIVAAGGKA-----EALACHIGEMEQIDALFAHIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   84 DRH--IDVLINNAGVG-LLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTA 160
Cdd:PRK07035  81 ERHgrLDILVNNAAANpYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 37590327  161 SKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEF 195
Cdd:PRK07035 161 TKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKF 195
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 6-202 1.70e-14

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 71.87  E-value: 1.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    6 GQKVvLITGCSSGIGLRIAVLLardeqkryHVIATMRDL--KKKDRLVEAAGEVyGQTLTLLPLDICSDESVRQCVNSVK 83
Cdd:PRK12936   6 GRKA-LVTGASGGIGEEIARLL--------HAQGAIVGLhgTRVEKLEALAAEL-GERVKIFPANLSDRDEVKALGQKAE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   84 D--RHIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTAS 161
Cdd:PRK12936  76 AdlEGVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCAS 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 37590327  162 KFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEE 202
Cdd:PRK12936 156 KAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDK 196
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 8-200 1.79e-14

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: 72.11  E-value: 1.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDRLVEAAGEVYGQTLTLLP--LDICSDESVRQCVNSvKDR 85
Cdd:cd08935   6 KVAVITGGTGVLGGAMARALAQAGAK---VAALGRNQEKGDKVAKEITALGGRAIALAAdvLDRASLERAREEIVA-QFG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 HIDVLINNAG---------VGLLGPVESISMDEM-----KRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQG 151
Cdd:cd08935  82 TVDILINGAGgnhpdattdPEHYEPETEQNFFDLdeegwEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSP 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 37590327 152 VVFNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMM 200
Cdd:cd08935 162 LTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLL 210
PRK07074 PRK07074
SDR family oxidoreductase;
7-216 3.29e-14

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 71.34  E-value: 3.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLARDEQkryHVIATMRDLKKKDRLVEAAGEvygQTLTLLPLDICSDESVRQCV-NSVKDR 85
Cdd:PRK07074   2 KRTALVTGAAGGIGQALARRFLAAGD---RVLALDIDAAALAAFADALGD---ARFVPVACDLTDAASLAAALaNAAAER 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 H-IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQgVVFNDVYTASKFA 164
Cdd:PRK07074  76 GpVDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGMA-ALGHPAYSAAKAG 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37590327  165 IEGFCESMAVQLLKFNVKLSLIEPGPVHTE-FETKMME-----EVAKMEYP---GADPDTV 216
Cdd:PRK07074 155 LIHYTKLLAVEYGRFGIRANAVAPGTVKTQaWEARVAAnpqvfEELKKWYPlqdFATPDDV 215
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 8-193 3.39e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 71.25  E-value: 3.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDRLVEA---AG-EVYGqtltlLPLDICSDESVRQCVNSVK 83
Cdd:PRK07097  11 KIALITGASYGIGFAIAKAYAKAGAT---IVFNDINQELVDKGLAAyreLGiEAHG-----YVCDVTDEDGVQAMVSQIE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   84 DRH--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVM---GLQGVVfndVY 158
Cdd:PRK07097  83 KEVgvIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMselGRETVS---AY 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 37590327  159 TASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHT 193
Cdd:PRK07097 160 AAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIAT 194
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 7-216 4.69e-14

(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: 70.43  E-value: 4.69e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   7 QKVVLITGCSSGIGLRIAVLLARDEQKryhVIatMRDLKkkdrlveaaGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH 86
Cdd:cd05353   5 GRVVLVTGAGGGLGRAYALAFAERGAK---VV--VNDLG---------GDRKGSGKSSSAADKVVDEIKAAGGKAVANYD 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 ------------------IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMG 148
Cdd:cd05353  71 svedgekivktaidafgrVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAG 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37590327 149 LQGVVFNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPvhtefETKMMEEVakMEYPGAD---PDTV 216
Cdd:cd05353 151 LYGNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPAA-----GSRMTETV--MPEDLFDalkPEYV 214
PRK07102 PRK07102
SDR family oxidoreductase;
8-216 1.05e-13

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 69.57  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDlkkKDRLVEAAGEV---YGQTLTLLPLDICSDESVRQCVNSVKD 84
Cdd:PRK07102   2 KKILIIGATSDIARACARRYA---AAGARLYLAARD---VERLERLADDLrarGAVAVSTHELDILDTASHAAFLDSLPA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   85 RHIDVLInnaGVGLLGPVESI--SMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASK 162
Cdd:PRK07102  76 LPDIVLI---AVGTLGDQAACeaDPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSAK 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 37590327  163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVhtefETKMMEEvakMEYPG---ADPDTV 216
Cdd:PRK07102 153 AALTAFLSGLRNRLFKSGVHVLTVKPGFV----RTPMTAG---LKLPGpltAQPEEV 202
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 8-194 2.36e-13

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


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 68.71  E-value: 2.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRD---LKKKDRLVEAAGEVYGQTltllpLDICSDESVRQCVNSVKD 84
Cdd:cd08937   5 KVVVVTGAAQGIGRGVAERLA---GEGARVLLVDRSelvHEVLAEILAAGDAAHVHT-----ADLETYAGAQGVVRAAVE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  85 RH--IDVLINNAGVGLLG-PVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVmGLQGvVFNDVYTAS 161
Cdd:cd08937  77 RFgrVDVLINNVGGTIWAkPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSI-ATRG-IYRIPYSAA 154

                       170       180       190
                ....*....|....*....|....*....|...
gi 37590327 162 KFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:cd08937 155 KGGVNALTASLAFEHARDGIRVNAVAPGGTEAP 187
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-207 2.70e-13

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 68.45  E-value: 2.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLLpLDICSDESVRQCVNSVKDR- 85
Cdd:PRK08217   5 DKVIVITGGAQGLGRAMAEYLA---QKGAKLALIDLNQEKLEEAVAECGALGTEVRGYA-ANVTDEEDVEATFAQIAEDf 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 -HIDVLINNAGV---GLL-----GPVES-ISMDEMKRVFETNFFGTVRMIKEVMPDM-KKRQAGHIIIMSSV-----MGL 149
Cdd:PRK08217  81 gQLNGLINNAGIlrdGLLvkakdGKVTSkMSLEQFQSVIDVNLTGVFLCGREAAAKMiESGSKGVIINISSIaragnMGQ 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  150 QGvvfndvYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFeTKMM--EEVAKME 207
Cdd:PRK08217 161 TN------YSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEM-TAAMkpEALERLE 213
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 8-189 2.72e-13

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 68.50  E-value: 2.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDLKKKDRLVEAAGEvygqTLTLLPLDICSDESVRQCVNSVKDR-- 85
Cdd:PRK08265   7 KVAIVTGGATLIGAAVARALVA---AGARVAIVDIDADNGAAVAASLGE----RARFIATDITDDAAIERAVATVVARfg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 HIDVLINNAGVGLLGPVESiSMDEMKRVFETNFFGTVRMIKEVMPDMKkRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:PRK08265  80 RVDILVNLACTYLDDGLAS-SRADWLAALDVNLVSAAMLAQAAHPHLA-RGGGAIVNFTSISAKFAQTGRWLYPASKAAI 157

                        170       180
                 ....*....|....*....|....
gi 37590327  166 EGFCESMAVQLLKFNVKLSLIEPG 189
Cdd:PRK08265 158 RQLTRSMAMDLAPDGIRVNSVSPG 181
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 8-220 2.95e-13

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: 68.19  E-value: 2.95e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQkryHVIATmrDLKKkDRLVEAAGEVYGQTLTL-LPLDICSDESVRQCVNSVKDRH 86
Cdd:cd08943   2 KVALVTGGASGIGLAIAKRLAAEGA---AVVVA--DIDP-EIAEKVAEAAQGGPRALgVQCDVTSEAQVQSAFEQAVLEF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 --IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMssvMGLQGVVF----NDVYTA 160
Cdd:cd08943  76 ggLDIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIGGNIVF---NASKNAVApgpnAAAYSA 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37590327 161 SKFAIEGFCESMAVQLLKFNVKLSLIEPGPVhteFET-KMMEEVAKMEYPGADPDTVRYFK 220
Cdd:cd08943 153 AKAAEAHLARCLALEGGEDGIRVNTVNPDAV---FRGsKIWEGVWRAARAKAYGLLEEEYR 210
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-193 3.46e-13

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 68.18  E-value: 3.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCS--SGIGLRIAVLLARD-------EQKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQC 78
Cdd:PRK12748   6 KIALVTGASrlNGIGAAVCRRLAAKgidifftYWSPYDKTMPWGMHDKEPVLLKEEIESYGVRCEHMEIDLSQPYAPNRV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   79 VNSVKDR--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSvmG-LQGVVFN 155
Cdd:PRK12748  86 FYAVSERlgDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLTS--GqSLGPMPD 163

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 37590327  156 DV-YTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHT 193
Cdd:PRK12748 164 ELaYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDT 202
PRK09730 PRK09730
SDR family oxidoreductase;
8-194 3.55e-13

