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Conserved domains on  [gi|1207168417|ref|XP_021324955|]
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retinol dehydrogenase 8 isoform X1 [Danio rerio]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 8-211 1.49e-130

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


The actual alignment was detected with superfamily member cd09806:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 258  Bit Score: 369.87  E-value: 1.49e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLARDEQKRYHV-------------------------------------------------- 37
Cdd:cd09806     1 TVVLITGCSSGIGLHLAVRLASDPSKRFKVyatmrdlkkkgrlweaagalaggtletlqldvcdsksvaaavervterhv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 ----NNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEG 113
Cdd:cd09806    81 dvlvCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFALEG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYPGADPDTVRYFKDVYVPSSIDIFEAMGQTPDDIAKCTKK 193
Cdd:cd09806   161 LCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSPEEVLDRTADDITTFHFFYQYLAHSKQVFREAAQNPEEVAEVFLT 240

                         250
                  ....*....|....*...
gi 1207168417 194 VIETSQPRFRNLTNSLYT 211
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, ...
 8-211 1.49e-130

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: 369.87  E-value: 1.49e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLARDEQKRYHV-------------------------------------------------- 37
Cdd:cd09806     1 TVVLITGCSSGIGLHLAVRLASDPSKRFKVyatmrdlkkkgrlweaagalaggtletlqldvcdsksvaaavervterhv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 ----NNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEG 113
Cdd:cd09806    81 dvlvCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFALEG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYPGADPDTVRYFKDVYVPSSIDIFEAMGQTPDDIAKCTKK 193
Cdd:cd09806   161 LCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSPEEVLDRTADDITTFHFFYQYLAHSKQVFREAAQNPEEVAEVFLT 240

                         250
                  ....*....|....*...
gi 1207168417 194 VIETSQPRFRNLTNSLYT 211
Cdd:cd09806   241 AIRAPKPPLRYFTNERYL 258
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
7-162 1.33e-51

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 168.89  E-value: 1.33e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIA----------VLLARDEQK---------------RYH------------------------- 36
Cdd:COG0300     5 GKTVLITGASSGIGRALAralaargarvVLVARDAERlealaaelraagarvEVValdvtdpdavaalaeavlarfgpid 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 --VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGF 114
Cdd:COG0300    85 vlVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEGF 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1207168417 115 CESMAVQLLKFNVKLSLIEPGPVHTEFETKMMeevAKMEYPGADPDTV 162
Cdd:COG0300   165 SESLRAELAPTGVRVTAVCPGPVDTPFTARAG---APAGRPLLSPEEV 209
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 7-212 2.49e-42

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 145.43  E-value: 2.49e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIAVLLAR------------------------------------------DEQKRYH--VNNAGV 42
Cdd:PRK06179    4 SKVALVTGASSGIGRATAEKLARagyrvfgtsrnparaapipgvelleldvtddasvqaavdeviARAGRIDvlVNNAGV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  43 GLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMAVQL 122
Cdd:PRK06179   84 GLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKHAVEGYSESLDHEV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 123 LKFNVKLSLIEPGPVHTEFETKMMEEVAKM-EYpgadpDTVR-YFKDVyvpssidIFEAM--GQTPDDIAKCTKKVIETS 198
Cdd:PRK06179  164 RQFGIRVSLVEPAYTKTNFDANAPEPDSPLaEY-----DRERaVVSKA-------VAKAVkkADAPEVVADTVVKAALGP 231

                         250
                  ....*....|....
gi 1207168417 199 QPRFRnltnslYTP 212
Cdd:PRK06179  232 WPKMR------YTA 239
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 8-153 9.75e-38

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 131.20  E-value: 9.75e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLA---------------------------------------RDEQKRYH------------ 36
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAkegakvvlvdrseekleavakelgalggkalfiqgdvtdRAQVKALVeqaverlgrldi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:pfam00106  81 lVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHTEfetkMMEEVAKME 153
Cdd:pfam00106 161 RSLALELAPHGIRVNAVAPGGVDTD----MTKELREDE 194
 
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, ...
 8-211 1.49e-130

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: 369.87  E-value: 1.49e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLARDEQKRYHV-------------------------------------------------- 37
Cdd:cd09806     1 TVVLITGCSSGIGLHLAVRLASDPSKRFKVyatmrdlkkkgrlweaagalaggtletlqldvcdsksvaaavervterhv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 ----NNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEG 113
Cdd:cd09806    81 dvlvCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFALEG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYPGADPDTVRYFKDVYVPSSIDIFEAMGQTPDDIAKCTKK 193
Cdd:cd09806   161 LCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSPEEVLDRTADDITTFHFFYQYLAHSKQVFREAAQNPEEVAEVFLT 240

                         250
                  ....*....|....*...
gi 1207168417 194 VIETSQPRFRNLTNSLYT 211
Cdd:cd09806   241 AIRAPKPPLRYFTNERYL 258
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 8-208 5.34e-58

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: 185.13  E-value: 5.34e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR----------------------------------DEQ----------KRYH-----VN 38
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAqgyrviatarnpdkleslgellndnlevleldvtDEEsikaavkeviERFGridvlVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  39 NAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESM 118
Cdd:cd05374    81 NAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEALSESL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 119 AVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYPGAdpdtvryfkdvYVPSSIDIFEAM------GQTPDDIAKCTK 192
Cdd:cd05374   161 RLELAPFGIKVTIIEPGPVRTGFADNAAGSALEDPEISP-----------YAPERKEIKENAagvgsnPGDPEKVADVIV 229

                         250
                  ....*....|....*.
gi 1207168417 193 KVIETSQPRFRNLTNS 208
Cdd:cd05374   230 KALTSESPPLRYFLGS 245
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
7-162 1.33e-51

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 168.89  E-value: 1.33e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIA----------VLLARDEQK---------------RYH------------------------- 36
Cdd:COG0300     5 GKTVLITGASSGIGRALAralaargarvVLVARDAERlealaaelraagarvEVValdvtdpdavaalaeavlarfgpid 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 --VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGF 114
Cdd:COG0300    85 vlVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEGF 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1207168417 115 CESMAVQLLKFNVKLSLIEPGPVHTEFETKMMeevAKMEYPGADPDTV 162
Cdd:COG0300   165 SESLRAELAPTGVRVTAVCPGPVDTPFTARAG---APAGRPLLSPEEV 209
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-201 3.03e-47

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: 157.27  E-value: 3.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   1 MASGGgqKVVLITGCSSGIGLRIA----------VLLARDEQK------------RYH---------------------- 36
Cdd:COG4221     1 MSDKG--KVALITGASSGIGAATAralaaagarvVLAARRAERlealaaelggraLAVpldvtdeaaveaavaaavaefg 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -----VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAI 111
Cdd:COG4221    79 rldvlVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 112 EGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAkmeypgadpdtvRYFKDVYVPssidiFEAMgqTPDDIAKCT 191
Cdd:COG4221   159 RGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDA------------EAAAAVYEG-----LEPL--TPEDVAEAV 219

                         250
                  ....*....|
gi 1207168417 192 KKVIetSQPR 201
Cdd:COG4221   220 LFAL--TQPA 227
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 7-212 2.49e-42

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 145.43  E-value: 2.49e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIAVLLAR------------------------------------------DEQKRYH--VNNAGV 42
Cdd:PRK06179    4 SKVALVTGASSGIGRATAEKLARagyrvfgtsrnparaapipgvelleldvtddasvqaavdeviARAGRIDvlVNNAGV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  43 GLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMAVQL 122
Cdd:PRK06179   84 GLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKHAVEGYSESLDHEV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 123 LKFNVKLSLIEPGPVHTEFETKMMEEVAKM-EYpgadpDTVR-YFKDVyvpssidIFEAM--GQTPDDIAKCTKKVIETS 198
Cdd:PRK06179  164 RQFGIRVSLVEPAYTKTNFDANAPEPDSPLaEY-----DRERaVVSKA-------VAKAVkkADAPEVVADTVVKAALGP 231

                         250
                  ....*....|....
gi 1207168417 199 QPRFRnltnslYTP 212
Cdd:PRK06179  232 WPKMR------YTA 239
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 10-159 5.81e-41

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: 140.88  E-value: 5.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  10 VLITGCSSGIGLRIAVLLARD-----------------EQKRYH----------------------------------VN 38
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREgakvvladrneealaelAAIEALggnavavqadvsdeedvealveealeefgrldilVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  39 NAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESM 118
Cdd:cd05233    81 NAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1207168417 119 AVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYPGADP 159
Cdd:cd05233   161 ALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAAIP 201
PRK06914 PRK06914
SDR family oxidoreductase;
7-203 8.28e-38

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 134.00  E-value: 8.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIAVLLAR---------------------------------------DEQ---------KRYH-- 36
Cdd:PRK06914    3 KKIAIVTGASSGFGLLTTLELAKkgylviatmrnpekqenllsqatqlnlqqnikvqqldvtDQNsihnfqlvlKEIGri 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 ---VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEG 113
Cdd:PRK06914   83 dllVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYALEG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVakMEYPGADPDTVRYFKDV--YVPSSIDIFEAmgqtPDDIAKCT 191
Cdd:PRK06914  163 FSESLRLELKPFGIDVALIEPGSYNTNIWEVGKQLA--ENQSETTSPYKEYMKKIqkHINSGSDTFGN----PIDVANLI 236

                         250
                  ....*....|..
gi 1207168417 192 KKVIETSQPRFR 203
Cdd:PRK06914  237 VEIAESKRPKLR 248
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 8-153 9.75e-38

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 131.20  E-value: 9.75e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLA---------------------------------------RDEQKRYH------------ 36
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAkegakvvlvdrseekleavakelgalggkalfiqgdvtdRAQVKALVeqaverlgrldi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:pfam00106  81 lVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHTEfetkMMEEVAKME 153
Cdd:pfam00106 161 RSLALELAPHGIRVNAVAPGGVDTD----MTKELREDE 194
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 8-148 1.81e-36

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 130.42  E-value: 1.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA----------VLLARDEQK----------RYH-----------------------------VN 38
Cdd:PRK06180    5 KTWLITGVSSGFGRALAqaalaaghrvVGTVRSEAAradfealhpdRALarlldvtdfdaidavvadaeatfgpidvlVN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  39 NAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESM 118
Cdd:PRK06180   85 NAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFALEGISESL 164

                         170       180       190
                  ....*....|....*....|....*....|
gi 1207168417 119 AVQLLKFNVKLSLIEPGPVHTEFETKMMEE 148
Cdd:PRK06180  165 AKEVAPFGIHVTAVEPGSFRTDWAGRSMVR 194
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 8-188 5.40e-35

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: 125.67  E-value: 5.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA----------VLLARDEQK---------------RYH-------------------------- 36
Cdd:COG1028     7 KVALVTGGSSGIGRAIAralaaegarvVITDRDAEAleaaaaelraaggraLAVaadvtdeaavealvaaavaafgrldi 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:COG1028    87 lVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLT 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHTEfetkMMEEVAkmeypgADPDTVRYFKDvYVPssidifeaMGQ--TPDDIA 188
Cdd:COG1028   167 RSLALELAPRGIRVNAVAPGPIDTP----MTRALL------GAEEVREALAA-RIP--------LGRlgTPEEVA 222
PRK06182 PRK06182
short chain dehydrogenase; Validated
 6-217 6.60e-35

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 126.23  E-value: 6.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   6 GQKVVLITGCSSGIGLRIAVLLAR-------------------------------DEQKRYH---------------VNN 39
Cdd:PRK06182    2 QKKVALVTGASSGIGKATARRLAAqgytvygaarrvdkmedlaslgvhplsldvtDEASIKAavdtiiaeegridvlVNN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  40 AGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMA 119
Cdd:PRK06182   82 AGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFALEGFSDALR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 120 VQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYPGADPDTVRYFKDVYVPSSIDifeAMGQTPDDIAKCTKKVIETSQ 199
Cdd:PRK06182  162 LEVAPFGIDVVVIEPGGIKTEWGDIAADHLLKTSGNGAYAEQAQAVAASMRSTYGS---GRLSDPSVIADAISKAVTARR 238

                         250
                  ....*....|....*...
gi 1207168417 200 PRFRNLTNSLYTPIVAMK 217
Cdd:PRK06182  239 PKTRYAVGFGAKPLIFLR 256
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 8-154 2.04e-33

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: 121.92  E-value: 2.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA----------VLLARDEQK-------------------------------------------R 34
Cdd:cd05332     4 KVVIITGASSGIGEELAyhlarlgarlVLSARREERleevkseclelgapsphvvpldmsdledaeqvveealklfgglD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  35 YHVNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGF 114
Cdd:cd05332    84 ILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHALQGF 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1207168417 115 CESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEY 154
Cdd:cd05332   164 FDSLRAELSEPNISVTVVCPGLIDTNIAMNALSGDGSMSA 203
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 10-158 1.72e-32

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: 117.62  E-value: 1.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  10 VLITGCSSGIGLRIAVLLARD--------EQKRYHVNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKR 81
Cdd:cd02266     1 VLVTGGSGGIGGAIARWLASRgspkvlvvSRRDVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  82 QAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETK---MMEEVAKMEYPGAD 158
Cdd:cd02266    81 RLGRFILISSVAGLFGAPGLGGYAASKAALDGLAQQWASEGWGNGLPATAVACGTWAGSGMAKgpvAPEEILGNRRHGVR 160
PRK08017 PRK08017
SDR family oxidoreductase;
7-141 2.46e-31

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 116.34  E-value: 2.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIAVLLardEQKRYHV------------------------------------------------- 37
Cdd:PRK08017    2 QKSVLITGCSSGIGLEAALEL---KRRGYRVlaacrkpddvarmnslgftgilldlddpesveraadevialtdnrlygl 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 -NNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK08017   79 fNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALEAWSD 158

                         170       180
                  ....*....|....*....|....*
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHTEF 141
Cdd:PRK08017  159 ALRMELRHSGIKVSLIEPGPIRTRF 183
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 37-153 1.62e-30

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 114.75  E-value: 1.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK08263   82 VNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALEGMSE 161

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKME 153
Cdd:PRK08263  162 ALAQEVAEFGIKVTLVEPGGYSTDWAGTSAKRATPLD 198
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 8-152 1.05e-28

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: 108.88  E-value: 1.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA----------VLLARDEQK-------------------RYH---------------------- 36
Cdd:cd08939     2 KHVLITGGSSGIGKALAkelvkeganvIIVARSESKleeaveeieaeanasgqkvSYIsadlsdyeeveqafaqavekgg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -----VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAI 111
Cdd:cd08939    82 ppdlvVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKFAL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1207168417 112 EGFCESMAVQLLKFNVKLSLIEPGPVHTEF----------ETKMMEEVAKM 152
Cdd:cd08939   162 RGLAESLRQELKPYNIRVSVVYPPDTDTPGfeeenktkpeETKAIEGSSGP 212
PRK05993 PRK05993
SDR family oxidoreductase;
6-141 2.58e-28