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 67.95  E-value: 3.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHV-IATMRDLKKKDRLVEAAGEVYGQTLTLLPlDIcSDESVRQCVNSVKDRH 86
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLA---QEGYTVaVNYQQNLHAAQEVVNLITQAGGKAFVLQA-DI-SDENQVVAMFTAIDQH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 ---IDVLINNAGVGLL-GPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKR---QAGHIIIMSSVMGLQGVVFNDV-Y 158
Cdd:PRK09730  77 depLAALVNNAGILFTqCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALKhggSGGAIVNVSSAASRLGAPGEYVdY 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 37590327  159 TASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK09730 157 AASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTE 192
PRK06114 PRK06114
SDR family oxidoreductase;
8-214 4.07e-13

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 67.88  E-value: 4.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIatMRDLKKKDRLVEAAG--EVYGQTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:PRK06114   9 QVAFVTGAGSGIGQRIAIGLA---QAGADVA--LFDLRTDDGLAETAEhiEAAGRRAIQIAADVTSKADLRAAVARTEAE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 --HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSvmgLQGVVFNDV-----Y 158
Cdd:PRK06114  84 lgALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIAS---MSGIIVNRGllqahY 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37590327  159 TASKFAIEGFCESMAVQLLKFNVKLSLIEPG----PVHTEFE----TKMMEEVAKMEYPgADPD 214
Cdd:PRK06114 161 NASKAGVIHLSKSLAMEWVGRGIRVNSISPGytatPMNTRPEmvhqTKLFEEQTPMQRM-AKVD 223
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 9-151 5.30e-13

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: 68.93  E-value: 5.30e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   9 VVLITGCSSGIGLRIAVLLARDEQKRyhVIATMR----DLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKD 84
Cdd:cd08953 207 VYLVTGGAGGIGRALARALARRYGAR--LVLLGRsplpPEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRE 284

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37590327  85 RH--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVmpdmKKRQAGHIIIMSSVMGLQG 151
Cdd:cd08953 285 RYgaIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQAL----ADEPLDFFVLFSSVSAFFG 349
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
7-203 5.33e-13

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 67.73  E-value: 5.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLARDEqkrYHVIATM-RDLKKKDRLVEAAGEVyGQTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:PRK12938   3 QRIAYVTGGMGGIGTSICQRLHKDG---FKVVAGCgPNSPRRVKWLEDQKAL-GFDFIASEGNVGDWDSTKAAFDKVKAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 --HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:PRK12938  79 vgEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAKA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 37590327  164 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEV 203
Cdd:PRK12938 159 GIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPDV 198
PRK06128 PRK06128
SDR family oxidoreductase;
11-193 6.39e-13

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 67.96  E-value: 6.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   11 LITGCSSGIGLRIAVLLARD--EQKRYHVIATMRDLKKKDRLVEAAGEVygqtLTLLPLDIcSDESVrqCVNSVKDRH-- 86
Cdd:PRK06128  59 LITGADSGIGRATAIAFAREgaDIALNYLPEEEQDAAEVVQLIQAEGRK----AVALPGDL-KDEAF--CRQLVERAVke 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 ---IDVLINNAGVGL-LGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKrqAGHIIIMSSVMGLQGVVFNDVYTASK 162
Cdd:PRK06128 132 lggLDILVNIAGKQTaVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPP--GASIINTGSIQSYQPSPTLLDYASTK 209

                        170       180       190
                 ....*....|....*....|....*....|.
gi 37590327  163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHT 193
Cdd:PRK06128 210 AAIVAFTKALAKQVAEKGIRVNAVAPGPVWT 240
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 8-120 6.59e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 68.13  E-value: 6.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKKKDRLVEA-AGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH 86
Cdd:PRK06197  17 RVAVVTGANTGLGYETAAALA---AKGAHVVLAVRNLDKGKAAAARiTAATPGADVTLQELDLTSLASVRAAADALRAAY 93

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 37590327   87 --IDVLINNAGVglLGPVESISMDEMKRVFETNFFG 120
Cdd:PRK06197  94 prIDLLINNAGV--MYTPKQTTADGFELQFGTNHLG 127
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 8-194 7.15e-13

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: 67.49  E-value: 7.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRDLKKKDrlvEAAGEVYGQTLT----LLPLDICSDESVRQCVNSVK 83
Cdd:cd09807   2 KTVIITGANTGIGKETARELAR---RGARVIMACRDMAKCE---EAAAEIRRDTLNheviVRHLDLASLKSIRAFAAEFL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  84 --DRHIDVLINNAGVgLLGPvESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVV-FNDV--- 157
Cdd:cd09807  76 aeEDRLDVLINNAGV-MRCP-YSKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAGKInFDDLnse 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 37590327 158 --------YTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:cd09807 154 ksyntgfaYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTE 198
PRK07831 PRK07831
SDR family oxidoreductase;
8-188 8.79e-13

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 66.98  E-value: 8.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCS-SGIGLRIAvLLARDEQKR-----YHViatmRDLKKK-DRLveaAGEVYGQTLTLLPLDICSDESVRQCVN 80
Cdd:PRK07831  18 KVVLVTAAAgTGIGSATA-RRALEEGARvvisdIHE----RRLGETaDEL---AAELGLGRVEAVVCDVTSEAQVDALID 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   81 SVKDRH--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIII-MSSVMGLQGVVFNDV 157
Cdd:PRK07831  90 AAVERLgrLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGGVIVnNASVLGWRAQHGQAH 169

                        170       180       190
                 ....*....|....*....|....*....|.
gi 37590327  158 YTASKFAIEGFCESMAVQLLKFNVKLSLIEP 188
Cdd:PRK07831 170 YAAAKAGVMALTRCSALEAAEYGVRINAVAP 200
PRK06123 PRK06123
SDR family oxidoreductase;
7-221 8.83e-13

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 67.11  E-value: 8.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVkDRH 86
Cdd:PRK06123   2 RKVMIITGASRGIGAATALLAAERG---YAVCLNYLRNRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAV-DRE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 ---IDVLINNAGVglLGP---VESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGH---IIIMSSVMGLQGVVFNDV 157
Cdd:PRK06123  78 lgrLDALVNNAGI--LEAqmrLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTRHGGRggaIVNVSSMAARLGSPGEYI 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37590327  158 -YTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEfetkmmeevakMEYPGADPDTVRYFKD 221
Cdd:PRK06123 156 dYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTE-----------IHASGGEPGRVDRVKA 209
PRK07062 PRK07062
SDR family oxidoreductase;
7-150 1.20e-12

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 66.60  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLL----------ARDEQKRYHVIATMRDLKKKDRLVEAAGEVygqtltllpLDicsDESVR 76
Cdd:PRK07062   8 GRVAVVTGGSSGIGLATVELLleagasvaicGRDEERLASAEARLREKFPGARLLAARCDV---------LD---EADVA 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37590327   77 QCVNSVKDR--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQ 150
Cdd:PRK07062  76 AFAAAVEARfgGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQ 151
PLN00015 PLN00015
protochlorophyllide reductase
 11-148 1.35e-12

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 67.04  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   11 LITGCSSGIGLRIAVLLArdEQKRYHVIATMRDLKKKDRLVEAAG---EVYgqtlTLLPLDICSDESVRQCVNSVK--DR 85
Cdd:PLN00015   1 IITGASSGLGLATAKALA--ETGKWHVVMACRDFLKAERAAKSAGmpkDSY----TVMHLDLASLDSVRQFVDNFRrsGR 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37590327   86 HIDVLINNAGVGLLGPVE-SISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAG--HIIIMSSVMG 148
Cdd:PLN00015  75 PLDVLVCNAAVYLPTAKEpTFTADGFELSVGTNHLGHFLLSRLLLDDLKKSDYPskRLIIVGSITG 140
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 87-201 1.79e-12

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 66.06  E-value: 1.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 IDVLINN-AGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:cd05361  73 IDVLVSNdYIPRPMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPARAAA 152

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 37590327 166 EGFCESMAVQLLKFNVKLSLIEPGPVHTE--FETKMME 201
Cdd:cd05361 153 VALAESLAKELSRDNILVYAIGPNFFNSPtyFPTSDWE 190
PRK08628 PRK08628
SDR family oxidoreductase;
8-193 1.80e-12

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 66.14  E-value: 1.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdEQKRYHVIAT--MRDLKKKDRLVEAAGEVygqtlTLLPLDICSDESVRQCVNSVKDR 85
Cdd:PRK08628   8 KVVIVTGGASGIGAAISLRLA--EEGAIPVIFGrsAPDDEFAEELRALQPRA-----EFVQVDLTDDAQCRDAVEQTVAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 H--IDVLINNAGV----GLlgpvESISMDEMKRVfETNFFGTVRMIKEVMPDMKKRQaGHIIIMSSVMGLQGVVFNDVYT 159
Cdd:PRK08628  81 FgrIDGLVNNAGVndgvGL----EAGREAFVASL-ERNLIHYYVMAHYCLPHLKASR-GAIVNISSKTALTGQGGTSGYA 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 37590327  160 ASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHT 193
Cdd:PRK08628 155 AAKGAQLALTREWAVALAKDGVRVNAVIPAEVMT 188
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 8-189 3.01e-12