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 108.96  E-value: 2.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   6 GQKVVLITGCSSGIG--------------------------LR----------------IAVL----LARDEQKRYHV-N 38
Cdd:PRK05993    3 MKRSILITGCSSGIGaycaralqsdgwrvfatcrkeedvaaLEaegleafqldyaepesIAALvaqvLELSGGRLDALfN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  39 NAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESM 118
Cdd:PRK05993   83 NGAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAYNASKFAIEGLSLTL 162

                         170       180
                  ....*....|....*....|...
gi 1207168417 119 AVQLLKFNVKLSLIEPGPVHTEF 141
Cdd:PRK05993  163 RMELQGSGIHVSLIEPGPIETRF 185
PRK09291 PRK09291
SDR family oxidoreductase;
7-147 1.04e-27

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 107.01  E-value: 1.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIAVLLAR-------------------------------------DEQKRYH---------VNNA 40
Cdd:PRK09291    2 SKTILITGAGSGFGREVALRLARkghnviagvqiapqvtalraeaarrglalrvekldltDAIDRAQaaewdvdvlLNNA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  41 GVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMAV 120
Cdd:PRK09291   82 GIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHALEAIAEAMHA 161

                         170       180
                  ....*....|....*....|....*..
gi 1207168417 121 QLLKFNVKLSLIEPGPVHTEFETKMME 147
Cdd:PRK09291  162 ELKPFGIQVATVNPGPYLTGFNDTMAE 188
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 1-141 2.14e-27

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 107.70  E-value: 2.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   1 MASGGGQKVVLITGCSSGIGLRIA----------VLLARDEQK--------RYH-------------------------- 36
Cdd:PRK07109    2 MLKPIGRQVVVITGASAGVGRATArafarrgakvVLLARGEEGlealaaeiRAAggealavvadvadaeavqaaadraee 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 --------VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASK 108
Cdd:PRK07109   82 elgpidtwVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAK 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1207168417 109 FAIEGFCESMAVQLL--KFNVKLSLIEPGPVHTEF 141
Cdd:PRK07109  162 HAIRGFTDSLRCELLhdGSPVSVTMVQPPAVNTPQ 196
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 3-154 1.14e-25

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: 101.08  E-value: 1.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   3 SGGGQKVVLITGCSSGIGLRIAVLLARDEQKRYH--VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKK 80
Cdd:cd08934    49 AEGGKALVLELDVTDEQQVDAAVERTVEALGRLDilVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLL 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207168417  81 RQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEY 154
Cdd:cd08934   129 RNKGTIVNISSVAGRVAVRNSAVYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHITHTITKEAY 202
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 8-213 2.37e-25

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: 100.43  E-value: 2.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA----------VLLAR-----------------------------------------DEQKRYH 36
Cdd:cd05346     1 KTVLITGASSGIGEATArrfakagaklILTGRraerlqeladelgakfpvkvlplqldvsdresieaalenlpEEFRDID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 --VNNAGVGL-LGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEG 113
Cdd:cd05346    81 ilVNNAGLALgLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAVRQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPGPVHTEFET---KMMEEVAKMEYPGADPdtvryfkdvyvpssidifeamgQTPDDIAKC 190
Cdd:cd05346   161 FSLNLRKDLIGTGIRVTNIEPGLVETEFSLvrfHGDKEKADKVYEGVEP----------------------LTPEDIAET 218

                         250       260
                  ....*....|....*....|...
gi 1207168417 191 TkkVIETSQPRFRNLTNSLYTPI 213
Cdd:cd05346   219 I--LWVASRPAHVNINDIEIMPV 239
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-148 3.33e-25

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 99.92  E-value: 3.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLA-----------RDEQ-------------------------------------KRYH--- 36
Cdd:PRK05565    6 KVAIVTGASGGIGRAIAELLAkegakvviaydINEEaaqelleeikeeggdaiavkadvsseedvenlveqivEKFGkid 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 --VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGF 114
Cdd:PRK05565   86 ilVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKGAVNAF 165

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1207168417 115 CESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEE 148
Cdd:PRK05565  166 TKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEE 199
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 9-141 4.85e-25

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


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 99.38  E-value: 4.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   9 VVLITGCSSGIGLRIA----------VLLARDEQKRYH------------------------------------------ 36
Cdd:cd05360     2 VVVITGASSGIGRATAlafaergakvVLAARSAEALHElarevrelggeaiavvadvadaaqveraadtaverfgridtw 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:cd05360    82 VNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTE 161

                         170       180
                  ....*....|....*....|....*..
gi 1207168417 117 SMAVQLLK--FNVKLSLIEPGPVHTEF 141
Cdd:cd05360   162 SLRAELAHdgAPISVTLVQPTAMNTPF 188
PRK06181 PRK06181
SDR family oxidoreductase;
8-157 1.85e-23

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 95.82  E-value: 1.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIG----LRIA------VLLARDEQ---------KRYH-------------------------------- 36
Cdd:PRK06181    2 KVVIITGASEGIGralaVRLAragaqlVLAARNETrlaslaqelADHGgealvvptdvsdaeacerlieaavarfggidi 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVGLLGPVESIS-MDEMKRVFETNFFGTVRMIKEVMPDMKKRQaGHIIVMSSVMGLQGVVFNDVYTASKFAIEGF 114
Cdd:PRK06181   82 lVNNAGITMWSRFDELTdLSVFERVMRVNYLGAVYCTHAALPHLKASR-GQIVVVSSLAGLTGVPTRSGYAASKHALHGF 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207168417 115 CESMAVQLLKFNVKLSLIEPGPVHTEF------------------ETKMM--EEVAKMEYPGA 157
Cdd:PRK06181  161 FDSLRIELADDGVAVTVVCPGFVATDIrkraldgdgkplgkspmqESKIMsaEECAEAILPAI 223
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-150 3.10e-23

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 94.76  E-value: 3.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAV----------LLARDEQ---------KRYHV------------------------------- 37
Cdd:PRK07666    8 KNALITGAGRGIGRAVAIalakegvnvgLLARTEEnlkavaeevEAYGVkvviatadvsdyeevtaaieqlknelgsidi 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 --NNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:PRK07666   88 liNNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKFGVLGLT 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHTEF----------ETKMM--EEVA 150
Cdd:PRK07666  168 ESLMQEVRKHNIRVTALTPSTVATDMavdlgltdgnPDKVMqpEDLA 214
PRK07326 PRK07326
SDR family oxidoreductase;
1-141 6.91e-23

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 93.54  E-value: 6.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   1 MASGGGqKVVLITGCSSGIGLRIAVLLAR---------------------------------------DEQKRYH----- 36
Cdd:PRK07326    1 MMSLKG-KVALITGGSKGIGFAIAEALLAegykvaitardqkeleeaaaelnnkgnvlglaadvrdeaDVQRAVDaivaa 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -------VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQaGHIIVMSSVMGLQGVVFNDVYTASKF 109
Cdd:PRK07326   80 fggldvlIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGG-GYIINISSLAGTNFFAGGAAYNASKF 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1207168417 110 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTEF 141
Cdd:PRK07326  159 GLVGFSEAAMLDLRQYGIKVSTIMPGSVATHF 190
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 9-141 7.71e-23

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


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 93.46  E-value: 7.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   9 VVLITGCSSGIGLRIAVLLAR--------------------------------------DEQ--------KRYH------ 36
Cdd:cd05339     1 IVLITGGGSGIGRLLALEFAKrgakvvildinekgaeetannvrkaggkvhyykcdvskREEvyeaakkiKKEVgdvtil 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:cd05339    81 INNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFHE 160

                         170       180
                  ....*....|....*....|....*...
gi 1207168417 117 SMAVQLL---KFNVKLSLIEPGPVHTEF 141
Cdd:cd05339   161 SLRLELKaygKPGIKTTLVCPYFINTGM 188
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 1-188 9.31e-23

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 93.97  E-value: 9.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   1 MASGGGqKVVLITGCSSGIGLRIAVLLAR--------------------------------------------DEQKRYH 36
Cdd:PRK12829    6 LKPLDG-LRVLVTGGASGIGRAIAEAFAEagarvhvcdvseaalaataarlpgakvtatvadvadpaqvervfDTAVERF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 ------VNNAGV-GLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAG-HIIVMSSVMGLQGVVFNDVYTASK 108
Cdd:PRK12829   85 ggldvlVNNAGIaGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGgVIIALSSVAGRLGYPGRTPYAASK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 109 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYPGADPDTVRYFKdvYVPssidiFEAMGqTPDDIA 188
Cdd:PRK12829  165 WAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEARAQQLGIGLDEMEQEYLE--KIS-----LGRMV-EPEDIA 236
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 8-151 4.21e-22

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


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 91.68  E-value: 4.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLARD----------------------EQKRYH---------------------------VN 38
Cdd:cd05341     6 KVAIVTGGARGLGLAHARLLVAEgakvvlsdildeegqaaaaelgDAARFFhldvtdedgwtavvdtareafgrldvlVN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  39 NAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESM 118
Cdd:cd05341    86 NAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKGAVRGLTKSA 165

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1207168417 119 AVQL--LKFNVKLSLIEPGPVHtefeTKMMEEVAK 151
Cdd:cd05341   166 ALECatQGYGIRVNSVHPGYIY----TPMTDELLI 196
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-162 2.68e-21

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 89.25  E-value: 2.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGL-RIAVLLARDEQ-------------KRYHV-----------------------NNAGVgLLG--PV 48
Cdd:PRK06550    6 KTVLITGAASGIGLaQARAFLAQGAQvygvdkqdkpdlsGNFHFlqldlsddleplfdwvpsvdilcNTAGI-LDDykPL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  49 ESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMAVQLLKFNVK 128
Cdd:PRK06550   85 LDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHALAGFTKQLALDYAKDGIQ 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1207168417 129 LSLIEPGPVHT-----EFET-KMMEEVAKmEYPG---ADPDTV 162
Cdd:PRK06550  165 VFGIAPGAVKTpmtaaDFEPgGLADWVAR-ETPIkrwAEPEEV 206
PRK12826 PRK12826
SDR family oxidoreductase;
8-188 2.86e-21

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 89.59  E-value: 2.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLARD--------------------------------------------------EQKRYH- 36
Cdd:PRK12826    7 RVALVTGAARGIGRAIAVRLAADgaevivvdicgddaaataelveaaggkararqvdvrdraalkaavaagveDFGRLDi 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQ-GVVFNDVYTASKFAIEGF 114
Cdd:PRK12826   87 lVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRvGYPGLAHYAASKAGLVGF 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207168417 115 CESMAVQLLKFNVKLSLIEPGPVHTEfetkMMEEVAKMEYPGAdpdtvryfkdvyVPSSIDIFEAMgqTPDDIA 188
Cdd:PRK12826  167 TRALALELAARNITVNSVHPGGVDTP----MAGNLGDAQWAEA------------IAAAIPLGRLG--EPEDIA 222
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 37-135 3.69e-21

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: 90.03  E-value: 3.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGV-GLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPdMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:cd09805    83 VNNAGIlGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLP-LLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAAVEAFS 161

                          90       100
                  ....*....|....*....|
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPG 135
Cdd:cd09805   162 DSLRRELQPWGVKVSIIEPG 181
PRK06482 PRK06482
SDR family oxidoreductase;
37-141 4.02e-21

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 89.79  E-value: 4.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK06482   81 VSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIEGFVE 160

                          90       100
                  ....*....|....*....|....*
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHTEF 141
Cdd:PRK06482  161 AVAQEVAPFGIEFTIVEPGPARTNF 185
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 8-203 4.76e-21

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: 88.19  E-value: 4.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLARD-------------------EQKRYH-----------------------------VNN 39
Cdd:cd08932     1 KVALVTGASRGIGIEIARALARDgyrvslglrnpedlaalsaSGGDVEavpydardpedaralvdalrdrfgridvlVHN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  40 AGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMA 119
Cdd:cd08932    81 AGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALAHALR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 120 VQLLKFNVKLSLIEPGPVhtefETKMMEEVAKMEYPGAdpdtvryfkdvyvpssidifEAMGQtPDDIAKCTKKVIETSQ 199
Cdd:cd08932   161 QEGWDHGVRVSAVCPGFV----DTPMAQGLTLVGAFPP--------------------EEMIQ-PKDIANLVRMVIELPE 215


                  ....
gi 1207168417 200 PRFR 203
Cdd:cd08932   216 NITS 219
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-188 4.91e-21

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 88.77  E-value: 4.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLARD-------------------EQKRYH-------------------------------- 36
Cdd:PRK12825    7 RVALVTGAARGLGRAIALRLARAgadvvvhyrsdeeaaeelvEAVEALgrraqavqadvtdkaaleaavaaaverfgrid 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 --VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGF 114
Cdd:PRK12825   87 ilVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKAGLVGL 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207168417 115 CESMAVQLLKFNVKLSLIEPGPVHTEfetkMMEEVAKMEypgadpdtvRYFKDVYVPssidifeaMGQ--TPDDIA 188
Cdd:PRK12825  167 TKALARELAEYGITVNMVAPGDIDTD----MKEATIEEA---------REAKDAETP--------LGRsgTPEDIA 221
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 37-152 1.00e-20

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: 87.87  E-value: 1.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVG--LLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRqaGHIIVMSSVMGLQGVVFNDVYTASKFAIEGF 114
Cdd:pfam13561  76 VNNAGFApkLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEG--GSIVNLSSIGAERVVPNYNAYGAAKAALEAL 153

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1207168417 115 CESMAVQLLKFNVKLSLIEPGPVHT-------EFEtKMMEEVAKM 152
Cdd:pfam13561 154 TRYLAVELGPRGIRVNAISPGPIKTlaasgipGFD-ELLAAAEAR 197
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 8-141 1.06e-20

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: 87.29  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA-----------VLLARDEQK---------------RYH------------------------- 36
Cdd:cd05324     1 KVALVTGANRGIGFEIVrqlaksgpgtvILTARDVERgqaaveklraeglsvRFHqldvtddasieaaadfveekyggld 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 --VNNAGVGLLGPVESISMDE-MKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVvfndVYTASKFAIEG 113
Cdd:cd05324    81 ilVNNAGIAFKGFDDSTPTREqARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLTS----AYGVSKAALNA 156

                         170       180
                  ....*....|....*....|....*...
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPGPVHTEF 141
Cdd:cd05324   157 LTRILAKELKETGIKVNACCPGWVKTDM 184
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
8-152 4.15e-20

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 86.37  E-value: 4.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLA----------RDEQK----------------------------------------RYH- 36
Cdd:PRK05653    6 KTALVTGASRGIGRAIALRLAadgakvviydSNEEAaealaaelraaggearvlvfdvsdeaavralieaaveafgALDi 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:PRK05653   86 lVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAGVIGFT 165

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVhtefETKMMEEVAKM 152
Cdd:PRK05653  166 KALALELASRGITVNAVAPGFI----DTDMTEGLPEE 198
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 7-140 7.84e-20