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 65.69  E-value: 3.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDRLVEAAGEvYGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:PRK08277  11 KVAVITGGGGVLGGAMAKELARAGAK---VAILDRNQEKAEAVVAEIKA-AGGEALAVKADVLDKESLEQARQQILEDFg 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 -IDVLINNAG------------VGLLGPVESI---SMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQ 150
Cdd:PRK08277  87 pCDILINGAGgnhpkattdnefHELIEPTKTFfdlDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNAFT 166

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 37590327  151 GVVFNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPG 189
Cdd:PRK08277 167 PLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPG 205
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 8-191 3.05e-12

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 65.47  E-value: 3.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDlkkKDRLVEAAGEVY---GQTLTlLPLDICSDESVRQCVNSVKD 84
Cdd:PRK07677   2 KVVIITGGSSGMGKAMAKRFA---EEGANVVITGRT---KEKLEEAKLEIEqfpGQVLT-VQMDVRNPEDVQKMVEQIDE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   85 R--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPD-MKKRQAGHIIIMSSVMGLQ---GVVFNdvy 158
Cdd:PRK07677  75 KfgRIDALINNAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKYwIEKGIKGNIINMVATYAWDagpGVIHS--- 151

                        170       180       190
                 ....*....|....*....|....*....|....
gi 37590327  159 TASKFAIEGFCESMAVQL-LKFNVKLSLIEPGPV 191
Cdd:PRK07677 152 AAAKAGVLAMTRTLAVEWgRKYGIRVNAIAPGPI 185
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
8-194 3.06e-12

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 65.31  E-value: 3.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKRYHViaTMRDLKKKDRLVEAAG-EVYGQTLTLLPLDICsDESVRQCVNSVKdrH 86
Cdd:PRK12481   9 KVAIITGCNTGLGQGMAIGLAKAGADIVGV--GVAEAPETQAQVEALGrKFHFITADLIQQKDI-DSIVSQAVEVMG--H 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 IDVLINNAGV----GLLGPVESISMDEMKRVFETNFFGTVRMIKEVMpdmKKRQAGHIIIMSSVMGLQGVVFNDVYTASK 162
Cdd:PRK12481  84 IDILINNAGIirrqDLLEFGNKDWDDVININQKTVFFLSQAVAKQFV---KQGNGGKIINIASMLSFQGGIRVPSYTASK 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 37590327  163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK12481 161 SAVMGLTRALATELSQYNINVNAIAPGYMATD 192
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 8-209 4.25e-12

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: 64.91  E-value: 4.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDRLVEAAGEvygqTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:cd09761   2 KVAIVTGGGHGIGKQICLDFLEAGDK---VVFADIDEERGADFAEAEGP----NLFFVHGDVADETLVKFVVYAMLEKLg 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 -IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQaGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:cd09761  75 rIDVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK-GRIINIASTRAFQSEPDSEAYAASKGGL 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 37590327 166 EGFCESMAVQLLKfNVKLSLIEPGPVHT----EFETKMMEEVAKMEYP 209
Cdd:cd09761 154 VALTHALAMSLGP-DIRVNCISPGWINTteqqEFTAAPLTQEDHAQHP 200
PRK08278 PRK08278
SDR family oxidoreductase;
8-144 5.25e-12

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 64.92  E-value: 5.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKRyhVIATMRDLKKKD---------RLVEAAGevyGQTLTLLpLDICSDESVRQC 78
Cdd:PRK08278   7 KTLFITGASRGIGLAIALRAARDGANI--VIAAKTAEPHPKlpgtihtaaEEIEAAG---GQALPLV-GDVRDEDQVAAA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37590327   79 VNSVKDRH--IDVLINNAGVGLLGPVESISM---DEMKRVfetNFFGTVRMIKEVMPDMKKRQAGHIIIMS 144
Cdd:PRK08278  81 VAKAVERFggIDICVNNASAINLTGTEDTPMkrfDLMQQI---NVRGTFLVSQACLPHLKKSENPHILTLS 148
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-176 6.70e-12

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 64.34  E-value: 6.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLARdeqKRYHVIATMRdlKKKDRLVEAAGEVYGQTLTLlPLDICSDESVRQCVNSVKDR- 85
Cdd:PRK08642   5 EQTVLVTGGSRGLGAAIARAFAR---EGARVVVNYH--QSEDAAEALADELGDRAIAL-QADVTDREQVQAMFATATEHf 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 --HIDVLINNAGVGLL------GPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDV 157
Cdd:PRK08642  79 gkPITTVVNNALADFSfdgdarKKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGTNLFQNPVVPYHD 158

                        170
                 ....*....|....*....
gi 37590327  158 YTASKFAIEGFCESMAVQL 176
Cdd:PRK08642 159 YTTAKAALLGLTRNLAAEL 177
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 8-214 9.45e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 64.26  E-value: 9.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKryHVIATMRDLKKKDRLVeAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH- 86
Cdd:PRK06198   7 KVALVTGGTQGLGAAIARAFAERGAA--GLVICGRNAEKGEAQA-AELEALGAKAVFVQADLSDVEDCRRVVAAADEAFg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 -IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQA-GHI--IIMSSVMGlqGVVFNDVYTASK 162
Cdd:PRK06198  84 rLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIvnIGSMSAHG--GQPFLAAYCASK 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 37590327  163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMmeevaKMEYPGADPD 214
Cdd:PRK06198 162 GALATLTRNAAYALLRNRIRVNGLNIGWMATEGEDRI-----QREFHGAPDD 208
PRK12746 PRK12746
SDR family oxidoreductase;
8-202 9.46e-12

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 63.90  E-value: 9.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQkrYHVIATMRDLKKKDRLVEAAgEVYGQTLTLLPLDICSDESVRQCVNSVKDR-- 85
Cdd:PRK12746   7 KVALVTGASRGIGRAIAMRLANDGA--LVAIHYGRNKQAADETIREI-ESNGGKAFLIEADLNSIDGVKKLVEQLKNElq 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 ------HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMkkRQAGHIIIMSSVMGLQGVVFNDVYT 159
Cdd:PRK12746  84 irvgtsEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL--RAEGRVINISSAEVRLGFTGSIAYG 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 37590327  160 ASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEE 202
Cdd:PRK12746 162 LSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLLDD 204
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 7-189 1.10e-11

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: 64.02  E-value: 1.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   7 QKVVLITGCSSGIGLRIAVLLArdeQKRYHV-IATMRDLKKKDRLVEAAGEvYGQTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:cd05322   2 NQVAVVIGGGQTLGEFLCHGLA---EAGYDVaVADINSENAEKVADEINAE-YGEKAYGFGADATNEQSVIALSKGVDEI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 --HIDVLINNAGVGLLGPVESISMDEMKRVFETN---FFGTVRMIKEVMpdMKKRQAGHIIIMSSVMGLQGVVFNDVYTA 160
Cdd:cd05322  78 fkRVDLLVYSAGIAKSAKITDFELGDFDRSLQVNlvgYFLCAREFSKLM--IRDGIQGRIIQINSKSGKVGSKHNSGYSA 155

                       170       180
                ....*....|....*....|....*....
gi 37590327 161 SKFAIEGFCESMAVQLLKFNVKLSLIEPG 189
Cdd:cd05322 156 AKFGGVGLTQSLALDLAEHGITVNSLMLG 184
PRK07856 PRK07856
SDR family oxidoreductase;
8-194 1.10e-11

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 63.80  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIA-VLLARDEQkryhVIATMRdlkkkdrlvEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH 86
Cdd:PRK07856   7 RVVLVTGGTRGIGAGIArAFLAAGAT----VVVCGR---------RAPETVDGRPAEFHAADVRDPDQVAALVDAIVERH 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 --IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIM-SSVMGLQGVVFNDVYTASKF 163
Cdd:PRK07856  74 grLDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPGGGSIVNiGSVSGRRPSPGTAAYGAAKA 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 37590327  164 AIEGFCESMAVQLLKfNVKLSLIEPGPVHTE 194
Cdd:PRK07856 154 GLLNLTRSLAVEWAP-KVRVNAVVVGLVRTE 183
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 8-204 1.26e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 63.62  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLAR----------DEQKRYHVIATMRDLkkkdrlveaagevyGQTLTLLPLDICSDESVRQ 77
Cdd:PRK08085  10 KNILITGSAQGIGFLLATGLAEygaeiiindiTAERAELAVAKLRQE--------------GIKAHAAPFNVTHKQEVEA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   78 CVNSVKDR--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHII---IMSSVMGLQGV 152
Cdd:PRK08085  76 AIEHIEKDigPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIInicSMQSELGRDTI 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 37590327  153 VfndVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVA 204
Cdd:PRK08085 156 T---PYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKALVEDEA 204
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
10-267 1.50e-11

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 63.84  E-value: 1.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  10 VLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDLKKKDRLVEAAGevygqtLTLLPLDICSDESVRQCVnsvkdRHIDV 89
Cdd:COG0451   2 ILVTGGAGFIGSHLARRLLARG---HEVVGLDRSPPGAANLAALPG------VEFVRGDLRDPEALAAAL-----AGVDA 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  90 LINNAGVGllgpveSISMDEMKRVFETNFFGTVRMIKEvmpdMKKRQAGHIIIMSS--VMGLQGVVFN--------DVYT 159
Cdd:COG0451  68 VVHLAAPA------GVGEEDPDETLEVNVEGTLNLLEA----ARAAGVKRFVYASSssVYGDGEGPIDedtplrpvSPYG 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327 160 ASKFAIEGFCESMAvqlLKFNVKLSLIEP----GPVHTEFETKMMEEVAK---MEYPGaDPDTVRYFkdVYVpssidife 232
Cdd:COG0451 138 ASKLAAELLARAYA---RRYGLPVTILRPgnvyGPGDRGVLPRLIRRALAgepVPVFG-DGDQRRDF--IHV-------- 203