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 85.63  E-value: 7.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIAVLLARD--------------------EQKRYH------------------------------ 36
Cdd:PRK05557    5 GKVALVTGASRGIGRAIAERLAAQganvvinyasseagaealvaEIGALGgkalavqgdvsdaesveravdeakaefggv 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 ---VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEG 113
Cdd:PRK05557   85 dilVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAGVIG 164

                         170       180
                  ....*....|....*....|....*..
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:PRK05557  165 FTKSLARELASRGITVNAVAPGFIETD 191
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 8-141 1.58e-19

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: 84.48  E-value: 1.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLL----------ARDE---------------------------QKRYH------------VN 38
Cdd:cd08929     1 KAALVTGASRGIGEATARLLhaegyrvgicARDEarlaaaaaqelegvlglagdvrdeadvRRAVDameeafggldalVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  39 NAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESM 118
Cdd:cd08929    81 NAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSEAA 160

                         170       180
                  ....*....|....*....|...
gi 1207168417 119 AVQLLKFNVKLSLIEPGPVHTEF 141
Cdd:cd08929   161 MLDLREANIRVVNVMPGSVDTGF 183
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 8-188 1.75e-19

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 84.63  E-value: 1.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLARDEQK---RYH------------------------------------------------ 36
Cdd:cd05362     4 KVALVTGASRGIGRAIAKRLARDGASvvvNYAsskaaaeevvaeieaaggkaiavqadvsdpsqvarlfdaaekafggvd 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 --VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMkkRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGF 114
Cdd:cd05362    84 ilVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAAYTPNYGAYAGSKAAVEAF 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207168417 115 CESMAVQLLKFNVKLSLIEPGPVHTEfetkmmeevakMEYPGADPDTVRYFKdvyvpsSIDIFEAMGQtPDDIA 188
Cdd:cd05362   162 TRVLAKELGGRGITVNAVAPGPVDTD-----------MFYAGKTEEAVEGYA------KMSPLGRLGE-PEDIA 217
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 10-145 1.87e-19

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: 84.30  E-value: 1.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  10 VLITGCSSGIGLRIA----------VLLARDE------------------------------QKRYH------------V 37
Cdd:cd05350     1 VLITGASSGIGRALArefakagynvALAARRTdrldelkaellnpnpsveveildvtdeernQLVIAeleaelggldlvI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 NNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCES 117
Cdd:cd05350    81 INAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLAES 160

                         170       180
                  ....*....|....*....|....*...
gi 1207168417 118 MAVQLLKFNVKLSLIEPGPVHTEFETKM 145
Cdd:cd05350   161 LRYDVKKRGIRVTVINPGFIDTPLTANM 188
PRK06138 PRK06138
SDR family oxidoreductase;
7-188 1.01e-18

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 82.89  E-value: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIAVLLAR------------------------DEQKRYH-------------------------- 36
Cdd:PRK06138    5 GRVAIVTGAGSGIGRATAKLFARegarvvvadrdaeaaervaaaiaaGGRAFARqgdvgsaeavealvdfvaarwgrldv 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:PRK06138   85 lVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAIASLT 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVakmeypgADPDTVRyfkdvyvpSSIDIFEAMGQ--TPDDIA 188
Cdd:PRK06138  165 RAMALDHATDGIRVNAVAPGTIDTPYFRRIFARH-------ADPEALR--------EALRARHPMNRfgTAEEVA 224
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 8-161 1.05e-18

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


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 82.41  E-value: 1.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR----------------DEQKRYH----------------------------------- 36
Cdd:cd05347     6 KVALVTGASRGIGFGIASGLAEaganivinsrneekaeEAQQLIEkegveataftcdvsdeeaikaaveaieedfgkidi 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:cd05347    86 lVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGVAGLT 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGpvhtEFETKMMEEVakmeypGADPDT 161
Cdd:cd05347   166 KALATEWARHGIQVNAIAPG----YFATEMTEAV------VADPEF 201
PRK05693 PRK05693
SDR family oxidoreductase;
7-141 4.94e-18

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 81.38  E-value: 4.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIA--------------------------------------VLLAR--DEQKRYH------VNNA 40
Cdd:PRK05693    1 MPVVLITGCSSGIGRALAdafkaagyevwatarkaedvealaaagftavqldvndgAALARlaEELEAEHggldvlINNA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  41 GVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMkKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMAV 120
Cdd:PRK05693   81 GYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLL-RRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHALSDALRL 159

                         170       180
                  ....*....|....*....|.
gi 1207168417 121 QLLKFNVKLSLIEPGPVHTEF 141
Cdd:PRK05693  160 ELAPFGVQVMEVQPGAIASQF 180
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 8-162 8.47e-18

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


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 80.04  E-value: 8.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLA----------RDEQK---------------RYH-------------------------- 36
Cdd:cd05323     1 KVAIITGGASGIGLATAKLLLkkgakvaildRNENPgaaaelqainpkvkaTFVqcdvtsweqlaaafkkaiekfgrvdi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVGllgpvESISMDE-------MKRVFETNFFGTVRMIKEVMPDMKKRQAGH---IIVMSSVMGLQGVVFNDVYT 105
Cdd:cd05323    81 lINNAGIL-----DEKSYLFagklpppWEKTIDVNLTGVINTTYLALHYMDKNKGGKggvIVNIGSVAGLYPAPQFPVYS 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 106 ASKFAIEGFCESMAVQL-LKFNVKLSLIEPGPVHTEFETKMMEEVAKME--YPGADPDTV 162
Cdd:cd05323   156 ASKHGVVGFTRSLADLLeYKTGVRVNAICPGFTNTPLLPDLVAKEAEMLpsAPTQSPEVV 215
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 8-190 1.10e-17

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: 80.11  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLARD----------------------EQKRYH----------------------------- 36
Cdd:cd05366     3 KVAIITGAAQGIGRAIAERLAADgfnivladlnleeaakstiqeiSEAGYNavavgadvtdkddvealidqavekfgsfd 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 --VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQ-AGHIIVMSSVMGLQGVVFNDVYTASKFAIEG 113
Cdd:cd05366    83 vmVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINASSIAGVQGFPNLGAYSASKFAVRG 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMeypGADPDTVRYfkdVYVPSSIdifeAMG--QTPDDIAKC 190
Cdd:cd05366   163 LTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVGEI---AGKPEGEGF---AEFSSSI----PLGrlSEPEDVAGL 231
PRK07832 PRK07832
SDR family oxidoreductase;
37-196 4.99e-17

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 78.55  E-value: 4.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDM-KKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:PRK07832   83 MNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMvAAGRGGHLVNVSSAAGLVALPWHAAYSASKFGLRGLS 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHTEFetkmmeeVAKMEYPGADPDTVRyfkdvyVPSSIDIFEAMGQTPDDIAKCTKKVI 195
Cdd:PRK07832  163 EVLRFDLARHGIGVSVVVPGAVKTPL-------VNTVEIAGVDREDPR------VQKWVDRFRGHAVTPEKAAEKILAGV 229


                  .
gi 1207168417 196 E 196
Cdd:PRK07832  230 E 230
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 8-140 9.03e-17

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 77.67  E-value: 9.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLA----------RDEQK-----------RYH---------------------------VNN 39
Cdd:PRK07825    6 KVVAITGGARGIGLATARALAalgarvaigdLDEALaketaaelglvVGGpldvtdpasfaafldaveadlgpidvlVNN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  40 AGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHII---VMSSVMGLQGVVfndVYTASKFAIEGFCE 116
Cdd:PRK07825   86 AGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVnvaSLAGKIPVPGMA---TYCASKHAVVGFTD 162

                         170       180
                  ....*....|....*....|....
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:PRK07825  163 AARLELRGTGVHVSVVLPSFVNTE 186
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 8-151 1.13e-16

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: 77.17  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLA--------------------------------------RDEQ---------KRYH---- 36
Cdd:cd05343     7 RVALVTGASVGIGAAVARALVqhgmkvvgcarrvdkiealaaecqsagyptlfpyqcdlSNEEqilsmfsaiRTQHqgvd 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 --VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQA--GHIIVMSSVMG---LQGVVFNdVYTASKF 109
Cdd:cd05343    87 vcINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVddGHIININSMSGhrvPPVSVFH-FYAATKH 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1207168417 110 AIEGFCESMAVQL--LKFNVKLSLIEPGPVHTEFETKMMEEVAK 151
Cdd:cd05343   166 AVTALTEGLRQELreAKTHIRATSISPGLVETEFAFKLHDNDPE 209
PRK08264 PRK08264
SDR family oxidoreductase;
8-162 1.77e-16

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 76.08  E-value: 1.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA-VLLARDEQKRYH-----------------------------------------VNNAGVGLL 45
Cdd:PRK08264    7 KVVLVTGANRGIGRAFVeQLLARGAAKVYAaardpesvtdlgprvvplqldvtdpasvaaaaeaasdvtilVNNAGIFRT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  46 G-PVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMAVQLLK 124
Cdd:PRK08264   87 GsLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAAAWSLTQALRAELAP 166

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1207168417 125 FNVKLSLIEPGPVHTEfetkMmeeVAKMEYPGADPDTV 162
Cdd:PRK08264  167 QGTRVLGVHPGPIDTD----M---AAGLDAPKASPADV 197
FabG-like PRK07231
SDR family oxidoreductase;
8-188 2.64e-16

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 76.02  E-value: 2.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR--------------------------------------DEQKR-------------YH 36
Cdd:PRK07231    6 KVAIVTGASSGIGEGIARRFAAegarvvvtdrneeaaervaaeilaggraiavaadvsdeADVEAavaaalerfgsvdIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLL-GPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:PRK07231   86 VNNAGTTHRnGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGAVITLT 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVhtefETKMMEEVAKMEYPGADpDTVRyfkdvyvpSSIdifeAMGQ--TPDDIA 188
Cdd:PRK07231  166 KALAAELGPDKIRVNAVAPVVV----ETGLLEAFMGEPTPENR-AKFL--------ATI----PLGRlgTPEDIA 223
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 8-145 2.92e-16

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: 75.91  E-value: 2.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLA----------RDEQK----------------------------------------RYH- 36
Cdd:cd05364     4 KVAIITGSSSGIGAGTAILFArlgarlaltgRDAERleetrqsclqagvsekkillvvadlteeegqdriisttlaKFGr 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 ----VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQaGHIIVMSSVMGlqGVVFNDV--YTASKFA 110
Cdd:cd05364    84 ldilVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVSSVAG--GRSFPGVlyYCISKAA 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1207168417 111 IEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKM 145
Cdd:cd05364   161 LDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRM 195
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 8-188 6.16e-16

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


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 75.00  E-value: 6.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLARD---------------------------------------------EQKRYH------ 36
Cdd:cd05344     2 KVALVTAASSGIGLAIARALAREgarvaicarnrenleraaselraggagvlavvadltdpedidrlvEKAGDAfgrvdi 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:cd05344    82 lVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIGLV 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEypGADPDTVRYFKDVYVPssidifeaMGQ--TPDDIA 188
Cdd:cd05344   162 KTLSRELAPDGVTVNSVLPGYIDTERVRRLLEARAEKE--GISVEEAEKEVASQIP--------LGRvgKPEELA 226
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 8-151 1.51e-15

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: 74.02  E-value: 1.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR-------------DEQKR--------------YH------------------------ 36
Cdd:cd08940     3 KVALVTGSTSGIGLGIARALAAaganivlngfgdaAEIEAvraglaakhgvkvlYHgadlskpaaiedmvayaqrqfggv 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 ---VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEG 113
Cdd:cd08940    83 dilVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHGVVG 162

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAK 151
Cdd:cd08940   163 LTKVVALETAGTGVTCNAICPGWVLTPLVEKQISALAQ 200
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 8-152 1.53e-15

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: 73.74  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLARD-------------------EQKRYHVNNAGVGL------------------LGPVE- 49
Cdd:cd05333     1 KVALVTGASRGIGRAIALRLAAEgakvavtdrseeaaaetveEIKALGGNAAALEAdvsdreavealvekveaeFGPVDi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  50 -----SISMDE----MKR-----VFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:cd05333    81 lvnnaGITRDNllmrMSEedwdaVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFT 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKM 152
Cdd:cd05333   161 KSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEK 197
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 7-149 3.87e-15

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: 72.96  E-value: 3.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIAVLL----------ARDEQK-------------------------------------RYH--- 36
Cdd:cd08945     3 SEVALVTGATSGIGLAIARRLgkeglrvfvcARGEEGlattvkelreagveadgrtcdvrsvpeiealvaaavaRYGpid 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 --VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPD--MKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIE 112
Cdd:cd08945    83 vlVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVV 162

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1207168417 113 GFCESMAVQLLKFNVKLSLIEPGPVhtefETKMMEEV 149
Cdd:cd08945   163 GFTKALGLELARTGITVNAVCPGFV----ETPMAASV 195
PRK07577 PRK07577
SDR family oxidoreductase;
8-140 5.42e-15

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 72.07  E-value: 5.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLARD--------------------------------------EQKRYH--VNNAGVGLLGP 47
Cdd:PRK07577    4 RTVLVTGATKGIGLALSLRLANLghqvigiarsaiddfpgelfacdladieqtaatlaqinEIHPVDaiVNNVGIALPQP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  48 VESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSvMGLQGVVFNDVYTASKFAIEGFCESMAVQLLKFNV 127
Cdd:PRK07577   84 LGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICS-RAIFGALDRTSYSAAKSALVGCTRTWALELAEYGI 162

                         170
                  ....*....|...
gi 1207168417 128 KLSLIEPGPVHTE 140
Cdd:PRK07577  163 TVNAVAPGPIETE 175
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 8-158 6.11e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 72.76  E-value: 6.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR----------------DEQKRY------------------------------------ 35
Cdd:PRK06701   47 KVALITGGDSGIGRAVAVLFAKegadiaivyldehedaNETKQRvekegvkcllipgdvsdeafckdaveetvrelgrld 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  36 -HVNNAGVGLlgPVES---ISMDEMKRVFETNFFGTVRMIKEVMPDMKkrQAGHIIVMSSVMGLQG-VVFNDvYTASKFA 110
Cdd:PRK06701  127 iLVNNAAFQY--PQQSledITAEQLDKTFKTNIYSYFHMTKAALPHLK--QGSAIINTGSITGYEGnETLID-YSATKGA 201

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207168417 111 IEGFCESMAVQLLKFNVKLSLIEPGPVHTEF--ETKMMEEVAKMeypGAD 158
Cdd:PRK06701  202 IHAFTRSLAQSLVQKGIRVNAVAPGPIWTPLipSDFDEEKVSQF---GSN 248
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 7-189 7.71e-15

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: 71.67  E-value: 7.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIA-VLLARDEQKRYH---------------------------------------------VNNA 40
Cdd:cd05354     3 DKTVLVTGANRGIGKAFVeSLLAHGAKKVYAavrdpgsaahlvakygdkvvplrldvtdpesikaaaaqakdvdvvINNA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  41 GVG-LLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMA 119
Cdd:cd05354    83 GVLkPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSAAYSLTQGLR 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207168417 120 VQLLKFNVKLSLIEPGPVHTEFetkmmeeVAKMEYPGADPDTV-----RYFKDvyvpssiDIFEAMgqtPDDIAK 189
Cdd:cd05354   163 AELAAQGTLVLSVHPGPIDTRM-------AAGAGGPKESPETVaeavlKALKA-------GEFHVF---PDEMAK 220
PRK06398 PRK06398
aldose dehydrogenase; Validated
 8-163 1.40e-14

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 71.40  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA----------VLLARDEQ--------------------------KRYH-----VNNAGVGLLG 46
Cdd:PRK06398    7 KVAIVTGGSQGIGKAVVnrlkeegsnvINFDIKEPsyndvdyfkvdvsnkeqvikgidyviSKYGridilVNNAGIESYG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  47 PVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMAVQ---LL 123
Cdd:PRK06398   87 AIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAVLGLTRSIAVDyapTI 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1207168417 124 KFNVKLsliePGPVhtefETKMMEEVAKMEYpGADPDTVR 163
Cdd:PRK06398  167 RCVAVC----PGSI----RTPLLEWAAELEV-GKDPEHVE 197
PRK07201 PRK07201
SDR family oxidoreductase;
8-132 1.69e-14

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 72.68  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA----------VLLARDEQK------------------------------------------RY 35
Cdd:PRK07201  372 KVVLITGASSGIGRATAikvaeagatvFLVARNGEAldelvaeirakggtahaytcdltdsaavdhtvkdilaehghvDY 451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  36 HVNNAGvgllgpvESI------SMDEM---KRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVmglqGVVFN----D 102
Cdd:PRK07201  452 LVNNAG-------RSIrrsvenSTDRFhdyERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSI----GVQTNaprfS 520

                         170       180       190
                  ....*....|....*....|....*....|
gi 1207168417 103 VYTASKFAIEGFCESMAVQLLKFNVKLSLI 132
Cdd:PRK07201  521 AYVASKAALDAFSDVAASETLSDGITFTTI 550
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 38-161 1.98e-14

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 70.67  E-value: 1.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 NNAGV-GLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK08945   98 HNAGLlGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRANWGAYAVSKFATEGMMQ 177

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHTEfetkmMEEVAkmeYPGADPDT 161
Cdd:PRK08945  178 VLADEYQGTNLRVNCINPGGTRTA-----MRASA---FPGEDPQK 214
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 8-163 1.99e-14

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 70.58  E-value: 1.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLARD---------------EQKRYH----------------------------VNNAGVGL 44
Cdd:cd05368     3 KVALITAAAQGIGRAIALAFAREganviatdineeklkELERGPgittrvldvtdkeqvaalakeegridvlFNCAGFVH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  45 LGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMG-LQGVVFNDVYTASKFAIEGFCESMAVQLL 123
Cdd:cd05368    83 HGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASsIKGVPNRFVYSTTKAAVIGLTKSVAADFA 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1207168417 124 KFNVKLSLIEPGPVhtefETKMMEEVAKMEypgADPDTVR 163
Cdd:cd05368   163 QQGIRCNAICPGTV----DTPSLEERIQAQ---PDPEEAL 195
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 8-188 2.15e-14

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 70.69  E-value: 2.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR-----------DEQKR--------------YH-------------------------- 36
Cdd:PRK12429    5 KVALVTGAASGIGLEIALALAKegakvviadlnDEAAAaaaealqkaggkaiGVamdvtdeeainagidyavetfggvdi 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:PRK12429   85 lVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGLIGLT 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEypGADPDTVRyfKDVYVPSSIDifeamGQ--TPDDIA 188
Cdd:PRK12429  165 KVVALEGATHGVTVNAICPGYVDTPLVRKQIPDLAKER--GISEEEVL--EDVLLPLVPQ-----KRftTVEEIA 230
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 8-140 3.46e-14

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 70.07  E-value: 3.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA----------VLLARDEQKR---------------------------------------YHVN 38
Cdd:PRK06841   16 KVAVVTGGASGIGHAIAelfaakgarvALLDRSEDVAevaaqllggnakglvcdvsdsqsveaavaavisafgridILVN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  39 NAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSS---VMGLQGVVfndVYTASKFAIEGFC 115
Cdd:PRK06841   96 SAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASqagVVALERHV---AYCASKAGVVGMT 172

                         170       180
                  ....*....|....*....|....*
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:PRK06841  173 KVLALEWGPYGITVNAISPTVVLTE 197
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 1-141 4.93e-14

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 69.62  E-value: 4.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   1 MASGGGQKVVLITGCSSGIGLRIAVLLARD---------------------EQKRYH----------------------- 36
Cdd:PRK12939    1 MASNLAGKRALVTGAARGLGAAFAEALAEAgatvafndglaaearelaaalEAAGGRahaiaadladpasvqrffdaaaa 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 --------VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASK 108
Cdd:PRK12939   81 alggldglVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASK 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1207168417 109 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEF 141
Cdd:PRK12939  161 GAVIGMTRSLARELGGRGITVNAIAPGLTATEA 193
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 8-156 6.07e-14

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: 69.63  E-value: 6.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR---------------------------------------DEQ------KRYH------ 36
Cdd:cd05355    27 KKALITGGDSGIGRAVAIAFARegadvainylpeeeddaeetkklieeegrkcllipgdlgDESfcrdlvKEVVkefgkl 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 ---VNNAGVGLLGP-VESISMDEMKRVFETNFFGTVRMIKEVMPDMKKrqAGHIIVMSSVMGLQGVVFNDVYTASKFAIE 112
Cdd:cd05355   107 dilVNNAAYQHPQEsIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKK--GSSIINTTSVTAYKGSPHLLDYAATKGAIV 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1207168417 113 GFCESMAVQLLKFNVKLSLIEPGPVHT-----EFETKMMEEVAK---MEYPG 156
Cdd:cd05355   185 AFTRGLSLQLAEKGIRVNAVAPGPIWTplipsSFPEEKVSEFGSqvpMGRAG 236
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
37-149 6.90e-14

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 69.41  E-value: 6.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK12824   85 VNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGMIGFTK 164

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEV 149
Cdd:PRK12824  165 ALASEGARYGITVNCIAPGYIATPMVEQMGPEV 197
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 8-140 7.02e-14

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 69.14  E-value: 7.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA------------VLLARDEQKRYH-------------------------------VNNAGVGL 44
Cdd:PRK08220    9 KTVWVTGAAQGIGYAVAlafveagakvigFDQAFLTQEDYPfatfvldvsdaaavaqvcqrllaetgpldvlVNAAGILR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  45 LGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSS------VMGLQgvvfndVYTASKFAIEGFCESM 118
Cdd:PRK08220   89 MGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSnaahvpRIGMA------AYGASKAALTSLAKCV 162

                         170       180
                  ....*....|....*....|..
gi 1207168417 119 AVQLLKFNVKLSLIEPGPVHTE 140
Cdd:PRK08220  163 GLELAPYGVRCNVVSPGSTDTD 184
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 37-140 9.08e-14

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 68.67  E-value: 9.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK12828   87 VNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAGVARLTE 166

                          90       100
                  ....*....|....*....|....
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:PRK12828  167 ALAAELLDRGITVNAVLPSIIDTP 190
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 38-145 1.08e-13

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: 68.25  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 NNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCES 117
Cdd:cd08931    82 NNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVRGLTEA 161

                          90       100
                  ....*....|....*....|....*...
gi 1207168417 118 MAVQLLKFNVKLSLIEPGPVHTEFETKM 145
Cdd:cd08931   162 LDVEWARHGIRVADVWPWFVDTPILTKG 189
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 8-151 1.11e-13

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: 68.70  E-value: 1.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLARD----------------------------------------EQKRYHV---------- 37
Cdd:cd05330     4 KVVLITGGGSGLGLATAVRLAKEgaklslvdlneegleaakaalleiapdaevllikadvsdeAQVEAYVdatveqfgri 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 ----NNAGV-GLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIE 112
Cdd:cd05330    84 dgffNNAGIeGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKHGVV 163

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1207168417 113 GFCESMAVQLLKFNVKLSLIEPGPVHtefeTKMMEEVAK 151
Cdd:cd05330   164 GLTRNSAVEYGQYGIRINAIAPGAIL----TPMVEGSLK 198
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
37-162 1.38e-13

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 68.67  E-value: 1.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISmDEMKRV-FETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGlqGVVFND---VYTASKFAIE 112
Cdd:PRK08226   87 VNNAGVCRLGSFLDMS-DEDRDFhIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTG--DMVADPgetAYALTKAAIV 163

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207168417 113 GFCESMAVQLLKFNVKLSLIEPGPVhtefETKMMEEVAKMEYPGaDPDTV 162
Cdd:PRK08226  164 GLTKSLAVEYAQSGIRVNAICPGYV----RTPMAESIARQSNPE-DPESV 208
PRK08219 PRK08219
SDR family oxidoreductase;
8-162 2.80e-13

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 67.27  E-value: 2.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLARD-----------------------------------------EQKRYH--VNNAGVGL 44
Cdd:PRK08219    4 PTALITGASRGIGAAIARELAPThtlllggrpaerldelaaelpgatpfpvdltdpeaiaaaveQLGRLDvlVHNAGVAD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  45 LGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQaGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESmavqlLK 124
Cdd:PRK08219   84 LGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAH-GHVVFINSGAGLRANPGWGSYAASKFALRALADA-----LR 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1207168417 125 F----NVKLSLIEPGPVHTEFETKMMEEvAKMEYPGA---DPDTV 162
Cdd:PRK08219  158 EeepgNVRVTSVHPGRTDTDMQRGLVAQ-EGGEYDPErylRPETV 201
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 8-189 4.40e-13

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 67.23  E-value: 4.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR-------------------------------------DEQ----------KRYH---- 36
Cdd:PRK13394    8 KTAVVTGAASGIGKEIALELARagaavaiadlnqdganavadeinkaggkaigvamdvtNEDavnagidkvaERFGsvdi 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKK-RQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGF 114
Cdd:PRK13394   88 lVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKdDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGL 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168417 115 CESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEypGADPDTVRyfKDVYVPSSIDifeamGQ--TPDDIAK 189
Cdd:PRK13394  168 ARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQIPEQAKEL--GISEEEVV--KKVMLGKTVD-----GVftTVEDVAQ 235
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 8-158 4.58e-13

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


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 66.75  E-value: 4.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR----------------------------------DEQK---------RYH------VN 38
Cdd:cd08944     4 KVAIVTGAGAGIGAACAARLARegarvvvadidggaaqavvaqiaggalalrvdvtDEQQvaalferavEEFggldllVN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  39 NAGVGLLGP-VESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCES 117
Cdd:cd08944    84 NAGAMHLTPaIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNLTRT 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1207168417 118 MAVQLLKFNVKLSLIEPGPVHTEF-ETKMMEEVAKMEYPGAD 158
Cdd:cd08944   164 LAAELRHAGIRCNALAPGLIDTPLlLAKLAGFEGALGPGGFH 205
PRK05650 PRK05650
SDR family oxidoreductase;
37-135 6.53e-13

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 66.99  E-value: 6.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK05650   82 VNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVALSE 161

                          90
                  ....*....|....*....
gi 1207168417 117 SMAVQLLKFNVKLSLIEPG 135
Cdd:PRK05650  162 TLLVELADDEIGVHVVCPS 180
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-209 9.90e-13

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 65.96  E-value: 9.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIG-----------LRIAVLLARDEQKRYH------------------------------------VNNA 40
Cdd:PRK06463    8 KVALITGGTRGIGraiaeaflregAKVAVLYNSAENEAKElrekgvftikcdvgnrdqvkkskevvekefgrvdvlVNNA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  41 GVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGL----QGVVFndvYTASKFAIEGFCE 116
Cdd:PRK06463   88 GIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIgtaaEGTTF---YAITKAGIIILTR 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHTEFET--KMMEEVAKMEYPGADPDTVRYF-KDVYVpSSIDIFEAmgqtPDDIAKCTKK 193
Cdd:PRK06463  165 RLAFELGKYGIRVNAVAPGWVETDMTLsgKSQEEAEKLRELFRNKTVLKTTgKPEDI-ANIVLFLA----SDDARYITGQ 239

                         250
                  ....*....|....*.
gi 1207168417 194 VIETSQPRFRNLTNSL 209
Cdd:PRK06463  240 VIVADGGRIDNLTHSL 255
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 8-153 1.34e-12

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: 65.55  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR--------------------------------------------DEQKRYH------V 37
Cdd:cd05326     5 KVAIITGGASGIGEATARLFAKhgarvviadidddagqavaaelgdpdisfvhcdvtveadvraavDTAVARFgrldimF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 NNAGVglLGP----VESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEG 113
Cdd:cd05326    85 NNAGV--LGApcysILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKHAVLG 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPGPVHTEFETKMM-EEVAKME 153
Cdd:cd05326   163 LTRSAATELGEHGIRVNCVSPYGVATPLLTAGFgVEDEAIE 203
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
7-151 1.71e-12

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 65.52  E-value: 1.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIAVLLARD---------------------------------------------EQKRYH----- 36
Cdd:PRK08643    2 SKVALVTGAGQGIGFAIAKRLVEDgfkvaivdyneetaqaaadklskdggkaiavkadvsdrdqvfaavRQVVDTfgdln 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 --VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKR-QAGHIIVMSSVMGLQGVVFNDVYTASKFAIEG 113
Cdd:PRK08643   82 vvVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLgHGGKIINATSQAGVVGNPELAVYSSTKFAVRG 161

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPGPVhtefETKMMEEVAK 151
Cdd:PRK08643  162 LTQTAARDLASEGITVNAYAPGIV----KTPMMFDIAH 195
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 8-142 1.80e-12

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: 64.93  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA----------VLLARDEQK----------------RYH------------------------- 36
Cdd:cd05356     2 TWAVVTGATDGIGKAYAeelakrgfnvILISRTQEKldavakeieekygvetKTIaadfsagddiyeriekelegldigi 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVGLLGPVESISMD--EMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEG 113
Cdd:cd05356    82 lVNNVGISHSIPEYFLETPedELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLDF 161

                         170       180
                  ....*....|....*....|....*....
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPGPVHTEFE 142
Cdd:cd05356   162 FSRALYEEYKSQGIDVQSLLPYLVATKMS 190
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 8-153 1.84e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 65.12  E-value: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR-----------------------------------------DEQKRYH--VNNAGVGL 44
Cdd:PRK07060   10 KSVLVTGASSGIGRACAVALAQrgarvvaaarnaaaldrlagetgceplrldvgddaairaalAAAGAFDglVNCAGIAS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  45 LGPVESISMDEMKRVFETNFFGTVRMIKEVMPDM-KKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMAVQLL 123
Cdd:PRK07060   90 LESALDMTAEGFDRVMAVNARGAALVARHVARAMiAAGRGGSIVNVSSQAALVGLPDHLAYCASKAALDAITRVLCVELG 169

                         170       180       190
                  ....*....|....*....|....*....|
gi 1207168417 124 KFNVKLSLIEPGPVHTEFETKMMEEVAKME 153
Cdd:PRK07060  170 PHGIRVNSVNPTVTLTPMAAEAWSDPQKSG 199
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 37-161 2.41e-12