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 37590327 233 amgqtpDDIAKCTKKVIETSQPRFR--NLTNSLYTPI 267
Cdd:COG0451 204 ------DDVARAIVLALEAPAAPGGvyNVGGGEPVTL 234
PRK05867 PRK05867
SDR family oxidoreductase;
8-195 2.18e-11

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 63.13  E-value: 2.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLkkkDRLVEAAGEVYGQTLTLLPL--DICSDESVRQCVNSVKDR 85
Cdd:PRK05867  10 KRALITGASTGIGKRVALAYV---EAGAQVAIAARHL---DALEKLADEIGTSGGKVVPVccDVSQHQQVTSMLDQVTAE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 --HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMglQGVVFN-----DVY 158
Cdd:PRK05867  84 lgGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQGGVIINTASM--SGHIINvpqqvSHY 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 37590327  159 TASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEF 195
Cdd:PRK05867 162 CASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTEL 198
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-209 2.19e-11

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 62.88  E-value: 2.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCS--SGIGLRIAVLLARDEQKRYHVIATMRDLK-----KKDRLVEAAGEV--YGQTLTLLPLDICSDESVRQC 78
Cdd:PRK12859   7 KVAVVTGVSrlDGIGAAICKELAEAGADIFFTYWTAYDKEmpwgvDQDEQIQLQEELlkNGVKVSSMELDLTQNDAPKEL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   79 VNSVKDR--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFND 156
Cdd:PRK12859  87 LNKVTEQlgYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTSGQFQGPMVGEL 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 37590327  157 VYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYP 209
Cdd:PRK12859 167 AYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGWMTEEIKQGLLPMFP 219
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 8-201 2.43e-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: 62.85  E-value: 2.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLArdeqKRYHVIA-TMRDLKKK-DRLVEAAGEVYGQTLTLLpLDICSDESVRQCVNSVKDR 85
Cdd:cd09763   4 KIALVTGASRGIGRGIALQLG----EAGATVYiTGRTILPQlPGTAEEIEARGGKCIPVR-CDHSDDDEVEALFERVARE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 ---HIDVLINNA--GVGLLGPV-------ESISM-DEMKRV-----FETNFFGTvrmikevmPDMKKRQAGHIIIMSSVM 147
Cdd:cd09763  79 qqgRLDILVNNAyaAVQLILVGvakpfweEPPTIwDDINNVglrahYACSVYAA--------PLMVKAGKGLIVIISSTG 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 37590327 148 GLQGVvFNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMME 201
Cdd:cd09763 151 GLEYL-FNVAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPE 203
PRK07985 PRK07985
SDR family oxidoreductase;
11-196 3.35e-11

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 63.09  E-value: 3.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   11 LITGCSSGIGLRIAVLLARD--EQKRYHVIATMRDLKKKDRLVEAAgevyGQTLTLLPLDICSDESVRQCVNSVKDR--H 86
Cdd:PRK07985  53 LVTGGDSGIGRAAAIAYAREgaDVAISYLPVEEEDAQDVKKIIEEC----GRKAVLLPGDLSDEKFARSLVHEAHKAlgG 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   87 IDVLINNAGVGLLGP-VESISMDEMKRVFETNFFGTVRMIKEVMPDMKKrqAGHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:PRK07985 129 LDIMALVAGKQVAIPdIADLTSEQFQKTFAINVFALFWLTQEAIPLLPK--GASIITTSSIQAYQPSPHLLDYAATKAAI 206

                        170       180       190
                 ....*....|....*....|....*....|.
gi 37590327  166 EGFCESMAVQLLKFNVKLSLIEPGPVHTEFE 196
Cdd:PRK07985 207 LNYSRGLAKQVAEKGIRVNIVAPGPIWTALQ 237
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 8-211 7.85e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 61.46  E-value: 7.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLaRDEQKRyhVIATMRdlKKKDRLVEAAGEVYGqtltllplDICSDESVRQCVNSVKDR-- 85
Cdd:PRK06523  10 KRALVTGGTKGIGAATVARL-LEAGAR--VVTTAR--SRPDDLPEGVEFVAA--------DLTTAEGCAAVARAVLERlg 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 HIDVLINNAG--VGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSS---VMGLQGVVFNdvYTA 160
Cdd:PRK06523  77 GVDILVHVLGgsSAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSiqrRLPLPESTTA--YAA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 37590327  161 SKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAK---MEYPGA 211
Cdd:PRK06523 155 AKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEAAVALAERLAEaagTDYEGA 208
PRK06101 PRK06101
SDR family oxidoreductase;
9-198 8.41e-11

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 61.04  E-value: 8.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    9 VVLITGCSSGIGLRIAVLLARDEQKryhVIATMRdlkkkDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRHiD 88
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQGWQ---VIACGR-----NQSVLDELHTQSANIFTLAFDVTDHPGTKAALSQLPFIP-E 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   89 VLINNAGvgllgpvESISMDE-------MKRVFETNFFGTVRMIKEVMPDMkkrQAGH-IIIMSSVMGLQGVVFNDVYTA 160
Cdd:PRK06101  74 LWIFNAG-------DCEYMDDgkvdatlMARVFNVNVLGVANCIEGIQPHL---SCGHrVVIVGSIASELALPRAEAYGA 143

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 37590327  161 SKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETK 198
Cdd:PRK06101 144 SKAAVAYFARTLQLDLRPKGIEVVTVFPGFVATPLTDK 181
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
8-193 8.76e-11

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 61.04  E-value: 8.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKRYHV-IATMRDLKKKdrlVEAAGEVYgqtltllpLDICSDESVRQCVNSVKDR- 85
Cdd:PRK08993  11 KVAVVTGCDTGLGQGMALGLAEAGCDIVGInIVEPTETIEQ---VTALGRRF--------LSLTADLRKIDGIPALLERa 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 -----HIDVLINNAGvgLLGPVESISMDE------MKRVFETNFFGTVRMIKEVMpdmKKRQAGHIIIMSSVMGLQGVVF 154
Cdd:PRK08993  80 vaefgHIDILVNNAG--LIRREDAIEFSEkdwddvMNLNIKSVFFMSQAAAKHFI---AQGNGGKIINIASMLSFQGGIR 154

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 37590327  155 NDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHT 193
Cdd:PRK08993 155 VPSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMAT 193
PRK06194 PRK06194
hypothetical protein; Provisional
 8-176 1.57e-10

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 60.80  E-value: 1.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKRyhVIATMrdlkKKDRLVEAAGEVYGQTLTLLPL--DICSDESVRQCVNSVKDR 85
Cdd:PRK06194   7 KVAVITGAASGFGLAFARIGAALGMKL--VLADV----QQDALDRAVAELRAQGAEVLGVrtDVSDAAQVEALADAALER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 H--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFG--------TVRMIKEVMPDMKKRqaGHIIIMSSVMGLQGVVFN 155
Cdd:PRK06194  81 FgaVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGvihgvrafTPLMLAAAEKDPAYE--GHIVNTASMAGLLAPPAM 158

                        170       180
                 ....*....|....*....|.
gi 37590327  156 DVYTASKFAIEGFCESMAVQL 176
Cdd:PRK06194 159 GIYNVSKHAVVSLTETLYQDL 179
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 9-243 3.74e-10

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: 59.40  E-value: 3.74e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   9 VVLITGCSSGIGLRIAVLLARDEQkryhVIATMrDLKKKDRLVEAAGEV--YGQTLTLLPLDICSDESVRQCVNSVKDR- 85
Cdd:cd05337   3 VAIVTGASRGIGRAIATELAARGF----DIAIN-DLPDDDQATEVVAEVlaAGRRAIYFQADIGELSDHEALLDQAWEDf 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 -HIDVLINNAGVGL--LGPVESISMDEMKRVFETNFFGTV--------RMIKEvmPDMKKRQAGHIIIMSSVMGLQGVVF 154
Cdd:cd05337  78 gRLDCLVNNAGIAVrpRGDLLDLTEDSFDRLIAINLRGPFfltqavarRMVEQ--PDRFDGPHRSIIFVTSINAYLVSPN 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327 155 NDVYTASKFAIegfceSMAVQLLKF-----NVKLSLIEPGPVHTEfetkmMEEVAKMEYPGAdpdtvryFKDVYVPSSid 229
Cdd:cd05337 156 RGEYCISKAGL-----SMATRLLAYrladeGIAVHEIRPGLIHTD-----MTAPVKEKYDEL-------IAAGLVPIR-- 216

                       250
                ....*....|....
gi 37590327 230 ifeAMGQtPDDIAK 243
Cdd:cd05337 217 ---RWGQ-PEDIAK 226
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 3-264 4.24e-10