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 64.78  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGL-LGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:PRK10538   79 VNNAGLALgLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFS 158

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVH-TEFET---KMMEEVAKMEYPGADPDT 161
Cdd:PRK10538  159 LNLRTDLHGTAVRVTDIEPGLVGgTEFSNvrfKGDDGKAEKTYQNTVALT 208
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 8-163 2.70e-12

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: 64.72  E-value: 2.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLA-------------------------------------------------RDEQKRYH-- 36
Cdd:cd05338     4 KVAFVTGASRGIGRAIALRLAkagatvvvaaktasegdngsakslpgtieetaeeieaaggqalpivvdvRDEDQVRAlv 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -------------VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDV 103
Cdd:cd05338    84 eatvdqfgrldilVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPARGDVA 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 104 YTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMeevakmeYPGADPDTVR 163
Cdd:cd05338   164 YAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIETPAATEL-------SGGSDPARAR 216
PRK07069 PRK07069
short chain dehydrogenase; Validated
 37-152 3.31e-12

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 64.73  E-value: 3.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK07069   84 VNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVASLTK 163

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1207168417 117 SMAVQLLKFNVKlslIEPGPVHTEF-ETKMMEEVAKM 152
Cdd:PRK07069  164 SIALDCARRGLD---VRCNSIHPTFiRTGIVDPIFQR 197
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 7-152 3.61e-12

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 64.38  E-value: 3.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIAVLLARD----------EQKRYH---------------------------------------- 36
Cdd:PRK12937    5 NKVAIVTGASRGIGAAIARRLAADgfavavnyagSAAAADelvaeieaaggraiavqadvadaaavtrlfdaaetafgri 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 ---VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMkkRQAGHIIVMS-SVMGLQGVVFNdVYTASKFAIE 112
Cdd:PRK12937   85 dvlVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLStSVIALPLPGYG-PYAASKAAVE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1207168417 113 GFCESMAVQLLKFNVKLSLIEPGPVHTE--FETKMMEEVAKM 152
Cdd:PRK12937  162 GLVHVLANELRGRGITVNAVAPGPVATElfFNGKSAEQIDQL 203
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 8-135 4.83e-12

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 64.26  E-value: 4.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAV-LLA-------------RDEQKRYH-----------------------------VNNAGVG- 43
Cdd:PRK06171   10 KIIIVTGGSSGIGLAIVKeLLAnganvvnadihggDGQHENYQfvptdvssaeevnhtvaeiiekfgridglVNNAGINi 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  44 --LL----GPVESISMDE--MKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:PRK06171   90 prLLvdekDPAGKYELNEaaFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEGQSCYAATKAALNSFT 169

                         170       180
                  ....*....|....*....|
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPG 135
Cdd:PRK06171  170 RSWAKELGKHNIRVVGVAPG 189
PRK08267 PRK08267
SDR family oxidoreductase;
8-139 4.84e-12

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 64.19  E-value: 4.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR-----------------------DEQKRYHV--------------------------- 37
Cdd:PRK08267    2 KSIFITGAASGIGRATALLFAAegwrvgaydineaglaalaaelgAGNAWTGAldvtdraawdaaladfaaatggrldvl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 -NNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK08267   82 fNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVRGLTE 161

                         170       180
                  ....*....|....*....|...
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHT 139
Cdd:PRK08267  162 ALDLEWRRHGIRVADVMPLFVDT 184
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
37-188 8.05e-12

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 63.51  E-value: 8.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKR-QAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:PRK07067   85 FNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQgRGGKIINMASQAGRRGEALVSHYCATKAAVISYT 164

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHTEfetkMMEEV----AKmeYPGADPDTVRYFKDVYVPssidiFEAMGqTPDDIA 188
Cdd:PRK07067  165 QSAALALIRHGINVNAIAPGVVDTP----MWDQVdalfAR--YENRPPGEKKRLVGEAVP-----LGRMG-VPDDLT 229
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 37-149 1.29e-11

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 62.71  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK12935   89 VNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAGMLGFTK 168

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEV 149
Cdd:PRK12935  169 SLALELAKTNVTVNAICPGFIDTEMVAEVPEEV 201
PRK07454 PRK07454
SDR family oxidoreductase;
7-140 1.55e-11

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 62.67  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIA----------VLLARDEQK-------------------------------------RYH--- 36
Cdd:PRK07454    6 MPRALITGASSGIGKATAlafakagwdlALVARSQDAlealaaelrstgvkaaaysidlsnpeaiapgiaelleQFGcpd 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 --VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQgvVFND--VYTASKFAIE 112
Cdd:PRK07454   86 vlINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARN--AFPQwgAYCVSKAALA 163

                         170       180
                  ....*....|....*....|....*...
gi 1207168417 113 GFCESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:PRK07454  164 AFTKCLAEEERSHGIRVCTITLGAVNTP 191
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 8-154 2.14e-11

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: 62.17  E-value: 2.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLARD-------EQKRYHVNNA-------GVGLLGPVESIS-MDEMKRVFETN--------- 63
Cdd:cd08936    11 KVALVTASTDGIGLAIARRLAQDgahvvvsSRKQQNVDRAvatlqgeGLSVTGTVCHVGkAEDRERLVATAvnlhggvdi 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  64 ---------FFG--------------------TVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGF 114
Cdd:cd08936    91 lvsnaavnpFFGnildsteevwdkildvnvkaTALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNVSKTALLGL 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1207168417 115 CESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEY 154
Cdd:cd08936   171 TKNLAPELAPRNIRVNCLAPGLIKTSFSSALWMDKAVEES 210
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 8-140 2.96e-11

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: 61.55  E-value: 2.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA---------VLLA-RDEQK---------------------------------RYH-----VNN 39
Cdd:cd05370     6 NTVLITGGTSGIGLALArkfleagntVIITgRREERlaeakkelpnihtivldvgdaesvealaeallsEYPnldilINN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  40 AGVGLlgPVE----SISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:cd05370    86 AGIQR--PIDlrdpASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATKAALHSYT 163

                         170       180
                  ....*....|....*....|....*
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:cd05370   164 LALRHQLKDTGVEVVEIVPPAVDTE 188
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 37-139 4.09e-11

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


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 61.33  E-value: 4.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:cd05331    73 VNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSK 152

                          90       100
                  ....*....|....*....|...
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHT 139
Cdd:cd05331   153 CLGLELAPYGVRCNVVSPGSTDT 175
PRK08251 PRK08251
SDR family oxidoreductase;
39-140 5.81e-11

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 61.10  E-value: 5.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  39 NAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFN-DVYTASKFAIEGFCES 117
Cdd:PRK08251   88 NAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRGLPGVkAAYAASKAGVASLGEG 167

                          90       100
                  ....*....|....*....|...
gi 1207168417 118 MAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:PRK08251  168 LRAELAKTPIKVSTIEPGYIRSE 190
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 37-162 7.79e-11

(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: 60.80  E-value: 7.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:cd05353    93 VNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANYSAAKLGLLGLSN 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPvhtefETKMMEEVakMEYPGAD---PDTV 162
Cdd:cd05353   173 TLAIEGAKYNITCNTIAPAA-----GSRMTETV--MPEDLFDalkPEYV 214
PRK06139 PRK06139
SDR family oxidoreductase;
8-139 8.10e-11

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 61.27  E-value: 8.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA----------VLLARDEQKRYHV---------------------------------------- 37
Cdd:PRK06139    8 AVVVITGASSGIGQATAeafarrgarlVLAARDEEALQAVaeecralgaevlvvptdvtdadqvkalatqaasfggridv 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 --NNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:PRK06139   88 wvNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSASKFGLRGFS 167

                         170       180
                  ....*....|....*....|....*
gi 1207168417 116 ESMAVQLLKF-NVKLSLIEPGPVHT 139
Cdd:PRK06139  168 EALRGELADHpDIHVCDVYPAFMDT 192
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 2-146 8.88e-11

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 60.50  E-value: 8.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   2 ASGGGQKVVLITGCSSGIGLRIAVLLARDEQKRYH--VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEV-MPDM 78
Cdd:PRK12827   55 EAAGGKALGLAFDVRDFAATRAALDAGVEEFGRLDilVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAAlPPMI 134

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207168417  79 KKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMM 146
Cdd:PRK12827  135 RARRGGRIVNIASVAGVRGNRGQVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADNAA 202
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 10-155 9.51e-11

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: 60.00  E-value: 9.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  10 VLITGCSSGIGLRIA-VLLARDEQK----------------------RYHV----------------------------- 37
Cdd:cd05325     1 VLITGASRGIGLELVrQLLARGNNTviatcrdpsaatelaalgashsRLHIleldvtdeiaesaeavaerlgdagldvli 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 NNAGV-GLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMG-LQGVVFNDVYT--ASKFAIEG 113
Cdd:cd05325    81 NNAGIlHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGsIGDNTSGGWYSyrASKAALNM 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPGPVhtefETKMMEEVAKMEYP 155
Cdd:cd05325   161 LTKSLAVELKRDGITVVSLHPGWV----RTDMGGPFAKNKGP 198
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 9-188 1.36e-10

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 59.82  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   9 VVLITGCSSGIGLRIAVLLA--------------------RDEQKRYH----------------VNNAGVGLLGPVESis 52
Cdd:cd05328     1 TIVITGAASGIGAATAELLEdaghtvigidlreadviadlSTPEGRAAaiadvlarcsgvldglVNCAGVGGTTVAGL-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  53 mdemkrVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFND---------------------------VYT 105
Cdd:cd05328    79 ------VLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAGWAQDKLelakalaagtearavalaehagqpgylAYA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 106 ASKFAIEGFCESMAVQ-LLKFNVKLSLIEPGPVhtefETKMMEEVAKMEypgadpdtvRYfkdvyvPSSIDIFEA-MGQ- 182
Cdd:cd05328   153 GSKEALTVWTRRRAATwLYGAGVRVNTVAPGPV----ETPILQAFLQDP---------RG------GESVDAFVTpMGRr 213


                  ....*..
gi 1207168417 183 -TPDDIA 188
Cdd:cd05328   214 aEPDEIA 220
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 38-147 1.42e-10

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: 59.90  E-value: 1.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 NNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCES 117
Cdd:cd05361    79 NDYIPRPMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPARAAAVALAES 158

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1207168417 118 MAVQLLKFNVKLSLIEPGPVHTE--FETKMME 147
Cdd:cd05361   159 LAKELSRDNILVYAIGPNFFNSPtyFPTSDWE 190
PRK07024 PRK07024
SDR family oxidoreductase;
10-139 1.75e-10

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 59.56  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  10 VLITGCSSGIGLRIAV----------LLARDEQ------------KRYHV-----------------------------N 38
Cdd:PRK07024    5 VFITGASSGIGQALAReyarqgatlgLVARRTDalqafaarlpkaARVSVyaadvrdadalaaaaadfiaahglpdvviA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  39 NAGVG---LLGPVESIsmDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:PRK07024   85 NAGISvgtLTEEREDL--AVFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIKYL 162

                         170       180
                  ....*....|....*....|....
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHT 139
Cdd:PRK07024  163 ESLRVELRPAGVRVVTIAPGYIRT 186
PRK07102 PRK07102
SDR family oxidoreductase;
52-162 1.92e-10

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 59.55  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  52 SMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMAVQLLKFNVKLSL 131
Cdd:PRK07102   96 DPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSAKAALTAFLSGLRNRLFKSGVHVLT 175

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1207168417 132 IEPGPVhtefETKMMEEvakMEYPG---ADPDTV 162
Cdd:PRK07102  176 VKPGFV----RTPMTAG---LKLPGpltAQPEEV 202
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 37-148 2.39e-10

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 59.16  E-value: 2.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK12936   85 VNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGMIGFSK 164

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHTEFETKMMEE 148
Cdd:PRK12936  165 SLAQEIATRNVTVNCVAPGFIESAMTGKLNDK 196
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 7-140 3.86e-10

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 58.55  E-value: 3.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIAVLLARDEQK---RYH----------------------------------------------- 36
Cdd:cd05358     3 GKVALVTGASSGIGKAIAIRLATAGANvvvNYRskedaaeevveeikavggkaiavqadvskeedvvalfqsaikefgtl 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 ---VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKK-RQAGHIIVMSSVMGLQGVVFNDVYTASKFAIE 112
Cdd:cd05358    83 dilVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKsKIKGKIINMSSVHEKIPWPGHVNYAASKGGVK 162

                         170       180
                  ....*....|....*....|....*...
gi 1207168417 113 GFCESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:cd05358   163 MMTKTLAQEYAPKGIRVNAIAPGAINTP 190
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 8-140 4.05e-10

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


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 58.62  E-value: 4.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR--------------------------------------------DEQKRYH------V 37
Cdd:cd05349     1 QVVLVTGASRGLGAAIARSFARegarvvvnyyrstesaeavaaeageraiaiqadvrdrdqvqamiEEAKNHFgpvdtiV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 NNAgvglLGP----------VESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTAS 107
Cdd:cd05349    81 NNA----LIDfpfdpdqrktFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTA 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1207168417 108 KFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:cd05349   157 KAALLGFTRNMAKELGPYGITVNMVSGGLLKVT 189
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 37-188 4.71e-10

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: 58.17  E-value: 4.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLL-GPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQ---GVVFndvYTASKFAIE 112
Cdd:cd05345    84 VNNAGITHRnKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRprpGLTW---YNASKGWVV 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 113 GFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMeevakmeypgaDPDTvryfkdvyvPSSIDIFEA---MGQ--TPDDI 187
Cdd:cd05345   161 TATKAMAVELAPRNIRVNCLCPVAGETPLLSMFM-----------GEDT---------PENRAKFRAtipLGRlsTPDDI 220


                  .
gi 1207168417 188 A 188
Cdd:cd05345   221 A 221
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
8-140 6.30e-10

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 58.21  E-value: 6.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR----------------------DEQKRYH----------------------------- 36
Cdd:PRK06935   16 KVAIVTGGNTGLGQGYAVALAKagadiiitthgtnwdetrrlieKEGRKVTfvqvdltkpesaekvvkealeefgkidil 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK06935   96 VNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGGKFVPAYTASKHGVAGLTK 175

                         170       180
                  ....*....|....*....|....
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:PRK06935  176 AFANELAAYNIQVNAIAPGYIKTA 199
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 8-145 7.09e-10

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 58.03  E-value: 7.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA----------VLLARD----EQKRYH------------------------------------- 36
Cdd:PRK08213   13 KTALVTGGSRGLGLQIAealgeagarvVLSARKaeelEEAAAHlealgidalwiaadvadeadierlaeetlerfghvdi 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPD-MKKRQAGHIIVMSSVMGLQGvvfND-------VYTAS 107
Cdd:PRK08213   93 lVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRsMIPRGYGRIINVASVAGLGG---NPpevmdtiAYNTS 169