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 59.58  E-value: 4.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    3 SGGGQKVVLITGCSSGIGLRIAVLLARDEQKryhviATMRDLKKKDrLVEAAGEVYGQTLTLLPLdICsDESVRQCVNSV 82
Cdd:PRK05876   2 DGFPGRGAVITGGASGIGLATGTEFARRGAR-----VVLGDVDKPG-LRQAVNHLRAEGFDVHGV-MC-DVRHREEVTHL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   83 KDR------HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPD-MKKRQAGHIIIMSSVMGLQGVVFN 155
Cdd:PRK05876  74 ADEafrllgHVDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRlLEQGTGGHVVFTASFAGLVPNAGL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  156 DVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVhtefETKMMEEVAKMEypGADpdtvryfkdvYVPSSIDifEAMG 235
Cdd:PRK05876 154 GAYGVAKYGVVGLAETLAREVTADGIGVSVLCPMVV----ETNLVANSERIR--GAA----------CAQSSTT--GSPG 215

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 37590327  236 QTP--------DDIAKCTKKVIetsqprfrnLTNSLY 264
Cdd:PRK05876 216 PLPlqddnlgvDDIAQLTADAI---------LANRLY 243
PRK06953 PRK06953
SDR family oxidoreductase;
8-194 8.99e-10

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 57.77  E-value: 8.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDLKKKDRLVEAAGEVygqtltlLPLDICSDESVRQCVNSVKDRHI 87
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADG---WRVIATARDAAALAALQALGAEA-------LALDVADPASVAGLAWKLDGEAL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   88 DVLINNAGVglLGP----VESISMDEMKRVFETNFFGTVRMIKEVMPdMKKRQAGHIIIMSSVMGLQGVVFND---VYTA 160
Cdd:PRK06953  72 DAAVYVAGV--YGPrtegVEPITREDFDAVMHTNVLGPMQLLPILLP-LVEAAGGVLAVLSSRMGSIGDATGTtgwLYRA 148

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 37590327  161 SKFAIegfceSMAVQLLKFNVK----LSLiEPGPVHTE 194
Cdd:PRK06953 149 SKAAL-----NDALRAASLQARhatcIAL-HPGWVRTD 180
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 7-176 1.37e-09

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 57.66  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGL-----------RIAVlLARDEQKryhvIATMRDlKKKDRLVEAAGEVYGQTltllpldiCSDESV 75
Cdd:PRK06200   6 GQVALITGGGSGIGRalverflaegaRVAV-LERSAEK----LASLRQ-RFGDHVLVVEGDVTSYA--------DNQRAV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   76 RQCVnsvkDR--HIDVLINNAGV-----GLLG-PVESIS--MDEMkrvFETNFFGTVRMIKEVMPDMKKRqAGHIIIMSS 145
Cdd:PRK06200  72 DQTV----DAfgKLDCFVGNAGIwdyntSLVDiPAETLDtaFDEI---FNVNVKGYLLGAKAALPALKAS-GGSMIFTLS 143

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 37590327  146 VMGLQ----GVvfndVYTASKFAIEGFCESMAVQL 176
Cdd:PRK06200 144 NSSFYpgggGP----LYTASKHAVVGLVRQLAYEL 174
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 8-218 1.58e-09

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: 57.29  E-value: 1.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDES----VRQCVNSVK 83
Cdd:cd05357   1 AVALVTGAAKRIGRAIAEALA---AEGYRVVVHYNRSEAEAQRLKDELNALRNSAVLVQADLSDFAAcadlVAAAFRAFG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  84 drHIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKF 163
Cdd:cd05357  78 --RCDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKA 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37590327 164 AIEGFCESMAVQLLKfNVKLSLIEPG----PVHTEFETKM--MEEVAKMEYPGADP--DTVRY 218
Cdd:cd05357 156 ALEGLTRSAALELAP-NIRVNGIAPGlillPEDMDAEYREnaLRKVPLKRRPSAEEiaDAVIF 217
PRK07041 PRK07041
SDR family oxidoreductase;
11-211 2.43e-09

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 56.58  E-value: 2.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   11 LITGCSSGIGLRIA-VLLARDEqkryHVIATMRDlkkKDRLVEAAGEV-YGQTLTLLPLDICSDESVRQ-CVNSVKDRHI 87
Cdd:PRK07041   1 LVVGGSSGIGLALArAFAAEGA----RVTIASRS---RDRLAAAARALgGGAPVRTAALDITDEAAVDAfFAEAGPFDHV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   88 DVlinNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEvmPDMkkRQAGHIIIMSSVMGLQGVVFNDVYTASKFAIEG 167
Cdd:PRK07041  74 VI---TAADTPGGPVRALPLAAAQAAMDSKFWGAYRVARA--ARI--APGGSLTFVSGFAAVRPSASGVLQGAINAALEA 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 37590327  168 FCESMAVQLLKfnVKLSLIEPGPVHTEFETKMMEEVAKMEYPGA 211
Cdd:PRK07041 147 LARGLALELAP--VRVNTVSPGLVDTPLWSKLAGDAREAMFAAA 188
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
2-212 3.31e-09

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


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 56.64  E-value: 3.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    2 ASGGGQKVVLITGcSSGIGLRIAVLLARDEQKRYhVIATMRDLKKKDRLV---EAAGEVYGQTLTLLPLDICSDESVRQC 78
Cdd:PRK07904   4 AVGNPQTILLLGG-TSEIGLAICERYLKNAPARV-VLAALPDDPRRDAAVaqmKAAGASSVEVIDFDALDTDSHPKVIDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   79 VNSVKDrhIDVLInnAGVGLLGPVESISMDEMKRV--FETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFND 156
Cdd:PRK07904  82 AFAGGD--VDVAI--VAFGLLGDAEELWQNQRKAVqiAEINYTAAVSVGVLLGEKMRAQGFGQIIAMSSVAGERVRRSNF 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37590327  157 VYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFE--------TKMMEEVAKMEYPGAD 212
Cdd:PRK07904 158 VYGSTKAGLDGFYLGLGEALREYGVRVLVVRPGQVRTRMSahakeaplTVDKEDVAKLAVTAVA 221
PRK12742 PRK12742
SDR family oxidoreductase;
8-194 5.57e-09

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 55.53  E-value: 5.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKRYHVIATMRDlkKKDRLVEAAGEVYGQTltllpldicsDESVR-QCVNSVKDR- 85
Cdd:PRK12742   7 KKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAGSKD--AAERLAQETGATAVQT----------DSADRdAVIDVVRKSg 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 HIDVLINNAGVGLLGPVESISMDEMKRVFETN----FFGTVRMIKEvMPDmkkrqAGHIIIMSSV----MGLQGVVfndV 157
Cdd:PRK12742  75 ALDILVVNAGIAVFGDALELDADDIDRLFKINihapYHASVEAARQ-MPE-----GGRIIIIGSVngdrMPVAGMA---A 145

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 37590327  158 YTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK12742 146 YAASKSALQGMARGLARDFGPRGITINVVQPGPIDTD 182
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 8-163 8.29e-09

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 55.14  E-value: 8.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDeQKRYHVIATMRDLKKK--------DRLVEAAGevyGQTLTLLpLDICSDESVRQCV 79
Cdd:cd09762   4 KTLFITGASRGIGKAIALKAARD-GANVVIAAKTAEPHPKlpgtiytaAEEIEAAG---GKALPCI-VDIRDEDQVRAAV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  80 NSVKDRH--IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFND- 156
Cdd:cd09762  79 EKAVEKFggIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNLNPKWFKNh 158


                ....*...
gi 37590327 157 -VYTASKF 163
Cdd:cd09762 159 tAYTMAKY 166
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 1-194 1.09e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 55.19  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    1 MASGGGQKVVLITGCSSGIGLRIAVLLARDEQkryHVIATMRDlkkKDRLVEAAGEVYGQT----LTLLPLDICSDESVR 76
Cdd:PRK05875   1 MQLSFQDRTYLVTGGGSGIGKGVAAGLVAAGA---AVMIVGRN---PDKLAAAAEEIEALKgagaVRYEPADVTDEDQVA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   77 QCVNSVKDRH--IDVLINNAGVGL-LGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVV 153
Cdd:PRK05875  75 RAVDAATAWHgrLHGVVHCAGGSEtIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHR 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 37590327  154 FNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK05875 155 WFGAYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTD 195
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 11-178 1.45e-08

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 55.26  E-value: 1.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   11 LITGCSSGIGLRIAVLLARdeqKRYHVIATMRDLKKKDRLVEAAGEVYGQT-LTLLPLDICSD--ESVRQCVNSVKDRHI 87
Cdd:PLN02780  57 LVTGPTDGIGKGFAFQLAR---KGLNLVLVARNPDKLKDVSDSIQSKYSKTqIKTVVVDFSGDidEGVKRIKETIEGLDV 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   88 DVLINNAGVGLLGPVESISMDE--MKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSvmGLQGVVFND----VYTAS 161
Cdd:PLN02780 134 GVLINNVGVSYPYARFFHEVDEelLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGS--GAAIVIPSDplyaVYAAT 211

                        170
                 ....*....|....*..
gi 37590327  162 KFAIEGFCESMAVQLLK 178
Cdd:PLN02780 212 KAYIDQFSRCLYVEYKK 228
PRK05717 PRK05717
SDR family oxidoreductase;
2-189 1.68e-08