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1207168417 108 KFAIEGFCESMAVQLLKFNVKLSLIEPGpvhtEFETKM 145
Cdd:PRK08213  170 KGAVINFTRALAAEWGPHGIRVNAIAPG----FFPTKM 203
PRK05855 PRK05855
SDR family oxidoreductase;
37-200 7.23e-10

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 58.84  E-value: 7.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKR-QAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:PRK05855  397 VNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERgTGGHIVNVASAAAYAPSRSLPAYATSKAAVLMLS 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHTEFetkmmeeVAKMEYPGADPDTVRYFKDvyvpsSID-IFEAMGQTPDDIAKCTKKV 194
Cdd:PRK05855  477 ECLRAELAAAGIGVTAICPGFVDTNI-------VATTRFAGADAEDEARRRG-----RADkLYQRRGYGPEKVAKAIVDA 544


                  ....*.
gi 1207168417 195 IETSQP 200
Cdd:PRK05855  545 VKRNKA 550
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 8-170 7.87e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 57.75  E-value: 7.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA----------VLLARDEQK----------------RYH-----------------------VN 38
Cdd:PRK06125    8 KRVLITGASKGIGAAAAeafaaegchlHLVARDADAlealaadlraahgvdvAVHaldlsspeareqlaaeagdidilVN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  39 NAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIvmsSVMGLQGVVFNDVY---TASKFAIEGFC 115
Cdd:PRK06125   88 NAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIV---NVIGAAGENPDADYicgSAGNAALMAFT 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKME-------------YPGADPDTVRYFKDVYV 170
Cdd:PRK06125  165 RALGGKSLDDGVRVVGVNPGPVATDRMLTLLKGRARAElgdesrwqellagLPLGRPATPEEVADLVA 232
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 37-140 9.97e-10

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: 57.19  E-value: 9.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVE-SISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:cd05365    81 VNNAGGGGPKPFDmPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNHMT 160

                          90       100
                  ....*....|....*....|....*
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:cd05365   161 RNLAFDLGPKGIRVNAVAPGAVKTD 185
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 9-169 1.06e-09

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: 57.30  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   9 VVLITGCSSGIGLRIA------------VLLARDE-------------------------------------QKRYH--- 36
Cdd:cd05367     1 VIILTGASRGIGRALAeellkrgspsvvVLLARSEeplqelkeelrpglrvttvkadlsdaagveqlleairKLDGErdl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVglLGPV---ESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQA-GHIIVMSSVMGLQGVVFNDVYTASKFAI 111
Cdd:cd05367    81 lINNAGS--LGPVskiEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkKTVVNVSSGAAVNPFKGWGLYCSSKAAR 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207168417 112 EGFCESMAVQLLKFNVkLSlIEPGPVHTEFETKMMEEvakmeypGADPDTVRYFKDVY 169
Cdd:cd05367   159 DMFFRVLAAEEPDVRV-LS-YAPGVVDTDMQREIRET-------SADPETRSRFRSLK 207
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 23-140 1.21e-09

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 57.24  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  23 IAVLLARDEQKRYHVNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKR-QAGHIIVMSSVMGLQGVVFN 101
Cdd:cd05363    68 VAALVDRWGSIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMASQAGRRGEALV 147

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1207168417 102 DVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:cd05363   148 GVYCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGE 186
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 37-161 1.87e-09

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: 56.77  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGL-LGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQaGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:cd08933    92 VNNAGWHPpHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQ-GNIINLSSLVGSIGQKQAAPYVATKGAITAMT 170

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHtefeTKMMEEVAkmeypGADPDT 161
Cdd:cd08933   171 KALAVDESRYGVRVNCISPGNIW----TPLWEELA-----AQTPDT 207
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 7-140 2.19e-09

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


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 56.44  E-value: 2.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIAVLLAR---------------------------------------------------DEQKRY 35
Cdd:cd05369     3 GKVAFITGGGTGIGKAIAKAFAElgasvaiagrkpevleaaaeeissatggrahpiqcdvrdpeaveaavdetlKEFGKI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  36 H--VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPD-MKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIE 112
Cdd:cd05369    83 DilINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRlIEAKHGGSILNISATYAYTGSPFQVHSAAAKAGVD 162

                         170       180
                  ....*....|....*....|....*...
gi 1207168417 113 GFCESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:cd05369   163 ALTRSLAVEWGPYGIRVNAIAPGPIPTT 190
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 37-140 2.28e-09

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: 56.57  E-value: 2.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVmglQGVVFND-----VYTASKFAI 111
Cdd:cd05352    91 IANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASM---SGTIVNRpqpqaAYNASKAAV 167

                          90       100
                  ....*....|....*....|....*....
gi 1207168417 112 EGFCESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:cd05352   168 IHLAKSLAVEWAKYFIRVNSISPGYIDTD 196
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 24-171 2.34e-09

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: 56.53  E-value: 2.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  24 AVLLARDEQKRYH--VNNAGVGLLGPV------ESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQA------GHIIVM 89
Cdd:cd05371    65 ALALAKAKFGRLDivVNCAGIAVAAKTynkkgqQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNEPdqggerGVIINT 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  90 SSVMGLQGVVFNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPvhteFETKMMeevAKMeypgadPDTVRYFKDVY 169
Cdd:cd05371   145 ASVAAFEGQIGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGL----FDTPLL---AGL------PEKVRDFLAKQ 211


                  ..
gi 1207168417 170 VP 171
Cdd:cd05371   212 VP 213
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 8-159 2.37e-09

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: 56.05  E-value: 2.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA----------VLLARDEQKRYHV---------------------------------------- 37
Cdd:cd05340     5 RIILVTGASDGIGREAAltyarygatvILLGRNEEKLRQVadhineeggrqpqwfildlltctsencqqlaqriavnypr 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 -----NNAG-VGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAI 111
Cdd:cd05340    85 ldgvlHNAGlLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVSKFAT 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1207168417 112 EGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMmeevakmeYPGADP 159
Cdd:cd05340   165 EGL*QVLADEYQQRNLRVNCINPGGTRTAMRASA--------FPTEDP 204
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 10-140 2.54e-09

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: 56.21  E-value: 2.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  10 VLITGCSSGIGLRIAVLLARD-------------------------------------------------EQKRYH---- 36
Cdd:cd05359     1 ALVTGGSRGIGKAIALRLAERgadvvinyrkskdaaaevaaeieelggkavvvradvsqpqdveemfaavKERFGRldvl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:cd05359    81 VSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEALVR 160

                         170       180
                  ....*....|....*....|....
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:cd05359   161 YLAVELGPRGIRVNAVSPGVIDTD 184
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 8-139 2.93e-09

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: 55.92  E-value: 2.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA----------VLLARDEQ-------------------------------------KRYH---- 36
Cdd:cd05329     7 KTALVTGGTKGIGYAIVeelaglgaevYTCARNQKeldecltewrekgfkvegsvcdvssrserqelmdtvaSHFGgkln 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 --VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGF 114
Cdd:cd05329    87 ilVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGALNQL 166

                         170       180
                  ....*....|....*....|....*
gi 1207168417 115 CESMAVQLLKFNVKLSLIEPGPVHT 139
Cdd:cd05329   167 TRSLACEWAKDNIRVNAVAPWVIAT 191
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 37-147 3.96e-09

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 55.62  E-value: 3.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVEsISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK06113   93 VNNAGGGGPKPFD-MPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAASHLVR 171

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHT---------EFETKMME 147
Cdd:PRK06113  172 NMAFDLGEKNIRVNGIAPGAILTdalksvitpEIEQKMLQ 211
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 37-135 4.90e-09

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 55.35  E-value: 4.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNA-GVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNdVYTASKFAIEGFC 115
Cdd:PRK07890   87 VNNAfRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMINSMVLRHSQPKYG-AYKMAKGALLAAS 165

                          90       100
                  ....*....|....*....|
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPG 135
Cdd:PRK07890  166 QSLATELGPQGIRVNSVAPG 185
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 37-140 5.56e-09

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


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 55.17  E-value: 5.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFN-DVYTASKFAIEGFC 115
Cdd:cd05351    81 VNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVPGSIVNVSSQASQRALTNhTVYCSTKAALDMLT 160

                          90       100
                  ....*....|....*....|....*
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:cd05351   161 KVMALELGPHKIRVNSVNPTVVMTD 185
PRK07774 PRK07774
SDR family oxidoreductase;
35-140 7.15e-09

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 54.75  E-value: 7.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  35 YHVNNAGV--GL-LGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLqgvVFNDVYTASKFAI 111
Cdd:PRK07774   86 YLVNNAAIygGMkLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAW---LYSNFYGLAKVGL 162

                          90       100
                  ....*....|....*....|....*....
gi 1207168417 112 EGFCESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:PRK07774  163 NGLTQQLARELGGMNIRVNAIAPGPIDTE 191
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 14-151 1.19e-08

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


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 54.41  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  14 GCSSGIGLRIAVLLARDEQKRYHVNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKK-RQAGH---IIVM 89
Cdd:cd08942    64 SSEEGIEALVARVAERSDRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAaATAENparVINI 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207168417  90 SSVMGLQGVVF-NDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPvhteFETKMMEEVAK 151
Cdd:cd08942   144 GSIAGIVVSGLeNYSYGASKAAVHQLTRKLAKELAGEHITVNAIAPGR----FPSKMTAFLLN 202
PRK09072 PRK09072
SDR family oxidoreductase;
7-122 1.64e-08

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 53.79  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIA----------VLLARDEQK------------RYH---------------------------- 36
Cdd:PRK09072    5 DKRVLLTGASGGIGQALAealaaagarlLLVGRNAEKlealaarlpypgRHRwvvadltseagreavlararemgginvl 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK09072   85 INNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFALRGFSE 164


                  ....*.
gi 1207168417 117 SMAVQL 122
Cdd:PRK09072  165 ALRREL 170
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-152 2.05e-08

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 53.57  E-value: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   5 GGQKVVLITGCSSGIGLRIAVLLARDEQKRYH--VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMkkRQ 82
Cdd:PRK06077   55 GGEGIGVLADVSTREGCETLAKATIDRYGVADilVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--RE 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  83 AGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMAVQlLKFNVKLSLIEPGPVhtefETKMMEEVAKM 152
Cdd:PRK06077  133 GGAIVNIASVAGIRPAYGLSIYGAMKAAVINLTKYLALE-LAPKIRVNAIAPGFV----KTKLGESLFKV 197
PRK06484 PRK06484
short chain dehydrogenase; Validated
 37-139 3.02e-08

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 54.08  E-value: 3.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVG-LLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMkkRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:PRK06484  348 VNNAGIAeVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLLALPPRNAYCASKAAVTMLS 425

                          90       100
                  ....*....|....*....|....
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHT 139
Cdd:PRK06484  426 RSLACEWAPAGIRVNTVAPGYIET 449
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 37-162 3.07e-08

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


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 52.77  E-value: 3.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:cd05373    82 VYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRALAQ 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1207168417 117 SMAVQLLKFNVKLS-LIEPGPVHTEFETKMMEEVAKMEYPGA--DPDTV 162
Cdd:cd05373   162 SMARELGPKGIHVAhVIIDGGIDTDFIRERFPKRDERKEEDGilDPDAI 210
PRK12743 PRK12743
SDR family oxidoreductase;
8-156 4.17e-08

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 52.73  E-value: 4.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR-----------DEQ-------------KRYH--------------------------- 36
Cdd:PRK12743    3 QVAIVTASDSGIGKACALLLAQqgfdigitwhsDEEgaketaeevrshgVRAEirqldlsdlpegaqaldkliqrlgrid 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 --VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKR-QAGHIIVMSSVMGLQGVVFNDVYTASKFAIEG 113
Cdd:PRK12743   83 vlVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQgQGGRIINITSVHEHTPLPGASAYTAAKHALGG 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYPG 156
Cdd:PRK12743  163 LTKAMALELVEHGILVNAVAPGAIATPMNGMDDSDVKPDSRPG 205
PRK07775 PRK07775
SDR family oxidoreductase;
37-139 5.61e-08

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 52.45  E-value: 5.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK07775   92 VSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEAMVT 171

                          90       100
                  ....*....|....*....|...
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHT 139
Cdd:PRK07775  172 NLQMELEGTGVRASIVHPGPTLT 194
PRK06124 PRK06124
SDR family oxidoreductase;
37-154 6.44e-08

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 52.02  E-value: 6.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGlQGVVFND-VYTASKFAIEGFC 115
Cdd:PRK06124   93 VNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAG-QVARAGDaVYPAAKQGLTGLM 171

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEY 154
Cdd:PRK06124  172 RALAAEFGPHGITSNAIAPGYFATETNAAMAADPAVGPW 210
PRK05866 PRK05866
SDR family oxidoreductase;
8-127 6.50e-08

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 52.44  E-value: 6.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR-----------------------------------------------DEQKRYH---- 36
Cdd:PRK05866   41 KRILLTGASSGIGEAAAEQFARrgatvvavarredlldavadritraggdamavpcdlsdldavdalvaDVEKRIGgvdi 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVGLLGPVESiSMD---EMKRVFETNFFGTVRMIKEVMPDMKKRQAGHII------VMSSVMGLQGvvfndVYTA 106
Cdd:PRK05866  121 lINNAGRSIRRPLAE-SLDrwhDVERTMVLNYYAPLRLIRGLAPGMLERGDGHIInvatwgVLSEASPLFS-----VYNA 194

                         170       180
                  ....*....|....*....|.
gi 1207168417 107 SKFAIEGFCESMAVQLLKFNV 127
Cdd:PRK05866  195 SKAALSAVSRVIETEWGDRGV 215
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 8-140 7.82e-08

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: 51.84  E-value: 7.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLA----------RDE---------------------------------------QKRYH-- 36
Cdd:cd05327     2 KVVVITGANSGIGKETARELAkrgahviiacRNEekgeeaaaeikketgnakveviqldlsslasvrqfaeefLARFPrl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 ---VNNAGVGLlgPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQG-VVFND---------- 102
Cdd:cd05327    82 dilINNAGIMA--PPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGpIDFNDldlennkeys 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1207168417 103 ---VYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:cd05327   160 pykAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTE 200
PRK08589 PRK08589
SDR family oxidoreductase;
8-139 9.12e-08

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 51.70  E-value: 9.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR-------------------------DEQKRYHV------------------------- 37
Cdd:PRK08589    7 KVAVITGASTGIGQASAIALAQegayvlavdiaeavsetvdkiksngGKAKAYHVdisdeqqvkdfaseikeqfgrvdvl 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 -NNAGV-GLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKrQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFC 115
Cdd:PRK08589   87 fNNAGVdNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMME-QGGSIINTSSFSGQAADLYRSGYNAAKGAVINFT 165

                         170       180
                  ....*....|....*....|....
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHT 139
Cdd:PRK08589  166 KSIAIEYGRDGIRANAIAPGTIET 189
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 58-146 9.50e-08

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: 51.69  E-value: 9.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  58 RVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPV 137
Cdd:cd08935   122 FVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFF 201