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 54.51  E-value: 1.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    2 ASGGGQKVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDLKKKDRLVEAAGEvygqTLTLLPLDICSDESVRQCVNS 81
Cdd:PRK05717   5 NPGHNGRVALVTGAARGIGLGIAAWLIAEG---WQVVLADLDRERGSKVAKALGE----NAWFIAMDVADEAQVAAGVAE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   82 VKDR--HIDVLINNAGVG--LLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKrQAGHIIIMSSVMGLQGVVFNDV 157
Cdd:PRK05717  78 VLGQfgRLDALVCNAAIAdpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRA-HNGAIVNLASTRARQSEPDTEA 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 37590327  158 YTASKFAIEGFCESMAVQLLKfNVKLSLIEPG 189
Cdd:PRK05717 157 YAASKGGLLALTHALAISLGP-EIRVNAVSPG 187
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 8-114 1.82e-08

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: 53.25  E-value: 1.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327      8 KVVLITGCSSGIGLRIAVLLARDEQKryHVIATMR---DLKKKDRLVEAAGEvYGQTLTLLPLDICSDESVRQCVNSVKD 84
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGAR--RLVLLSRsgpDAPGAAALLAELEA-AGARVTVVACDVADRDALAAVLAAIPA 77

                           90       100       110
                   ....*....|....*....|....*....|..
gi 37590327     85 RH--IDVLINNAGVGLLGPVESISMDEMKRVF 114
Cdd:smart00822  78 VEgpLTGVIHAAGVLDDGVLASLTPERFAAVL 109
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-177 3.39e-08

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 53.43  E-value: 3.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDeqkRYHVIATmrDLKKKDRLVEAAGEV--YGQTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAA---GFDLAIN--DRPDDEELAATQQELraLGVEVIFFPADVADLSAHEAMLDAAQAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 --HIDVLINNAGVGLL--GPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGH------IIIMSSVMGLQGVVFN 155
Cdd:PRK12745  78 wgRIDCLVNNAGVGVKvrGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPEelphrsIVFVSSVNAIMVSPNR 157

                        170       180
                 ....*....|....*....|..
gi 37590327  156 DVYTASKFAIegfceSMAVQLL 177
Cdd:PRK12745 158 GEYCISKAGL-----SMAAQLF 174
PRK05854 PRK05854
SDR family oxidoreductase;
8-164 3.62e-08

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 53.92  E-value: 3.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDRLVEAAGE-VYGQTLTLLPLDICSDESVRQCVNSV--KD 84
Cdd:PRK05854  15 KRAVVTGASDGLGLGLARRLAAAGAE---VILPVRNRAKGEAAVAAIRTaVPDAKLSLRALDLSSLASVAALGEQLraEG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   85 RHIDVLINNAGVgLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAgHIIIMSSVMGLQGVV-FNDV------ 157
Cdd:PRK05854  92 RPIHLLINNAGV-MTPPERQTTADGFELQFGTNHLGHFALTAHLLPLLRAGRA-RVTSQSSIAARRGAInWDDLnwersy 169

                        170
                 ....*....|..
gi 37590327  158 -----YTASKFA 164
Cdd:PRK05854 170 agmraYSQSKIA 181
PRK05599 PRK05599
SDR family oxidoreductase;
10-216 4.28e-08

SDR family oxidoreductase;


Pssm-ID: 235527 [Multi-domain]  Cd Length: 246  Bit Score: 53.35  E-value: 4.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   10 VLITGCSSGIGLRIAVLLARDEQkryhVIATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRHIDV 89
Cdd:PRK05599   3 ILILGGTSDIAGEIATLLCHGED----VVLAARRPEAAQGLASDLRQRGATSVHVLSFDAQDLDTHRELVKQTQELAGEI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   90 LINNAGVGLLGPVESISMDEMKRV--FETNFFGTVRMIKeVMPDMKKRQA--GHIIIMSSVMGLQGVVFNDVYTASKFAI 165
Cdd:PRK05599  79 SLAVVAFGILGDQERAETDEAHAVeiATVDYTAQVSMLT-VLADELRAQTapAAIVAFSSIAGWRARRANYVYGSTKAGL 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 37590327  166 EGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMmeEVAKME-YPGADPDTV 216
Cdd:PRK05599 158 DAFCQGLADSLHGSHVRLIIARPGFVIGSMTTGM--KPAPMSvYPRDVAAAV 207
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 7-176 5.83e-08

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: 52.74  E-value: 5.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   7 QKVVLITGCSSGIGLriaVLLARDEQKRYHVIATMRDLKKKDRLVEAAGE----VYGqtltllplDICSDESVRQCVNSV 82
Cdd:cd05348   4 GEVALITGGGSGLGR---ALVERFVAEGAKVAVLDRSAEKVAELRADFGDavvgVEG--------DVRSLADNERAVARC 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  83 KDR--HIDVLINNAGV-----GLLG-PVESIS--MDEMkrvFETNFFGTVRMIKEVMPDMKKRQaGHIIIMSSVMGLQGV 152
Cdd:cd05348  73 VERfgKLDCFIGNAGIwdystSLVDiPEEKLDeaFDEL---FHINVKGYILGAKAALPALYATE-GSVIFTVSNAGFYPG 148

                       170       180
                ....*....|....*....|....
gi 37590327 153 VFNDVYTASKFAIEGFCESMAVQL 176
Cdd:cd05348 149 GGGPLYTASKHAVVGLVKQLAYEL 172
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 10-205 5.91e-08

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: 52.20  E-value: 5.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  10 VLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDlkkkdrlveaAGEVygqtltllPLDICSDESVRQCVNSVKdrHIDV 89
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLS---AHGHEVITAGRS----------SGDY--------QVDITDEASIKALFEKVG--HFDA 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  90 LINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRqaGHIIIMSSVMGLQGVVFNDVYTASKFAIEGFC 169
Cdd:cd11731  58 IVSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYLNDG--GSITLTSGILAQRPIPGGAAAATVNGALEGFV 135

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 37590327 170 ESMAVQLLK---FN------VKLSLIEPGPVHTEFETKMMEEVAK 205
Cdd:cd11731 136 RAAAIELPRgirINavspgvVEESLEAYGDFFPGFEPVPAEDVAK 180
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 10-195 6.11e-08

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: 52.14  E-value: 6.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  10 VLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDLKKkdrLVEAAGEVYGQtltLLPLDICSDESVRQCVNSVKDrhIDV 89
Cdd:cd11730   1 ALILGATGGIGRALARALAGRG---WRLLLSGRDAGA---LAGLAAEVGAL---ARPADVAAELEVWALAQELGP--LDL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  90 LINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPdmKKRQAGHIIIMSS------VMGLQGvvfndvYTASKF 163
Cdd:cd11730  70 LVYAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHALA--LLAAGARLVFLGAypelvmLPGLSA------YAAAKA 141

                       170       180       190
                ....*....|....*....|....*....|..
gi 37590327 164 AIEGFCESMAVQLLKfnVKLSLIEPGPVHTEF 195
Cdd:cd11730 142 ALEAYVEVARKEVRG--LRLTLVRPPAVDTGL 171
PRK08703 PRK08703
SDR family oxidoreductase;
8-212 1.05e-07

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 51.86  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDRLVEAAGEVYGQTLTLLPLDI--CSDESVRQCVNSVKDR 85
Cdd:PRK08703   7 KTILVTGASQGLGEQVAKAYAAAGAT---VILVARHQKKLEKVYDAIVEAGHPEPFAIRFDLmsAEEKEFEQFAATIAEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 ---HIDVLINNAG-VGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTAS 161
Cdd:PRK08703  84 tqgKLDGIVHCAGyFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAYWGGFGAS 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 37590327  162 KFAIEGFCESMAVQLLKF-NVKLSLIEPGPVHTEFETKMMEEVAKMEYPGAD 212
Cdd:PRK08703 164 KAALNYLCKVAADEWERFgNLRANVLVPGPINSPQRIKSHPGEAKSERKSYG 215
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 8-145 1.62e-07

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 51.83  E-value: 1.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQkryHVIATMRDLKKKDRLVE-AAGEVYGQTLTLLPLDICSDESVRQCVNSVKDR- 85
Cdd:cd09809   2 KVIIITGANSGIGFETARSFALHGA---HVILACRNMSRASAAVSrILEEWHKARVEAMTLDLASLRSVQRFAEAFKAKn 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37590327  86 -HIDVLINNAGVglLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSS 145
Cdd:cd09809  79 sPLHVLVCNAAV--FALPWTLTEDGLETTFQVNHLGHFYLVQLLEDVLRRSAPARVIVVSS 137
PRK06196 PRK06196
oxidoreductase; Provisional
 8-157 2.29e-07

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 51.61  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLkkkDRLVEAAGEVYGqtLTLLPLDICSDESVRQCVNSVKD--R 85
Cdd:PRK06196  27 KTAIVTGGYSGLGLETTRALA---QAGAHVIVPARRP---DVAREALAGIDG--VEVVMLDLADLESVRAFAERFLDsgR 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37590327   86 HIDVLINNAGVglLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSV-MGLQGVVFNDV 157
Cdd:PRK06196  99 RIDILINNAGV--MACPETRVGDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSSAgHRRSPIRWDDP 169
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 8-189 3.07e-07