                  ....*....
gi 1207168417 138 HTEFETKMM 146
Cdd:cd08935   202 VTPQNRKLL 210
PRK06484 PRK06484
short chain dehydrogenase; Validated
 8-163 1.04e-07

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 52.54  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR----------------------------------DEQKRYH---------------VN 38
Cdd:PRK06484    6 RVVLVTGAAGGIGRAACQRFARagdqvvvadrnverareradslgpdhhalamdvsDEAQIREgfeqlhrefgridvlVN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  39 NAGVglLGPVES----ISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIV-MSSVMGLQGVVFNDVYTASKFAIEG 113
Cdd:PRK06484   86 NAGV--TDPTMTatldTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAAIVnVASGAGLVALPKRTAYSASKAAVIS 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPGPVHTEFetkmmeeVAKMEYPGA-DPDTVR 163
Cdd:PRK06484  164 LTRSLACEWAAKGIRVNAVLPGYVRTQM-------VAELERAGKlDPSAVR 207
PRK06947 PRK06947
SDR family oxidoreductase;
8-140 1.12e-07

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 51.34  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLA-----------RDEQK----------------------------------------RYH 36
Cdd:PRK06947    3 KVVLITGASRGIGRATAVLAAargwsvginyaRDAAAaeetadavraaggracvvagdvaneadviamfdavqsafgRLD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 --VNNAG-VGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGH---IIVMSSVMGLQGVVFNDV-YTASKF 109
Cdd:PRK06947   83 alVNNAGiVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGGRggaIVNVSSIASRLGSPNEYVdYAGSKG 162

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1207168417 110 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:PRK06947  163 AVDTLTLGLAKELGPHGVRVNAVRPGLIETE 193
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 37-155 1.22e-07

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 51.33  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK12859  101 VNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTSGQFQGPMVGELAYAATKGAIDALTS 180

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKMEYP 155
Cdd:PRK12859  181 SLAAEVAHLGITVNAINPGPTDTGWMTEEIKQGLLPMFP 219
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 8-161 1.55e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 51.08  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLARD-----------------------------------EQKRYH---------------- 36
Cdd:PRK07478    7 KVAIITGASSGIGRAAAKLFAREgakvvvgarrqaeldqlvaeiraeggeavalagdvRDEAYAkalvalaverfggldi 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAG-VGLLGPVESISMDEMKRVFETN----FFGTvrmiKEVMPDMKKRQAGHIIVMSSVMG----LQGVVfndVYTA 106
Cdd:PRK07478   87 aFNNAGtLGEMGPVAEMSLEGWRETLATNltsaFLGA----KHQIPAMLARGGGSLIFTSTFVGhtagFPGMA---AYAA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207168417 107 SKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMmeevakmeypGADPDT 161
Cdd:PRK07478  160 SKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAM----------GDTPEA 204
PRK09242 PRK09242
SDR family oxidoreductase;
6-153 2.02e-07

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 50.90  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   6 GQKVvLITGCSSGIGLRIA----------VLLARDEQ---------------KRYH------------------------ 36
Cdd:PRK09242    9 GQTA-LITGASKGIGLAIAreflglgadvLIVARDADalaqardelaeefpeREVHglaadvsddedrraildwvedhwd 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -----VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAI 111
Cdd:PRK09242   88 glhilVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMTKAAL 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1207168417 112 EGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAKME 153
Cdd:PRK09242  168 LQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDYYE 209
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
37-149 2.75e-07

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 50.40  E-value: 2.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK12938   86 VNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAKAGIHGFTM 165

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEV 149
Cdd:PRK12938  166 SLAQEVATKGVTVNTVSPGYIGTDMVKAIRPDV 198
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 8-139 2.96e-07

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 50.45  E-value: 2.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR---------------DEQKRYH------------------------------------ 36
Cdd:PRK07097   11 KIALITGASYGIGFAIAKAYAKagativfndinqelvDKGLAAYrelgieahgyvcdvtdedgvqamvsqiekevgvidi 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVM---GLQGVVfndVYTASKFAIE 112
Cdd:PRK07097   91 lVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMselGRETVS---AYAAAKGGLK 167

                         170       180
                  ....*....|....*....|....*..
gi 1207168417 113 GFCESMAVQLLKFNVKLSLIEPGPVHT 139
Cdd:PRK07097  168 MLTKNIASEYGEANIQCNGIGPGYIAT 194
PRK06949 PRK06949
SDR family oxidoreductase;
8-140 3.55e-07

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 50.15  E-value: 3.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR------------DEQKRYH--------------------------------------- 36
Cdd:PRK06949   10 KVALVTGASSGLGARFAQVLAQagakvvlasrrvERLKELRaeieaeggaahvvsldvtdyqsikaavahaeteagtidi 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQ--------AGHIIVMSSVMGLQGVVFNDVYTAS 107
Cdd:PRK06949   90 lVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAkgagntkpGGRIINIASVAGLRVLPQIGLYCMS 169

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1207168417 108 KFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:PRK06949  170 KAAVVHMTRAMALEWGRHGINVNAICPGYIDTE 202
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 37-135 4.97e-07

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 49.65  E-value: 4.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETN---FFGTVRMIKEVMpdMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEG 113
Cdd:PRK12384   86 VYNAGIAKAAFITDFQLGDFDRSLQVNlvgYFLCAREFSRLM--IRDGIQGRIIQINSKSGKVGSKHNSGYSAAKFGGVG 163

                          90       100
                  ....*....|....*....|..
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPG 135
Cdd:PRK12384  164 LTQSLALDLAEYGITVHSLMLG 185
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
43-158 5.76e-07

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


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 49.32  E-value: 5.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  43 GLLGPVESISMDEMKRV--FETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMAV 120
Cdd:PRK07904   96 GLLGDAEELWQNQRKAVqiAEINYTAAVSVGVLLGEKMRAQGFGQIIAMSSVAGERVRRSNFVYGSTKAGLDGFYLGLGE 175

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1207168417 121 QLLKFNVKLSLIEPGPVHTEFE--------TKMMEEVAKMEYPGAD 158
Cdd:PRK07904  176 ALREYGVRVLVVRPGQVRTRMSahakeaplTVDKEDVAKLAVTAVA 221
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
7-140 1.00e-06

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 48.56  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIAVLLA--------------------------------------RDEQK--------------- 33
Cdd:PRK08063    4 GKVALVTGSSRGIGKAIALRLAeegydiavnyarsrkaaeetaeeiealgrkalavkanvGDVEKikemfaqideefgrl 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  34 RYHVNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSvMGLQGVVFNdvYTA---SKFA 110
Cdd:PRK08063   84 DVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSS-LGSIRYLEN--YTTvgvSKAA 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1207168417 111 IEGFCESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:PRK08063  161 LEALTRYLAVELAPKGIAVNAVSGGAVDTD 190
PRK07074 PRK07074
SDR family oxidoreductase;
37-162 1.04e-06

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 48.61  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQgVVFNDVYTASKFAIEGFCE 116
Cdd:PRK07074   82 VANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGMA-ALGHPAYSAAKAGLIHYTK 160

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHTE-FETKMME-----EVAKMEYP---GADPDTV 162
Cdd:PRK07074  161 LLAVEYGRFGIRANAVAPGTVKTQaWEARVAAnpqvfEELKKWYPlqdFATPDDV 215
PRK06500 PRK06500
SDR family oxidoreductase;
8-139 2.87e-06

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 47.26  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGL-----------RIAV--------LLARDE-----------------QK------RYHVN------- 38
Cdd:PRK06500    7 KTALITGGTSGIGLetarqflaegaRVAItgrdpaslEAARAElgesalviradagdvaaQKalaqalAEAFGrldavfi 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  39 NAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAghIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESM 118
Cdd:PRK06500   87 NAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPAS--IVLNGSINAHIGMPNSSVYAASKAALLSLAKTL 164

                         170       180
                  ....*....|....*....|.
gi 1207168417 119 AVQLLKFNVKLSLIEPGPVHT 139
Cdd:PRK06500  165 SGELLPRGIRVNAVSPGPVQT 185
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 8-166 3.15e-06

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: 47.00  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR--------------------DEQKRYH------------------------------- 36
Cdd:cd08943     2 KVALVTGGASGIGLAIAKRLAAegaavvvadidpeiaekvaeAAQGGPRalgvqcdvtseaqvqsafeqavlefggldiv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMssvMGLQGVVF----NDVYTASKFAIE 112
Cdd:cd08943    82 VSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIGGNIVF---NASKNAVApgpnAAAYSAAKAAEA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207168417 113 GFCESMAVQLLKFNVKLSLIEPGPVhteFET-KMMEEVAKMEYPGADPDTVRYFK 166
Cdd:cd08943   159 HLARCLALEGGEDGIRVNTVNPDAV---FRGsKIWEGVWRAARAKAYGLLEEEYR 210
PRK06114 PRK06114
SDR family oxidoreductase;
5-160 3.19e-06

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 47.08  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   5 GGQKVVLITGCSSGIGLRIAVLLARDEQKRYH--VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQ 82
Cdd:PRK06114   57 GRRAIQIAADVTSKADLRAAVARTEAELGALTlaVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENG 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  83 AGHIIVMSSvmgLQGVVFNDV-----YTASKFAIEGFCESMAVQLLKFNVKLSLIEPG----PVHTEFE----TKMMEEV 149
Cdd:PRK06114  137 GGSIVNIAS---MSGIIVNRGllqahYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGytatPMNTRPEmvhqTKLFEEQ 213

                         170
                  ....*....|.
gi 1207168417 150 AKMEYPgADPD 160
Cdd:PRK06114  214 TPMQRM-AKVD 223
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 37-135 3.96e-06

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: 46.69  E-value: 3.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETN---FFGTVRMIKEVMpdMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEG 113
Cdd:cd05322    85 VYSAGIAKSAKITDFELGDFDRSLQVNlvgYFLCAREFSKLM--IRDGIQGRIIQINSKSGKVGSKHNSGYSAAKFGGVG 162

                          90       100
                  ....*....|....*....|..
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPG 135
Cdd:cd05322   163 LTQSLALDLAEHGITVNSLMLG 184
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 8-139 4.75e-06

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 46.64  E-value: 4.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLARDEQK---RYH------------------------------------------------ 36
Cdd:PRK08936    8 KVVVITGGSTGLGRAMAVRFGKEKAKvviNYRsdeeeandvaeeikkaggeaiavkgdvtvesdvvnliqtavkefgtld 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 --VNNAGVGLLGPVESISMDEMKRVFETN----FFGTVRMIKEVMPDMKKrqaGHIIVMSSVMGLQGVVFNDVYTASKFA 110
Cdd:PRK08936   88 vmINNAGIENAVPSHEMSLEDWNKVINTNltgaFLGSREAIKYFVEHDIK---GNIINMSSVHEQIPWPLFVHYAASKGG 164

                         170       180
                  ....*....|....*....|....*....
gi 1207168417 111 IEGFCESMAVQLLKFNVKLSLIEPGPVHT 139
Cdd:PRK08936  165 VKLMTETLAMEYAPKGIRVNNIGPGAINT 193
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 11-135 5.10e-06

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 46.68  E-value: 5.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  11 LITGCSSGIGLRIAVLLA----------RDEQK-------------RYH-----------------------------VN 38
Cdd:PRK07523   14 LVTGSSQGIGYALAEGLAqagaevilngRDPAKlaaaaeslkgqglSAHalafdvtdhdavraaidafeaeigpidilVN 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  39 NAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSV---MGLQGVVfndVYTASKFAIEGFC 115
Cdd:PRK07523   94 NAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVqsaLARPGIA---PYTATKGAVGNLT 170

                         170       180
                  ....*....|....*....|
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPG 135
Cdd:PRK07523  171 KGMATDWAKHGLQCNAIAPG 190
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
8-140 7.62e-06

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 46.05  E-value: 7.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLAR----------------DEQ-----KRYH-----------------------------V 37
Cdd:PRK12481    9 KVAIITGCNTGLGQGMAIGLAKagadivgvgvaeapetQAQvealgRKFHfitadliqqkdidsivsqavevmghidilI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 NNAGV----GLLGPVESISMDEMKRVFETNFFGTVRMIKEVMpdmKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEG 113
Cdd:PRK12481   89 NNAGIirrqDLLEFGNKDWDDVININQKTVFFLSQAVAKQFV---KQGNGGKIINIASMLSFQGGIRVPSYTASKSAVMG 165

                         170       180
                  ....*....|....*....|....*..
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:PRK12481  166 LTRALATELSQYNINVNAIAPGYMATD 192
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 38-210 8.05e-06

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 46.10  E-value: 8.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 NNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPD-MKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK05876   89 SNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRlLEQGTGGHVVFTASFAGLVPNAGLGAYGVAKYGVVGLAE 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVhtefETKMMEEVAKMEypGADpdtvryfkdvYVPSSIDifEAMGQTP--------DDIA 188
Cdd:PRK05876  169 TLAREVTADGIGVSVLCPMVV----ETNLVANSERIR--GAA----------CAQSSTT--GSPGPLPlqddnlgvDDIA 230

                         170       180
                  ....*....|....*....|..
gi 1207168417 189 KCTKKVIetsqprfrnLTNSLY 210
Cdd:PRK05876  231 QLTADAI---------LANRLY 243
PRK07831 PRK07831
SDR family oxidoreductase;
10-134 1.08e-05

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 45.41  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  10 VLITGCSSGIGlRIAVLlardeqkryhVNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIV- 88
Cdd:PRK07831   86 ALIDAAVERLG-RLDVL----------VNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGGVIVn 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1207168417  89 MSSVMGLQGVVFNDVYTASKFAIEGFCESMAVQLLKFNVKLSLIEP 134
Cdd:PRK07831  155 NASVLGWRAQHGQAHYAAAKAGVMALTRCSALEAAEYGVRINAVAP 200
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 38-139 1.36e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 45.11  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  38 NNAGVGllgPVE--SI---SMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDV-YTASKFAI 111
Cdd:PRK06057   85 NNAGIS---PPEddSIlntGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSATSQIsYTASKGGV 161

                          90       100
                  ....*....|....*....|....*...
gi 1207168417 112 EGFCESMAVQLLKFNVKLSLIEPGPVHT 139
Cdd:PRK06057  162 LAMSRELGVQFARQGIRVNALCPGPVNT 189
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 8-140 1.61e-05

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


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 45.21  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLA----------RDE------------------------------------QKRYH----- 36
Cdd:cd08937     5 KVVVVTGAAQGIGRGVAERLAgegarvllvdRSElvhevlaeilaagdaahvhtadletyagaqgvvraaVERFGrvdvl 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLG-PVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVmGLQGvVFNDVYTASKFAIEGFC 115
Cdd:cd08937    85 INNVGGTIWAkPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSI-ATRG-IYRIPYSAAKGGVNALT 162

                         170       180
                  ....*....|....*....|....*
gi 1207168417 116 ESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:cd08937   163 ASLAFEHARDGIRVNAVAPGGTEAP 187
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 52-135 1.73e-05

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 44.89  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  52 SMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMAVQLLKFNVKLSL 131
Cdd:PRK08277  122 DEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNA 201