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 50.71  E-value: 3.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATmrdlkkkDR--LV-EAAGEVY---GQTLTLLPlDICSDESVRQCVNS 81
Cdd:PRK12823   9 KVVVVTGAAQGIGRGVALRAAAEGAR---VVLV-------DRseLVhEVAAELRaagGEALALTA-DLETYAGAQAAMAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   82 VKDRH--IDVLINNAGvgllG-----PVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVmGLQGVvf 154
Cdd:PRK12823  78 AVEAFgrIDVLINNVG----GtiwakPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSI-ATRGI-- 150

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 37590327  155 NDV-YTASKFAIEGFCESMAVQLLKFNVKLSLIEPG 189
Cdd:PRK12823 151 NRVpYSAAKGGVNALTASLAFEYAEHGIRVNAVAPG 186
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-216 3.61e-07

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 50.14  E-value: 3.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDRLVEAAGEvYGQtLTLLPLDICSDESVRQCVNSVKD-- 84
Cdd:PRK05786   5 GKKVAIIGVSEGLGYAVAYFALKEGAQ---VCINSRNENKLKRMKKTLSK-YGN-IHYVVGDVSSTESARNVIEKAAKvl 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   85 RHIDVLINNAGVGLLGPVESIS-MDEMkrvFETNFFGTVRMIKEVMPDMKKrqAGHIIIMSSVMGLQGVVFNDV-YTASK 162
Cdd:PRK05786  80 NAIDGLVVTVGGYVEDTVEEFSgLEEM---LTNHIKIPLYAVNASLRFLKE--GSSIVLVSSMSGIYKASPDQLsYAVAK 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 37590327  163 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFET-KMMEEVAKMEYPGADPDTV 216
Cdd:PRK05786 155 AGLAKAVEILASELLGRGIRVNGIAPTTISGDFEPeRNWKKLRKLGDDMAPPEDF 209
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 7-142 8.36e-07

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 49.57  E-value: 8.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    7 QKVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDR----LVEAAGEVYGqtltlLPLDICSDESVRQCVNSV 82
Cdd:PRK07576   9 GKNVVVVGGTSGINLGIAQAFARAGAN---VAVASRSQEKVDAavaqLQQAGPEGLG-----VSADVRDYAAVEAAFAQI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37590327   83 KDR--HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIII 142
Cdd:PRK07576  81 ADEfgPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPGASIIQI 142
PRK07814 PRK07814
SDR family oxidoreductase;
8-194 1.33e-06

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 49.01  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdEQKRYHVIA--TMRDLKKKDRLVEAAGevygQTLTLLPLDICSDESVRQCVNSVKDR 85
Cdd:PRK07814  11 QVAVVTGAGRGLGAAIALAFA--EAGADVLIAarTESQLDEVAEQIRAAG----RRAHVVAADLAHPEATAGLAGQAVEA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   86 --HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDM-KKRQAGHIIIMSSVMG-LQGVVFNdVYTAS 161
Cdd:PRK07814  85 fgRLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMlEHSGGGSVINISSTMGrLAGRGFA-AYGTA 163

                        170       180       190
                 ....*....|....*....|....*....|...
gi 37590327  162 KFAIeGFCESMAVQLLKFNVKLSLIEPGPVHTE 194
Cdd:PRK07814 164 KAAL-AHYTRLAALDLCPRIRVNAIAPGSILTS 195
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
8-254 1.51e-06

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 48.53  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRdlKKKDRLVEAAgEVYGQTLTLLPLDICSDESVRQCVNSV----- 82
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLL---EKGTHVISISR--TENKELTKLA-EQYNSNLTFHSLDLQDVHELETNFNEIlssiq 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   83 KDRHIDV-LINNAG-VGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIII-MSSVMGLQGVVFNDVYT 159
Cdd:PRK06924  76 EDNVSSIhLINNAGmVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKVDKRVInISSGAAKNPYFGWSAYC 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  160 ASKFAIEGFCESMAVQ--LLKFNVKLSLIEPGPVHTEFEtKMMEEVAKMEYPgaDPDTVRYFKDvyvpssidifEAMGQT 237
Cdd:PRK06924 156 SSKAGLDMFTQTVATEqeEEEYPVKIVAFSPGVMDTNMQ-AQIRSSSKEDFT--NLDRFITLKE----------EGKLLS 222

                        250
                 ....*....|....*..
gi 37590327  238 PDDIAKCTKKVIETSQP 254
Cdd:PRK06924 223 PEYVAKALRNLLETEDF 239
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 2-224 2.99e-06

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 47.87  E-value: 2.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   2 ASGGGQKVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRDLKK----KDRLVEAAGEVYGqtltllplDICSDESVRQ 77
Cdd:cd08951   2 RSPPPMKRIFITGSSDGLGLAAARTLL---HQGHEVVLHARSQKRaadaKAACPGAAGVLIG--------DLSSLAETRK 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  78 CVNSVKDR-HIDVLINNAGVgLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPdmKKRqaghIIIMSSVMGLQGVVFND 156
Cdd:cd08951  71 LADQVNAIgRFDAVIHNAGI-LSGPNRKTPDTGIPAMVAVNVLAPYVLTALIRR--PKR----LIYLSSGMHRGGNASLD 143

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37590327 157 VYTASK---FAIEGFCES--------MAVQLLKFNVKLSLIEPGPVHTefetkmmeevaKMEYPGAdPDTVRYFKDVYV 224
Cdd:cd08951 144 DIDWFNrgeNDSPAYSDSklhvltlaAAVARRWKDVSSNAVHPGWVPT-----------KMGGAGA-PDDLEQGHLTQV 210
PRK09186 PRK09186
flagellin modification protein A; Provisional
 8-189 3.32e-06

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 47.68  E-value: 3.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKryhVIATMRDLKKKDRLVEAAGEVYGQT-LTLLPLDICSDESVRQCVNSV--KD 84
Cdd:PRK09186   5 KTILITGAGGLIGSALVKAILEAGGI---VIAADIDKEALNELLESLGKEFKSKkLSLVELDITDQESLEEFLSKSaeKY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   85 RHIDVLINNA-----GVGLLgpVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDV-- 157
Cdd:PRK09186  82 GKIDGAVNCAyprnkDYGKK--FFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVVAPKFEIYeg 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 37590327  158 --------YTASKFAIEGFCESMAVQLLKFNVKLSLIEPG 189
Cdd:PRK09186 160 tsmtspveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPG 199
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 8-208 3.56e-06

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 47.38  E-value: 3.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDeqkryHVIATMRDLKKKDRLVEAAGEVY---GQTLTlLPLDICSDESVRQCVNSVKD 84
Cdd:PRK12747   5 KVALVTGASRGIGRAIAKRLAND-----GALVAIHYGNRKEEAEETVYEIQsngGSAFS-IGANLESLHGVEALYSSLDN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   85 R--------HIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMkkRQAGHIIIMSSVMGLQGVVFND 156
Cdd:PRK12747  79 ElqnrtgstKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRISLPDFI 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 37590327  157 VYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEY 208
Cdd:PRK12747 157 AYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLSDPMMKQY 208
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 8-145 4.82e-06

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: 47.20  E-value: 4.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARdEQKRYHVIAtmrdlKKKDRLVEAAGEVY----GQTLTLLPLDICSDESVRQCVNSVK 83
Cdd:cd09808   2 RSFLITGANSGIGKAAALAIAK-RGGTVHMVC-----RNQTRAEEARKEIEtesgNQNIFLHIVDMSDPKQVWEFVEEFK 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37590327  84 DRH--IDVLINNAGVgLLGPVEsISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSS 145
Cdd:cd09808  76 EEGkkLHVLINNAGC-MVNKRE-LTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSS 137
PRK12744 PRK12744
SDR family oxidoreductase;
8-242 6.04e-06

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 46.66  E-value: 6.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKR----YHVIATMRDLKKKDRLVEAAGevyGQTLtLLPLDICSDESVRQCVNSVK 83
Cdd:PRK12744   9 KVVLIAGGAKNLGGLIARDLAAQGAKAvaihYNSAASKADAEETVAAVKAAG---AKAV-AFQADLTTAAAVEKLFDDAK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   84 DR--HIDVLINNAGVGLLGPVESISMDEMKRVFETN-----FFgtvrmIKEVMPDMKKRqaGHII-IMSSVMGlqgvVFN 155
Cdd:PRK12744  85 AAfgRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNsksafFF-----IKEAGRHLNDN--GKIVtLVTSLLG----AFT 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  156 DVYTA---SKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFetkmmeevakmEYPGADPDTVRYFKDVyvpSSIDIFE 232
Cdd:PRK12744 154 PFYSAyagSKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPF-----------FYPQEGAEAVAYHKTA---AALSPFS 219

                        250
                 ....*....|.
gi 37590327  233 AMGQT-PDDIA 242
Cdd:PRK12744 220 KTGLTdIEDIV 230
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 8-206 1.25e-05