                  ....
gi 1207168417 132 IEPG 135
Cdd:PRK08277  202 IAPG 205
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 37-150 1.81e-05

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 44.74  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHII---VMSSVMGLQGVVfndVYTASKFAIEG 113
Cdd:PRK08085   91 INNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIInicSMQSELGRDTIT---PYAASKGAVKM 167

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVA 150
Cdd:PRK08085  168 LTRGMCVELARHNIQVNGIAPGYFKTEMTKALVEDEA 204
PRK12742 PRK12742
SDR family oxidoreductase;
37-140 2.11e-05

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 44.75  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETN----FFGTVRMIKEvMPDmkkrqAGHIIVMSSV----MGLQGVVfndVYTASK 108
Cdd:PRK12742   80 VVNAGIAVFGDALELDADDIDRLFKINihapYHASVEAARQ-MPE-----GGRIIIIGSVngdrMPVAGMA---AYAASK 150

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1207168417 109 FAIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:PRK12742  151 SALQGMARGLARDFGPRGITINVVQPGPIDTD 182
PRK06123 PRK06123
SDR family oxidoreductase;
7-167 2.12e-05

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 44.77  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIAVLLAR--------------------------------------DEQKRYH------------ 36
Cdd:PRK06123    2 RKVMIITGASRGIGAATALLAAErgyavclnylrnrdaaeavvqairrqggealavaadvaDEADVLRlfeavdrelgrl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 ---VNNAGVglLGP---VESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGH---IIVMSSVMGLQGVVFNDV-YTA 106
Cdd:PRK06123   82 dalVNNAGI--LEAqmrLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTRHGGRggaIVNVSSMAARLGSPGEYIdYAA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207168417 107 SKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEfetkmmeevakMEYPGADPDTVRYFKD 167
Cdd:PRK06123  160 SKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTE-----------IHASGGEPGRVDRVKA 209
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 8-147 2.36e-05

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: 44.74  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLA----------RDEQKRYHVNNAGVGLLG----PV--ESISMDEMKRVFE---------- 61
Cdd:cd09763     4 KIALVTGASRGIGRGIALQLGeagatvyitgRTILPQLPGTAEEIEARGgkciPVrcDHSDDDEVEALFErvareqqgrl 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  62 ----TNFFGTVRMIKEVM-------------------------------PDMKKRQAGHIIVMSSVMGLQGVvFNDVYTA 106
Cdd:cd09763    84 dilvNNAYAAVQLILVGVakpfweepptiwddinnvglrahyacsvyaaPLMVKAGKGLIVIISSTGGLEYL-FNVAYGV 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1207168417 107 SKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMME 147
Cdd:cd09763   163 GKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPE 203
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
8-111 2.95e-05

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 44.84  E-value: 2.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA----------VLLARDEQK------------------------------------RYH----- 36
Cdd:PRK08324  423 KVALVTGAAGGIGKATAkrlaaegacvVLADLDEEAaeaaaaelggpdralgvacdvtdeaavqaafeeaalAFGgvdiv 502

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKrqaghiivmssvMGLQGVVfndVYTASKFAI 111
Cdd:PRK08324  503 VSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKA------------QGLGGSI---VFIASKNAV 562
PRK07985 PRK07985
SDR family oxidoreductase;
48-142 3.13e-05

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 44.22  E-value: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  48 VESISMDEMKRVFETNFFGTVRMIKEVMPDMKKrqAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESMAVQLLKFNV 127
Cdd:PRK07985  145 IADLTSEQFQKTFAINVFALFWLTQEAIPLLPK--GASIITTSSIQAYQPSPHLLDYAATKAAILNYSRGLAKQVAEKGI 222

                          90
                  ....*....|....*
gi 1207168417 128 KLSLIEPGPVHTEFE 142
Cdd:PRK07985  223 RVNIVAPGPIWTALQ 237
PRK07035 PRK07035
SDR family oxidoreductase;
8-141 3.44e-05

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 43.85  E-value: 3.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIAVLLA--------------------------------------RDEQ--------KRYH----- 36
Cdd:PRK07035    9 KIALVTGASRGIGEAIAKLLAqqgahvivssrkldgcqavadaivaaggkaealachigEMEQidalfahiRERHgrldi 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVG-LLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGF 114
Cdd:PRK07035   89 lVNNAAANpYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSITKAAVISM 168

                         170       180
                  ....*....|....*....|....*..
gi 1207168417 115 CESMAVQLLKFNVKLSLIEPGPVHTEF 141
Cdd:PRK07035  169 TKAFAKECAPFGIRVNALLPGLTDTKF 195
PRK09730 PRK09730
SDR family oxidoreductase;
37-140 3.69e-05

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 44.07  E-value: 3.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLL-GPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKR---QAGHIIVMSSVMGLQGVVFNDV-YTASKFAI 111
Cdd:PRK09730   84 VNNAGILFTqCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALKhggSGGAIVNVSSAASRLGAPGEYVdYAASKGAI 163

                          90       100
                  ....*....|....*....|....*....
gi 1207168417 112 EGFCESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:PRK09730  164 DTLTTGLSLEVAAQGIRVNCVRPGFIYTE 192
PRK05867 PRK05867
SDR family oxidoreductase;
37-141 4.06e-05

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 43.87  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMglQGVVFN-----DVYTASKFAI 111
Cdd:PRK05867   91 VCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQGGVIINTASM--SGHIINvpqqvSHYCASKAAV 168

                          90       100       110
                  ....*....|....*....|....*....|
gi 1207168417 112 EGFCESMAVQLLKFNVKLSLIEPGPVHTEF 141
Cdd:PRK05867  169 IHLTKAMAVELAPHKIRVNSVSPGYILTEL 198
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 8-114 5.25e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 43.81  E-value: 5.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA----------VLLARDEQK------------RYH----------------------------- 36
Cdd:PRK05872   10 KVVVVTGAARGIGAELArrlhargaklALVDLEEAElaalaaelggddRVLtvvadvtdlaamqaaaeeaverfggidvv 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRqAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGF 114
Cdd:PRK05872   90 VANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIER-RGYVLQVSSLAAFAAAPGMAAYCASKAGVEAF 166
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 40-139 1.08e-04

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: 42.76  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  40 AGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQA-GHIIVMSSVMG---------LQGVVFNDVYTASKF 109
Cdd:cd08941   128 QAEGLLSQGDKATEDGLGEVFQTNVFGHYYLIRELEPLLCRSDGgSQIIWTSSLNAspkyfsledIQHLKGPAPYSSSKY 207

                          90       100       110
                  ....*....|....*....|....*....|
gi 1207168417 110 AIEGFCESMAVQLLKFNVKLSLIEPGPVHT 139
Cdd:cd08941   208 LVDLLSLALNRKFNKLGVYSYVVHPGICTT 237
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 37-137 1.13e-04

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: 42.32  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGV---GLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFND----------V 103
Cdd:cd08930    85 INNAYPspkVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIAPDFRIyentqmyspvE 164

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1207168417 104 YTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPV 137
Cdd:cd08930   165 YSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGI 198
PRK12746 PRK12746
SDR family oxidoreductase;
37-148 1.45e-04

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 42.33  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMkkRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:PRK12746   95 VNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL--RAEGRVINISSAEVRLGFTGSIAYGLSKGALNTMTL 172

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1207168417 117 SMAVQLLKFNVKLSLIEPGPVHTEFETKMMEE 148
Cdd:PRK12746  173 PLAKHLGERGITVNTIMPGYTKTDINAKLLDD 204
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 37-153 1.86e-04

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 41.87  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGV---GLL-----GPVES-ISMDEMKRVFETNFFGTVRMIKEVMPDM-KKRQAGHIIVMSSV-----MGLQGvvfn 101
Cdd:PRK08217   87 INNAGIlrdGLLvkakdGKVTSkMSLEQFQSVIDVNLTGVFLCGREAAAKMiESGSKGVIINISSIaragnMGQTN---- 162

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1207168417 102 dvYTASKFAIEGFCESMAVQLLKFNVKLSLIEPGPVHTEFeTKMM--EEVAKME 153
Cdd:PRK08217  163 --YSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEM-TAAMkpEALERLE 213
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 37-139 2.05e-04

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 41.60  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSvmG-LQGVVFNDV-YTASKFAIEGF 114
Cdd:PRK12748  100 INNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLTS--GqSLGPMPDELaYAATKGAIEAF 177

                          90       100
                  ....*....|....*....|....*
gi 1207168417 115 CESMAVQLLKFNVKLSLIEPGPVHT 139
Cdd:PRK12748  178 TKSLAPELAEKGITVNAVNPGPTDT 202
PRK07062 PRK07062
SDR family oxidoreductase;
7-96 2.32e-04

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 41.57  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIAVLL----------ARDEQK----------RYH------------------------------ 36
Cdd:PRK07062    8 GRVAVVTGGSSGIGLATVELLleagasvaicGRDEERlasaearlreKFPgarllaarcdvldeadvaafaaavearfgg 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207168417  37 ----VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQ 96
Cdd:PRK07062   88 vdmlVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQ 151
PRK08177 PRK08177
SDR family oxidoreductase;
39-140 2.54e-04

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 41.17  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  39 NAGVglLGP----VESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQaGHIIVMSSVMGlqGVVFND-----VYTASKF 109
Cdd:PRK08177   78 NAGI--SGPahqsAADATAAEIGQLFLTNAIAPIRLARRLLGQVRPGQ-GVLAFMSSQLG--SVELPDggempLYKASKA 152

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1207168417 110 AIEGFCESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:PRK08177  153 ALNSMTRSFVAELGEPTLTVLSMHPGWVKTD 183
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-122 2.74e-04

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 41.23  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   7 QKVVLITGCSSGIGLRIAVLLARD-------------------------------------------EQKRYH------- 36
Cdd:PRK08642    5 EQTVLVTGGSRGLGAAIARAFAREgarvvvnyhqsedaaealadelgdraialqadvtdreqvqamfATATEHfgkpitt 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 -VNNAGVGLL------GPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKF 109
Cdd:PRK08642   85 vVNNALADFSfdgdarKKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGTNLFQNPVVPYHDYTTAKA 164

                         170
                  ....*....|...
gi 1207168417 110 AIEGFCESMAVQL 122
Cdd:PRK08642  165 ALLGLTRNLAAEL 177
PRK05599 PRK05599
SDR family oxidoreductase;
43-162 2.84e-04

SDR family oxidoreductase;


Pssm-ID: 235527 [Multi-domain]  Cd Length: 246  Bit Score: 41.41  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  43 GLLGPVESISMDEMKRV--FETNFFGTVRMIKeVMPDMKKRQA--GHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCESM 118
Cdd:PRK05599   86 GILGDQERAETDEAHAVeiATVDYTAQVSMLT-VLADELRAQTapAAIVAFSSIAGWRARRANYVYGSTKAGLDAFCQGL 164

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1207168417 119 AVQLLKFNVKLSLIEPGPVHTEFETKMmeEVAKME-YPGADPDTV 162
Cdd:PRK05599  165 ADSLHGSHVRLIIARPGFVIGSMTTGM--KPAPMSvYPRDVAAAV 207
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 37-157 4.29e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 40.66  E-value: 4.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAG--VGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSS---VMGLQGVVFNdvYTASKFAI 111
Cdd:PRK06523   82 VHVLGgsSAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSiqrRLPLPESTTA--YAAAKAAL 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1207168417 112 EGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMEEVAK---MEYPGA 157
Cdd:PRK06523  160 STYSKSLSKEVAPKGVRVNTVSPGWIETEAAVALAERLAEaagTDYEGA 208
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 37-164 5.00e-04

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


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 40.34  E-value: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEGFCE 116
Cdd:cd05357    83 VNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALEGLTR 162

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207168417 117 SMAVQLLKfNVKLSLIEPG----PVHTEFETKM--MEEVAKMEYPGADP--DTVRY 164
Cdd:cd05357   163 SAALELAP-NIRVNGIAPGlillPEDMDAEYREnaLRKVPLKRRPSAEEiaDAVIF 217
PRK06194 PRK06194
hypothetical protein; Provisional
 27-122 6.00e-04

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 40.38  E-value: 6.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  27 LARDEQKRY---HV--NNAGVGLLGPVESISMDEMKRVFETNFFG--------TVRMIKEVMPDMKKRqaGHIIVMSSVM 93
Cdd:PRK06194   73 LADAALERFgavHLlfNNAGVGAGGLVWENSLADWEWVLGVNLWGvihgvrafTPLMLAAAEKDPAYE--GHIVNTASMA 150

                          90       100
                  ....*....|....*....|....*....
gi 1207168417  94 GLQGVVFNDVYTASKFAIEGFCESMAVQL 122
Cdd:PRK06194  151 GLLAPPAMGIYNVSKHAVVSLTETLYQDL 179
PRK07063 PRK07063
SDR family oxidoreductase;
8-140 9.13e-04

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 39.65  E-value: 9.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417   8 KVVLITGCSSGIGLRIA----------VLLARDEQKRYH----------------------------------------- 36
Cdd:PRK07063    8 KVALVTGAAQGIGAAIArafaregaavALADLDAALAERaaaaiardvagarvlavpadvtdaasvaaavaaaeeafgpl 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 ---VNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFAIEG 113
Cdd:PRK07063   88 dvlVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPVAKHGLLG 167

                         170       180
                  ....*....|....*....|....*..
gi 1207168417 114 FCESMAVQLLKFNVKLSLIEPGPVHTE 140
Cdd:PRK07063  168 LTRALGIEYAARNVRVNAIAPGYIETQ 194
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
37-139 1.03e-03

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 39.47  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  37 VNNAGvgLLGPVESISMDE------MKRVFETNFFGTVRMIKEVMpdmKKRQAGHIIVMSSVMGLQGVVFNDVYTASKFA 110
Cdd:PRK08993   90 VNNAG--LIRREDAIEFSEkdwddvMNLNIKSVFFMSQAAAKHFI---AQGNGGKIINIASMLSFQGGIRVPSYTASKSG 164

                          90       100
                  ....*....|....*....|....*....
gi 1207168417 111 IEGFCESMAVQLLKFNVKLSLIEPGPVHT 139
Cdd:PRK08993  165 VMGVTRLMANEWAKHNINVNAIAPGYMAT 193
PRK07041 PRK07041
SDR family oxidoreductase;
23-157 6.17e-03

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 36.94  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168417  23 IAVLLARDEQKRYHVNNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEvmPDMkkRQAGHIIVMSSVMGLQGVVFND 102
Cdd:PRK07041   60 VDAFFAEAGPFDHVVITAADTPGGPVRALPLAAAQAAMDSKFWGAYRVARA--ARI--APGGSLTFVSGFAAVRPSASGV 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207168417 103 VYTASKFAIEGFCESMAVQLLKfnVKLSLIEPGPVHTEFETKMMEEVAKMEYPGA 157
Cdd:PRK07041  136 LQGAINAALEALARGLALELAP--VRVNTVSPGLVDTPLWSKLAGDAREAMFAAA 188
 
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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