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


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 45.65  E-value: 1.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSS--GIGLRIAVLLARDEQKryhVIATMRDLKKKDRLVEAAGEVYGQTLtLLPLDICSDESVRQCVNSVKDR 85
Cdd:cd05372   2 KRILITGIANdrSIAWGIAKALHEAGAE---LAFTYQPEALRKRVEKLAERLGESAL-VLPCDVSNDEEIKELFAEVKKD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  86 --HIDVLINNAG----VGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKrqAGHIIIMSSVmGLQGVVFN-DVY 158
Cdd:cd05372  78 wgKLDGLVHSIAfapkVQLKGPFLDTSRKGFLKALDISAYSLVSLAKAALPIMNP--GGSIVTLSYL-GSERVVPGyNVM 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 37590327 159 TASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHT-------EFEtKMMEEVAKM 206
Cdd:cd05372 155 GVAKAALESSVRYLAYELGRKGIRVNAISAGPIKTlaasgitGFD-KMLEYSEQR 208
PRK07806 PRK07806
SDR family oxidoreductase;
8-145 1.25e-05

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 45.87  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLArdeQKRYHVIATMRD-LKKKDRLVEAAGEVYGQTLTlLPLDICSDESVRQCVNSVKDR- 85
Cdd:PRK07806   7 KTALVTGSSRGIGADTAKILA---GAGAHVVVNYRQkAPRANKVVAEIEAAGGRASA-VGADLTDEESVAALMDTAREEf 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37590327   86 -HIDVLINNAgvglLGPVESiSMDE---MKrvfeTNFFGTVRMIKEVMPDMkkRQAGHIIIMSS 145
Cdd:PRK07806  83 gGLDALVLNA----SGGMES-GMDEdyaMR----LNRDAQRNLARAALPLM--PAGSRVVFVTS 135
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 9-221 1.60e-05

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 45.67  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327     9 VVLITGCSSGIGLRIAV-LLARDEQKRYHVIATMRDLKK-KDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSV---- 82
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQeLAKCLKSPGSVLVLSARNDEAlRQLKAEIGAERSGLRVVRVSLDLGAEAGLEQLLKALrelp 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    83 --KDRHIDVLINNAG-VGLLGPVE-SIS-MDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIII--MSSVMGLQGVVFN 155
Cdd:TIGR01500  82 rpKGLQRLLLINNAGtLGDVSKGFvDLSdSTQVQNYWALNLTSMLCLTSSVLKAFKDSPGLNRTVvnISSLCAIQPFKGW 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37590327   156 DVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEvakmeypGADPDTVRYFKD 221
Cdd:TIGR01500 162 ALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQQVREE-------SVDPDMRKGLQE 220
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 8-164 5.31e-05

Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase [Carbohydrate transport and metabolism];


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 44.91  E-value: 5.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   8 KVVLITGCSSGIGLRIAVLLARDEQkryHVIATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRHI 87
Cdd:COG3347 426 RVALVTGGAGGIGRATAARLAAEGA---AVVVADLDGEAAEAAAAELGGGYGADAVDATDVDVTAEAAVAAAFGFAGLDI 502

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  88 ---DVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGhiIIMSSVMGLQGVVFNDVYTASKFA 164
Cdd:COG3347 503 ggsDIGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGLG--GSSVFAVSKNAAAAAYGAAAAATA 580
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 9-151 7.61e-05

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes 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: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 42.55  E-value: 7.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327     9 VVLITGCSSGIGLRIAVLLArdEQKRYHVIATMRDLKKKDRLVE--AAGEVYGQTLTLLPLDICSDESVRQCVNSVKDRH 86
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLA--ERGARHLVLLSRSAAPRPDAQAliAELEARGVEVVVVACDVSDPDAVAALLAEIKAEG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37590327    87 --IDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTvRMIKEVMPDmkkRQAGHIIIMSSVMGLQG 151
Cdd:pfam08659  80 ppIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGT-WNLHEATPD---EPLDFFVLFSSIAGLLG 142
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 8-222 1.99e-04

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 42.15  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    8 KVVLITGCSSGIGLRIAVLLARDEQKRYHVIATMRDLKKKDRLVEAAGEVygqTLTLLPLDICSDESVRQCVNSVKDRHI 87
Cdd:PRK08339   9 KLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNV---DVSYIVADLTKREDLERTVKELKNIGE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   88 -DVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIIMSSVMGLQGVVFNDVYTASKFAIE 166
Cdd:PRK08339  86 pDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVRISMA 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 37590327  167 GFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYPGADPDTVRYFKDV 222
Cdd:PRK08339 166 GLVRTLAKELGPKGITVNGIMPGIIRTDRVIQLAQDRAKREGKSVEEALQEYAKPI 221
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
 9-53 7.15e-04

aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 40.72  E-value: 7.15e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 37590327   9 VVLITGCSSGIGLRIAV-LLARDeqkrYHVIATMRDLKKKDRLVEA 53
Cdd:cd05227   1 LVLVTGATGFIASHIVEqLLKAG----YKVRGTVRSLSKSAKLKAL 42
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 7-215 7.60e-04

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: 40.00  E-value: 7.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   7 QKVVLITGCSSGIGLRIAVLLArdeQKRYHVIAtmRDLkkkdrlveAAGEVYGQTLTLLPLDICsDESVRQCVNSVKDRH 86
Cdd:cd05334   1 ARVVLVYGGRGALGSAVVQAFK---SRGWWVAS--IDL--------AENEEADASIIVLDSDSF-TEQAKQVVASVARLS 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  87 --IDVLINNAGvGLLG--PVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKrqAGHIIIMSSVMGLQGVVFNDVYTASK 162
Cdd:cd05334  67 gkVDALICVAG-GWAGgsAKSKSFVKNWDLMWKQNLWTSFIASHLATKHLLS--GGLLVLTGAKAALEPTPGMIGYGAAK 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 37590327 163 FAIEGFCESMAVQL--LKFNVKLSLIEPGPVHTEFETKMMeevakmeyPGADPDT 215
Cdd:cd05334 144 AAVHQLTQSLAAENsgLPAGSTANAILPVTLDTPANRKAM--------PDADFSS 190
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 9-198 1.67e-03

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: 39.53  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327     9 VVLITGCSSGIGLRIAVLLardEQKRYHV-IATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKD--- 84
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVAL---HQEGYRVvLHYHRSAAAASTLAAELNARRPNSAVTCQADLSNSATLFSRCEAIIDacf 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327    85 RHI---DVLINNA---------------GVGLLGPVESISMDemkrVFETNFFGTVRMIKEvmpdMKKRQAG-------- 138
Cdd:TIGR02685  80 RAFgrcDVLVNNAsafyptpllrgdageGVGDKKSLEVQVAE----LFGSNAIAPYFLIKA----FAQRQAGtraeqrst 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37590327   139 --HIIIMSSVMGLQGVVFNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPG----PVHTEFETK 198
Cdd:TIGR02685 152 nlSIVNLCDAMTDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGlsllPDAMPFEVQ 217
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 10-82 2.49e-03

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 38.89  E-value: 2.49e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37590327  10 VLITGCSSGIGlRIAVLLARdeQKRYHVIATMRDLKKKDRLVEAAGEVygQTLTLLPLdicSDESVRQCVNSV 82
Cdd:cd08270 136 VLVTGASGGVG-RFAVQLAA--LAGAHVVAVVGSPARAEGLRELGAAE--VVVGGSEL---SGAPVDLVVDSV 200
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 2-151 2.59e-03

ketoreductase (KR) and fatty acid synthase (FAS), 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. In some instances, such as porcine FAS, an enoyl reductase (ER) 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 consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase 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-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. 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. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in 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: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 39.29  E-value: 2.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   2 ASGGGQKVVLITGCSSGIGLRIAVLLARdeqkRY--HVIATMR-----DLKKKDRLVEAAGEVygqtLTLLPLDICSDES 74
Cdd:cd05274 145 APGGLDGTYLITGGLGGLGLLVARWLAA----RGarHLVLLSRrgpapRAAARAALLRAGGAR----VSVVRCDVTDPAA 216

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37590327  75 VRQCVNSV-KDRHIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIkEVMPDMKKRqagHIIIMSSVMGLQG 151
Cdd:cd05274 217 LAALLAELaAGGPLAGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNLH-ELTPDLPLD---FFVLFSSVAALLG 290
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
38-193 2.90e-03

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 38.56  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327   38 IATMRDLKKKDRLVEAAGEVYGQTLTLLPLDICSDESVRQCVNSVKDR--HIDvlinnagvGLLGPVESISMDEMK-RVF 114
Cdd:PRK08594  37 VFTYAGERLEKEVRELADTLEGQESLLLPCDVTSDEEITACFETIKEEvgVIH--------GVAHCIAFANKEDLRgEFL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590327  115 ETNFFG--------------TVRMIKEVMPDmkkrqaGHIIIMSSVMGLQGVVFN-DVYTASKFAIEGFCESMAVQLLKF 179
Cdd:PRK08594 109 ETSRDGfllaqnisaysltaVAREAKKLMTE------GGSIVTLTYLGGERVVQNyNVMGVAKASLEASVKYLANDLGKD 182

                        170
                 ....*....|....
gi 37590327  180 NVKLSLIEPGPVHT 193
Cdd:PRK08594 183 GIRVNAISAGPIRT 196
 
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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